Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 48 (13 Nov 2019)
Sequence version 1 (16 Apr 2014)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Decaprenylphosphoryl-beta-D-ribose oxidase

Gene

dprE1

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Component of the DprE1-DprE2 complex that catalyzes the 2-step epimerization of decaprenyl-phospho-ribose (DPR) to decaprenyl-phospho-arabinose (DPA), a key precursor that serves as the arabinose donor required for the synthesis of cell-wall arabinans (PubMed:16291675, PubMed:19299584). DprE1 catalyzes the first step of epimerization, namely FAD-dependent oxidation of the C2' hydroxyl of DPR to yield the keto intermediate decaprenyl-phospho-2'-keto-D-arabinose (DPX) (PubMed:22733761). The intermediate DPX is then transferred to DprE2 subunit of the epimerase complex, most probably through a 'substrate channel' at the interface of DprE1-DprE2 complex (PubMed:25789990). Can also use farnesyl-phosphoryl-beta-D-ribofuranose (FPR) as substrate in vitro (PubMed:25427196). Appears to be essential for the growth and survival of M.tuberculosis (PubMed:12657046, PubMed:24517327).1 Publication6 Publications
DprE1 is a highly vulnerable and fully validated tuberculosis drug target.3 Publications

Miscellaneous

Was identified as a high-confidence drug target.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Is inhibited by 8-nitro-benzothiazinones (BTZs) such as BTZ043 and PBTZ169; BTZs are a new class of antimycobacterial agents that kill M.tuberculosis in vitro, ex vivo, and in mouse models of tuberculosis (PubMed:20828197, PubMed:19299584, PubMed:22733761, PubMed:24500695). Is also inhibited by dinitrobenzamide derivatives (DNBs), which thus block formation of both cell-wall lipoarabinomannan and arabinogalactan via inhibition of decaprenyl-phospho-arabinose (DPA) synthesis; DNBs show high activity against intracellular growth of M.tuberculosis inside macrophages, including extensively drug resistant (XDR) strains (PubMed:19876393). BTZs and DNBs are suicide inhibitors that act via covalent modification of DprE1; the essential nitro group of these compounds is reduced by DprE1 to a nitroso group, which then specifically reacts with Cys-387 of DprE1 to form an irreversible semimercaptal adduct (PubMed:20828197, PubMed:22733761, PubMed:24500695). Many other compounds with diverse scaffolds were found to act as either covalent (e.g. nitroquinoxalines, nitroimidazoles) or non-covalent (e.g. the benzothiazole derivative TCA1, the 2-carboxyquinoxaline Ty38C, 8-pyrrole-benzothiazinones, 1,4-azaindoles, pyrazolopyridones, 4-aminoquinolone piperidine amides) DprE1 inhibitors (PubMed:23776209, PubMed:25427196, PubMed:25987616, PubMed:24215368, PubMed:24818517, PubMed:27666194).1 Publication10 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 4.1 min(-1) with farnesyl-phosphoryl-beta-D-ribofuranose as substrate (at pH 8 and 30 degrees Celsius).1 Publication

      <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: cell wall polysaccharide biosynthesis

      This protein is involved in the pathway cell wall polysaccharide biosynthesis, which is part of Cell wall biogenesis.2 Publications
      View all proteins of this organism that are known to be involved in the pathway cell wall polysaccharide biosynthesis and in Cell wall biogenesis.

      Sites

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei117FAD; via amide nitrogenCombined sources4 Publications1
      Binding sitei184FAD; via amide nitrogen and carbonyl oxygenCombined sources4 Publications1
      Binding sitei415FADCombined sources4 Publications1

      Regions

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi53 – 63FADCombined sources4 PublicationsAdd BLAST11
      Nucleotide bindingi122 – 125FADCombined sources4 Publications4
      Nucleotide bindingi129 – 132FADCombined sources4 Publications4

      <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

      GO - Biological processi

      <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

      Molecular functionOxidoreductase
      Biological processAntibiotic resistance, Cell wall biogenesis/degradation
      LigandFAD, Flavoprotein

      Enzyme and pathway databases

      BioCyc Collection of Pathway/Genome Databases

      More...
      BioCyci
      MetaCyc:G185E-8086-MONOMER
      MTBH37RV:G185E-8086-MONOMER

