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Entry version 35 (16 Oct 2019)
Sequence version 1 (16 Apr 2014)
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Protein

3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component

Gene

hmp

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

Involved in the degradation of cholesterol. Catalyzes the introduction of a 9a-hydroxyl moiety into 1,4-androstadiene-3,17-dione (ADD) to yield the 9alpha-hydroxy-1,4-androstadiene-3,17-dione (9OHADD) intermediate which spontaneously form 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione (HSA) via the meta-cleavage of ring B with concomitant aromatization of ring A. KSH is also able to use 4-androstene-3,17-dione (AD), 3-oxo-23,24-bisnorcholesta-4-en-22-oate (4-BNC), 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate (1,4-BNC), 3-oxo-23,24-bisnorcholesta-4-en-22-oyl-coenzyme A thioester (4-BNC-CoA) and 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-coenzyme A thioester (1,4-BNC-CoA) as substrates.2 Publications

<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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<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 2.7 sec(-1) for 1,4-BNC-CoA as substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574). Kcat is 0.8 sec(-1) for ADD as substrate (at pH 7 and at 25 degrees Celsius) (PubMed:19234303). Kcat is 0.61 sec(-1) for 4-BNC-CoA as substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574). Kcat is 0.25 sec(-1) for 1,4-BNC as substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574). Kcat is 0.08 sec(-1) for 4-BNC as substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574). Kcat is 0.07 sec(-1) for AD as substrate (at pH 7 and at 25 degrees Celsius) (PubMed:19234303).2 Publications
  1. KM=3 µM for 4-BNC (at pH 7 and at 22 degrees Celsius)1 Publication
  2. KM=6.8 µM for 4-BNC-CoA (at pH 7 and at 22 degrees Celsius)1 Publication
  3. KM=17 µM for 1,4-BNC-CoA (at pH 7 and at 22 degrees Celsius)1 Publication
  4. KM=24 µM for AD (at pH 7 and at 25 degrees Celsius)1 Publication
  5. KM=70 µM for 1,4-BNC (at pH 7 and at 22 degrees Celsius)1 Publication
  6. KM=110 µM for ADD (at pH 7 and at 25 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: steroid biosynthesis

    This protein is involved in the pathway steroid biosynthesis, which is part of Lipid metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway steroid biosynthesis and in Lipid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi305Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
    Metal bindingi310Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
    Metal bindingi313Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
    Metal bindingi343Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1

    <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 processCholesterol metabolism, Lipid degradation, Lipid metabolism, Steroid metabolism, Sterol metabolism, Virulence
    Ligand2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:G185E-7849-MONOMER
    MTBH37RV:G185E-7849-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.14.13.142 3445

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

    More...
    UniPathwayi
    UPA00062

    <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:
    3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component1 Publication
    Alternative name(s):
    3-ketosteroid-9-alpha-hydroxylase, ferredoxin reductase component1 Publication
    Short name:
    KSH1 Publication
    Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase1 Publication (EC:1.14.15.302 Publications)
    Rieske-type oxygenase1 Publication
    Short name:
    RO1 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:hmp
    Synonyms:kshB
    Ordered Locus Names:Rv3571
    <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
    Rv3571

    <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_00004041001 – 3583-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase componentAdd BLAST358

    Proteomic databases

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

    More...
    PaxDbi
    P9WJ93

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Induced by KstR.1 Publication

    <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. The two-component system 3-ketosteroid-9-alpha-monooxygenase is composed of an oxygenase component KshA and a reductase component KshB.

    1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    83332.Rv3571

    <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

    3D structure databases

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

    More...
    SMRi
    P9WJ93

    Database of comparative protein structure models

    More...
    ModBasei
    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>Domaini12 – 124FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST113
    Domaini269 – 3582Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST90

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CJJ Bacteria
    COG1018 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K15983

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    ILACQSH

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P9WJ93

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00207 fer2, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.10.20.30, 1 hit
    3.40.50.80, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR036010 2Fe-2S_ferredoxin-like_sf
    IPR001041 2Fe-2S_ferredoxin-type
    IPR006058 2Fe2S_fd_BS
    IPR012675 Beta-grasp_dom_sf
    IPR008333 Cbr1-like_FAD-bd_dom
    IPR017927 FAD-bd_FR_type
    IPR001709 Flavoprot_Pyr_Nucl_cyt_Rdtase
    IPR039261 FNR_nucleotide-bd
    IPR001433 OxRdtase_FAD/NAD-bd
    IPR017938 Riboflavin_synthase-like_b-brl

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00970 FAD_binding_6, 1 hit
    PF00111 Fer2, 1 hit
    PF00175 NAD_binding_1, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00371 FPNCR

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52343 SSF52343, 1 hit
    SSF54292 SSF54292, 1 hit
    SSF63380 SSF63380, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00197 2FE2S_FER_1, 1 hit
    PS51085 2FE2S_FER_2, 1 hit
    PS51384 FAD_FR, 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.

