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UniProtKB - P9WJJ3 (NADE_MYCTU)

Entry version 33 (18 Sep 2019)
Sequence version 1 (16 Apr 2014)
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Protein

Glutamine-dependent NAD(+) synthetase

Gene

nadE

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

Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. In vitro, can also use ammonia with comparable specific activity.3 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 <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

The formation of the intermediates complex at the synthetase domain stimulates the glutaminase activity.1 Publication

<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 0.55 sec(-1) for glutamine-dependent activity. kcat is 2.8 sec(-1) for ammonia-dependent activity.1 Publication
  1. KM=1.3 mM for glutamine1 Publication
  2. KM=0.13 mM for deamido-NAD+ (with glutamine as a nitrogen source)1 Publication
  3. KM=0.12 mM for ATP (with glutamine as a nitrogen source)1 Publication
  4. KM=20 mM for ammonia1 Publication
  5. KM=0.7 mM for deamido-NAD+ (with ammonia as a nitrogen source)1 Publication
  6. KM=1.4 mM for ATP (with ammonia as a nitrogen source)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: NAD(+) biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes NAD(+) from deamido-NAD(+) (L-Gln route).UniRule annotation1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Glutamine-dependent NAD(+) synthetase (nadE)
    This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes NAD(+) from deamido-NAD(+) (L-Gln route), the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei52Proton acceptor; for glutaminase activityUniRule annotation2 Publications1
    Active sitei121For glutaminase activityUniRule annotation2 Publications1
    <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 sitei127L-glutamineUniRule annotationCombined sources1
    Active sitei176Nucleophile; for glutaminase activityUniRule annotation2 Publications1
    Binding sitei203L-glutamineUniRule annotationCombined sources1
    Binding sitei209L-glutamineUniRule annotationCombined sources1
    Binding sitei354Deamido-NAD; shared with neighboring subunitCombined sources1
    Binding sitei456Deamido-NADUniRule annotationCombined sources1
    Binding sitei471Deamido-NAD; shared with neighboring subunitCombined sources1
    Binding sitei475Deamido-NAD; via carbonyl oxygen; shared with neighboring subunitCombined sources1
    Binding sitei480ATPUniRule annotationCombined sources1
    Binding sitei485Deamido-NADUniRule annotationCombined sources1
    Binding sitei501Deamido-NAD; shared with neighboring subunitCombined sources1
    Binding sitei635Deamido-NADUniRule annotationCombined sources1
    Binding sitei661Deamido-NAD; via carbonyl oxygenCombined sources1

    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 bindingi366 – 373ATPUniRule annotationCombined sources8
    Nucleotide bindingi490 – 493Deamido-NADUniRule annotationCombined sources4

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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 functionLigase
    LigandATP-binding, NAD, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MTBH37RV:G185E-6669-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		6.3.5.1 3445

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

    More...    UniPathwayi    		UPA00253;UER00334

    <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:
    Glutamine-dependent NAD(+) synthetase2 PublicationsUniRule annotation (EC:6.3.5.1UniRule annotation3 Publications)
    Alternative name(s):
    NAD(+) synthase [glutamine-hydrolyzing]UniRule annotation
    <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:nadEUniRule annotation
    Ordered Locus Names:Rv2438c
    ORF Names:MTCY428.08
    <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 lineageiBacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium 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    		Rv2438c

    <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

    Complete GO annotation on QuickGO ...

    <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

    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>Mutagenesisi52E → A: Lack of glutamine-dependent activity. Retains 30% of ammonia-dependent activity. 1 Publication1
    Mutagenesisi121K → A: Lack of glutamine-dependent and ammonia-dependent activities. 1 Publication1
    Mutagenesisi176C → A: Lack of glutamine-dependent activity. Retains 90% of ammonia-dependent activity. 1 Publication1
    Mutagenesisi656D → A: Causes a decrease in ammonia channel efficiency to 70% compared with wild-type enzyme. 1 Publication1

    <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_00001522411 – 679Glutamine-dependent NAD(+) synthetaseAdd BLAST679

    Proteomic databases

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

    More...    PaxDbi    		P9WJJ3

    <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

    Homooctamer; composed of two stacked homotetramers that form a ring-like structure.