      UniPathway: a resource for the exploration and annotation of metabolic pathways

      More...
      UniPathwayi
      UPA00963

      <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
      Recommended name:
      Decaprenylphosphoryl-beta-D-ribose oxidase3 Publications (EC:1.1.98.31 Publication)
      Alternative name(s):
      Decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase1 Publication
      Decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase subunit DprE11 Publication
      Short name:
      Decaprenyl-phosphoribose 2'-epimerase subunit 11 Publication
      Decaprenylphosphoryl-beta-D-ribofuranose 2'-oxidaseCurated
      Decaprenylphosphoryl-beta-D-ribose 2-epimerase flavoprotein subunit1 Publication
      FAD-dependent decaprenylphosphoryl-beta-D-ribofuranose 2-oxidase1 Publication
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
      Name:dprE12 Publications
      Ordered Locus Names:Rv3790
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83332 [NCBI]
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
      • UP000001584 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

      Organism-specific databases

      Mycobacterium tuberculosis strain H37Rv genome database

      More...
      TubercuListi
      Rv3790

      <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

      GO - Cellular componenti

      Keywords - Cellular componenti

      Periplasm

      <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

      <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

      Traditional knockout mutant with dprE1 disruption could not be achieved, suggesting this gene is essential (PubMed:24517327). Conditional knock-down mutant of dprE1 show that down-regulation of DprE1 results in rapid in vitro growth arrest, swelling of the bacteria, cell wall damage, stop of cell division or lysis, decreased survival in macrophages and virulence attenuation (PubMed:24517327). Cells lacking this gene display impaired growth (PubMed:12657046).2 Publications

      Mutagenesis

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi17G → C: Significantly less susceptible to Ty38c inhibition. 34-fold reduction in catalytic activity. 1 Publication1
      Mutagenesisi368L → P: Significantly less susceptible to Ty38c inhibition. 7-fold reduction in catalytic activity. 1 Publication1
      Mutagenesisi387C → A, S or T: Confers resistance to BTZ043 and PBTZ169. Decreases M.tuberculosis cytotoxicity in macrophages. Does not affect binding affinity of the substrate to the enzyme, and only slightly affects catalytic efficiency. Is only partially inhibited by PBTZ169 at high concentrations, while totally inhibited by the non-covalent inhibitor Ty38c. 1 Publication1
      Mutagenesisi387C → G: Confers resistance to BTZ043 and PBTZ169. Loss of covalent modification with BTZ043. Decreases M.tuberculosis cytotoxicity in macrophages. Does not affect binding affinity of the substrate to the enzyme, but reduces catalytic efficiency by 4-fold. Is only partially inhibited by PBTZ169 at high concentrations, while nearly totally inhibited by the non-covalent inhibitor Ty38c. 2 Publications1
      Mutagenesisi387C → N: Confers resistance to BTZ043 and PBTZ169. Decreases M.tuberculosis cytotoxicity in macrophages. Does not affect binding affinity of the substrate to the enzyme, but reduces catalytic efficiency by 4-fold. Is only partially inhibited by PBTZ169 at high concentrations, while totally inhibited by the non-covalent inhibitor Ty38c. 1 Publication1

      Chemistry databases

      ChEMBL database of bioactive drug-like small molecules

      More...
      ChEMBLi
      CHEMBL3804751

      <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

      Molecule processing

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003908911 – 461Decaprenylphosphoryl-beta-D-ribose oxidaseAdd BLAST461

      Proteomic databases

      PaxDb, a database of protein abundance averages across all three domains of life

      More...
      PaxDbi
      P9WJF1

      <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

      <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

      Monomer. Although forming apparent dimer in crystals, DprE1 does not dimerize appreciably in solution (PubMed:22733761).

      Interacts with DprE2 to form an epimerase complex (PubMed:25789990).

      2 Publications

      Protein-protein interaction databases

      STRING: functional protein association networks

      More...
      STRINGi
      83332.Rv3790

      Chemistry databases

      BindingDB database of measured binding affinities

      More...
      BindingDBi
      P9WJF1

      <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

      Secondary structure

      1461
      Legend: HelixTurnBeta strandPDB Structure known for this area
      Show more details

      3D structure databases

      SWISS-MODEL Repository - a database of annotated 3D protein structure models

      More...
      SMRi
      P9WJF1

      Database of comparative protein structure models

      More...
      ModBasei
      Search...

      Protein Data Bank in Europe - Knowledge Base

      More...
      PDBe-KBi
      Search...