    P9WJ93-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTEAIGDEPL GDHVLELQIA EVVDETDEAR SLVFAVPDGS DDPEIPPRRL
    60 70 80 90 100
    RYAPGQFLTL RVPSERTGSV ARCYSLCSSP YTDDALAVTV KRTADGYASN
    110 120 130 140 150
    WLCDHAQVGM RIHVLAPSGN FVPTTLDADF LLLAAGSGIT PIMSICKSAL
    160 170 180 190 200
    AEGGGQVTLL YANRDDRSVI FGDALRELAA KYPDRLTVLH WLESLQGLPS
    210 220 230 240 250
    ASALAKLVAP YTDRPVFICG PGPFMQAARD ALAALKVPAQ QVHIEVFKSL
    260 270 280 290 300
    ESDPFAAVKV DDSGDEAPAT AVVELDGQTH TVSWPRTAKL LDVLLAAGLD
    310 320 330 340 350
    APFSCREGHC GACACTLRAG KVNMGVNDVL EQQDLDEGLI LACQSRPESD

    SVEVTYDE
    Length:358
    Mass (Da):38,265
    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:i182A799D00ADC8B2
    GO

    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: CCP46394.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A70606

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_218088.1, NC_000962.3
    WP_003900102.1, NZ_NVQJ01000014.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CCP46394; CCP46394; Rv3571

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    887315

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mtu:Rv3571
    mtv:RVBD_3571

    <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: CCP46394.1
    PIRiA70606
    RefSeqiNP_218088.1, NC_000962.3
    WP_003900102.1, NZ_NVQJ01000014.1

    3D structure databases

    SMRiP9WJ93
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv3571

    Proteomic databases

    PaxDbiP9WJ93

    Genome annotation databases

    EnsemblBacteriaiCCP46394; CCP46394; Rv3571
    GeneIDi887315
    KEGGimtu:Rv3571
    mtv:RVBD_3571

    Organism-specific databases

    TubercuListiRv3571

    Phylogenomic databases

    eggNOGiENOG4105CJJ Bacteria
    COG1018 LUCA
    KOiK15983
    OMAiILACQSH
    PhylomeDBiP9WJ93

    Enzyme and pathway databases

    UniPathwayiUPA00062
    BioCyciMetaCyc:G185E-7849-MONOMER
    MTBH37RV:G185E-7849-MONOMER
    BRENDAi1.14.13.142 3445

    Family and domain databases

    CDDicd00207 fer2, 1 hit
    Gene3Di3.10.20.30, 1 hit
    3.40.50.80, 1 hit
    InterProiView protein in InterPro
    IPR036010 2Fe-2S_ferredoxin-like_sf
    IPR001041 2Fe-2S_ferredoxin-type
    IPR006058 2Fe2S_fd_BS
    IPR012675 Beta-grasp_dom_sf
    IPR008333 Cbr1-like_FAD-bd_dom
    IPR017927 FAD-bd_FR_type
    IPR001709 Flavoprot_Pyr_Nucl_cyt_Rdtase
    IPR039261 FNR_nucleotide-bd
    IPR001433 OxRdtase_FAD/NAD-bd
    IPR017938 Riboflavin_synthase-like_b-brl
    PfamiView protein in Pfam
    PF00970 FAD_binding_6, 1 hit
    PF00111 Fer2, 1 hit
    PF00175 NAD_binding_1, 1 hit
    PRINTSiPR00371 FPNCR
    SUPFAMiSSF52343 SSF52343, 1 hit
    SSF54292 SSF54292, 1 hit
    SSF63380 SSF63380, 1 hit
    PROSITEiView protein in PROSITE
    PS00197 2FE2S_FER_1, 1 hit
    PS51085 2FE2S_FER_2, 1 hit
    PS51384 FAD_FR, 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 nameiKSHB_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: P9WJ93
    Secondary accession number(s): L0TD71, P96853, Q7D594
    <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: October 16, 2019
    This is version 35 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

    Complete proteome, Reference proteome

    Documents

    1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    UniProt is an ELIXIR core data resource
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