      <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

      Domains and Repeats

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini19 – 194FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST176

      <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

      Belongs to the DprE1 family.Curated

      Phylogenomic databases

      evolutionary genealogy of genes: Non-supervised Orthologous Groups

      More...
      eggNOGi
      ENOG4105IQ5 Bacteria
      COG0277 LUCA

      KEGG Orthology (KO)

      More...
      KOi
      K16653

      Identification of Orthologs from Complete Genome Data

      More...
      OMAi
      PRGWFLP

      Database for complete collections of gene phylogenies

      More...
      PhylomeDBi
      P9WJF1

      Family and domain databases

      Gene3D Structural and Functional Annotation of Protein Families

      More...
      Gene3Di
      3.30.465.10, 1 hit

      Integrated resource of protein families, domains and functional sites

      More...
      InterProi
      View protein in InterPro
      IPR007173 ALO
      IPR016166 FAD-bd_PCMH
      IPR036318 FAD-bd_PCMH-like_sf
      IPR016169 FAD-bd_PCMH_sub2
      IPR006094 Oxid_FAD_bind_N

      Pfam protein domain database

      More...
      Pfami
      View protein in Pfam
      PF04030 ALO, 1 hit
      PF01565 FAD_binding_4, 1 hit

      Superfamily database of structural and functional annotation

      More...
      SUPFAMi
      SSF56176 SSF56176, 1 hit

      PROSITE; a protein domain and family database

      More...
      PROSITEi
      View protein in PROSITE
      PS51387 FAD_PCMH, 1 hit

      <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

      <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

      P9WJF1-1 [UniParc]FASTAAdd to basket
      « Hide
              10         20         30         40         50
      MLSVGATTTA TRLTGWGRTA PSVANVLRTP DAEMIVKAVA RVAESGGGRG
      60 70 80 90 100
      AIARGLGRSY GDNAQNGGGL VIDMTPLNTI HSIDADTKLV DIDAGVNLDQ
      110 120 130 140 150
      LMKAALPFGL WVPVLPGTRQ VTVGGAIACD IHGKNHHSAG SFGNHVRSMD
      160 170 180 190 200
      LLTADGEIRH LTPTGEDAEL FWATVGGNGL TGIIMRATIE MTPTSTAYFI
      210 220 230 240 250
      ADGDVTASLD ETIALHSDGS EARYTYSSAW FDAISAPPKL GRAAVSRGRL
      260 270 280 290 300
      ATVEQLPAKL RSEPLKFDAP QLLTLPDVFP NGLANKYTFG PIGELWYRKS
      310 320 330 340 350
      GTYRGKVQNL TQFYHPLDMF GEWNRAYGPA GFLQYQFVIP TEAVDEFKKI
      360 370 380 390 400
      IGVIQASGHY SFLNVFKLFG PRNQAPLSFP IPGWNICVDF PIKDGLGKFV
      410 420 430 440 450
      SELDRRVLEF GGRLYTAKDS RTTAETFHAM YPRVDEWISV RRKVDPLRVF
      460
      ASDMARRLEL L
      Length:461
      Mass (Da):50,163
      Last modified:April 16, 2014 - v1
      <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB9B770002E5FE81C
      GO

      Natural variant

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti17G → C in strain: TRC11; Ty38c-resistant mutant strain lacking Rv3406, but sensitive to moxifloxacin. 1 Publication1
      Natural varianti314Y → C in a spontaneous TCA1-resistant mutant strain, but sensitive to BTZ. 1 Publication1
      Natural varianti368L → P in strain: TRC12; Ty38c-resistant mutant strain lacking Rv3406, but sensitive to moxifloxacin. 1 Publication1
      Natural varianti387C → G in strain: NTB9; BTZ043-resistant. 1 Publication1
      Natural varianti387C → S in strain: NTB1; BTZ043-resistant. 1 Publication1

      Sequence databases

      Select the link destinations:

      EMBL nucleotide sequence database

      More...
      EMBLi

      GenBank nucleotide sequence database

      More...
      GenBanki

      DNA Data Bank of Japan; a nucleotide sequence database

      More...
      DDBJi
      Links Updated
      AL123456 Genomic DNA Translation: CCP46619.1

      Protein sequence database of the Protein Information Resource

      More...
      PIRi
      B70697

      NCBI Reference Sequences

      More...
      RefSeqi
      NP_218307.1, NC_000962.3
      WP_003420630.1, NZ_NVQJ01000009.1

      Genome annotation databases

      Ensembl bacterial and archaeal genome annotation project

      More...
      EnsemblBacteriai
      CCP46619; CCP46619; Rv3790

      Database of genes from NCBI RefSeq genomes

      More...
      GeneIDi
      886125

      KEGG: Kyoto Encyclopedia of Genes and Genomes

      More...
      KEGGi
      mtu:Rv3790
      mtv:RVBD_3790

      <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

      <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      AL123456 Genomic DNA Translation: CCP46619.1
      PIRiB70697
      RefSeqiNP_218307.1, NC_000962.3
      WP_003420630.1, NZ_NVQJ01000009.1

      3D structure databases

      Select the link destinations:

      Protein Data Bank Europe

      More...
      PDBei

      Protein Data Bank RCSB

      More...
      RCSB PDBi

      Protein Data Bank Japan

      More...
      PDBji
      Links Updated
      PDB entryMethodResolution (Å)ChainPositionsPDBsum
      4FDNX-ray2.40A1-461[»]
      4FDOX-ray2.40A1-461[»]
      4FDPX-ray2.23A/B1-461[»]
      4FEHX-ray2.04A1-461[»]
      4FF6X-ray2.60A/B1-461[»]
      4KW5X-ray2.61A/B1-461[»]
      4NCRX-ray1.88A/B1-461[»]
      4P8CX-ray1.95A/B1-461[»]
      4P8HX-ray3.00A/B1-461[»]
      4P8KX-ray2.49A/B1-461[»]
      4P8LX-ray2.02A/B1-461[»]
      4P8MX-ray2.09A/B1-461[»]
      4P8NX-ray1.79A/B1-461[»]
      4P8PX-ray2.20A/B1-461[»]
      4P8TX-ray2.55A/B1-461[»]
      4P8YX-ray2.01A/B1-461[»]
      4PFAX-ray2.56A/B1-461[»]
      4PFDX-ray2.30A/B1-461[»]
      5OEPX-ray2.35A/B1-461[»]
      5OEQX-ray2.25A/B1-461[»]
      6HEZX-ray2.30A/B1-461[»]
      6HF0X-ray2.38A/B1-461[»]
      6HF3X-ray2.20A/B1-461[»]
      6HFVX-ray2.05A/B1-461[»]
      6HFWX-ray2.47A/B1-461[»]
      SMRiP9WJF1
      ModBaseiSearch...
      PDBe-KBiSearch...

      Protein-protein interaction databases

      STRINGi83332.Rv3790

      Chemistry databases

      BindingDBiP9WJF1
      ChEMBLiCHEMBL3804751

      Proteomic databases

      PaxDbiP9WJF1

      Genome annotation databases

      EnsemblBacteriaiCCP46619; CCP46619; Rv3790
      GeneIDi886125
      KEGGimtu:Rv3790
      mtv:RVBD_3790

      Organism-specific databases

      TubercuListiRv3790

      Phylogenomic databases

      eggNOGiENOG4105IQ5 Bacteria
      COG0277 LUCA
      KOiK16653
      OMAiPRGWFLP
      PhylomeDBiP9WJF1

      Enzyme and pathway databases

      UniPathwayiUPA00963
      BioCyciMetaCyc:G185E-8086-MONOMER
      MTBH37RV:G185E-8086-MONOMER

      Family and domain databases

      Gene3Di3.30.465.10, 1 hit
      InterProiView protein in InterPro
      IPR007173 ALO
      IPR016166 FAD-bd_PCMH
      IPR036318 FAD-bd_PCMH-like_sf
      IPR016169 FAD-bd_PCMH_sub2
      IPR006094 Oxid_FAD_bind_N
      PfamiView protein in Pfam
      PF04030 ALO, 1 hit
      PF01565 FAD_binding_4, 1 hit
      SUPFAMiSSF56176 SSF56176, 1 hit
      PROSITEiView protein in PROSITE
      PS51387 FAD_PCMH, 1 hit

      ProtoNet; Automatic hierarchical classification of proteins

      More...
      ProtoNeti
      Search...

      MobiDB: a database of protein disorder and mobility annotations

      More...
      MobiDBi
      Search...

      <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

      <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDPRE1_MYCTU
      <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P9WJF1
      Secondary accession number(s): L0TDT1, P72056, Q7D4V3
      <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
      Last sequence update: April 16, 2014
      Last modified: November 13, 2019
      This is version 48 of the entry and version 1 of the sequence. See complete history.
      <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programProkaryotic Protein Annotation Program

      <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

      Keywords - Technical termi

      3D-structure, Complete proteome, Reference proteome

      Documents

      1. SIMILARITY comments
        Index of protein domains and families
      2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
        Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
      3. PATHWAY comments
        Index of metabolic and biosynthesis pathways
      4. PDB cross-references
        Index of Protein Data Bank (PDB) cross-references
      UniProt is an ELIXIR core data resource
      Main funding by: National Institutes of Health

      We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

      Do not show this banner again