    2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-15763158,EBI-15763158

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...    STRINGi    		83332.Rv2438c

    <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

    1679
    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    		P9WJJ3

    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>Domaini12 – 276CN hydrolasePROSITE-ProRule annotationAdd BLAST265

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni337 – 679LigaseAdd BLAST343

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    An ammonia tunnel 40 Angstroms long allows transfer of ammonia from the glutaminase active site, where it is produced, to the synthetase active site, where it is used for the ATP-dependent formation of NAD+.2 Publications

    <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

    In the C-terminal section; belongs to the NAD synthetase family.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4108DWA Bacteria
    COG0171 LUCA
    COG0388 LUCA

    KEGG Orthology (KO)

    More...    KOi    		K01950

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		RLAQDCY

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P9WJJ3

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd00553 NAD_synthase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		1.10.10.1140, 1 hit
    3.40.50.620, 1 hit
    3.60.110.10, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_02090 NadE_glutamine_dep, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR003010 C-N_Hydrolase
    IPR036526 C-N_Hydrolase_sf
    IPR014445 Gln-dep_NAD_synthase
    IPR041856 NAD+_synth_C
    IPR022310 NAD/GMP_synthase
    IPR003694 NAD_synthase
    IPR014729 Rossmann-like_a/b/a_fold

    The PANTHER Classification System

    More...    PANTHERi    		PTHR23090 PTHR23090, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00795 CN_hydrolase, 1 hit
    PF02540 NAD_synthase, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF006630 NADS_GAT, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF56317 SSF56317, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS50263 CN_HYDROLASE, 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.

    P9WJJ3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNFYSAYQHG FVRVAACTHH TTIGDPAANA ASVLDMARAC HDDGAALAVF 
            60         70         80         90        100
    PELTLSGYSI EDVLLQDSLL DAVEDALLDL VTESADLLPV LVVGAPLRHR 
           110        120        130        140        150
    HRIYNTAVVI HRGAVLGVVP KSYLPTYREF YERRQMAPGD GERGTIRIGG 
           160        170        180        190        200
    ADVAFGTDLL FAASDLPGFV LHVEICEDMF VPMPPSAEAA LAGATVLANL 
           210        220        230        240        250
    SGSPITIGRA EDRRLLARSA SARCLAAYVY AAAGEGESTT DLAWDGQTMI 
           260        270        280        290        300
    WENGALLAES ERFPKGVRRS VADVDTELLR SERLRMGTFD DNRRHHRELT 
           310        320        330        340        350
    ESFRRIDFAL DPPAGDIGLL REVERFPFVP ADPQRLQQDC YEAYNIQVSG 
           360        370        380        390        400
    LEQRLRALDY PKVVIGVSGG LDSTHALIVA THAMDREGRP RSDILAFALP 
           410        420        430        440        450
    GFATGEHTKN NAIKLARALG VTFSEIDIGD TARLMLHTIG HPYSVGEKVY 
           460        470        480        490        500
    DVTFENVQAG LRTDYLFRIA NQRGGIVLGT GDLSELALGW STYGVGDQMS 
           510        520        530        540        550
    HYNVNAGVPK TLIQHLIRWV ISAGEFGEKV GEVLQSVLDT EITPELIPTG 
           560        570        580        590        600
    EEELQSSEAK VGPFALQDFS LFQVLRYGFR PSKIAFLAWH AWNDAERGNW 
           610        620        630        640        650
    PPGFPKSERP SYSLAEIRHW LQIFVQRFYS FSQFKRSALP NGPKVSHGGA 
           660        670 
    LSPRGDWRAP SDMSARIWLD QIDREVPKG
    Length:679
    Mass (Da):74,683
    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:i14AC29CE434A8B0D
    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: CCP45230.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		D70680

    NCBI Reference Sequences

    More...    RefSeqi    		NP_216954.2, NC_000962.3
    WP_003901403.1, NZ_NVQJ01000024.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		CCP45230; CCP45230; Rv2438c

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		885808

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		mtu:Rv2438c
    mtv:RVBD_2438c

    <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: CCP45230.1
    PIRiD70680
    RefSeqiNP_216954.2, NC_000962.3
    WP_003901403.1, NZ_NVQJ01000024.1

    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
    3DLAX-ray2.35A/B/C/D1-679[»]
    3SDBX-ray2.00A1-679[»]
    3SEQX-ray2.73A/B/C/D1-679[»]
    3SEZX-ray2.65A/B/C/D1-679[»]
    3SYTX-ray2.65A/B/C/D1-679[»]
    3SZGX-ray2.25A/B/C/D1-679[»]
    SMRiP9WJJ3
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv2438c

    Proteomic databases

    PaxDbiP9WJJ3

    Genome annotation databases

    EnsemblBacteriaiCCP45230; CCP45230; Rv2438c
    GeneIDi885808
    KEGGimtu:Rv2438c
    mtv:RVBD_2438c

    Organism-specific databases

    TubercuListiRv2438c

    Phylogenomic databases

    eggNOGiENOG4108DWA Bacteria
    COG0171 LUCA
    COG0388 LUCA
    KOiK01950
    OMAiRLAQDCY
    PhylomeDBiP9WJJ3

    Enzyme and pathway databases

    UniPathwayiUPA00253;UER00334
    BioCyciMTBH37RV:G185E-6669-MONOMER
    BRENDAi6.3.5.1 3445

    Family and domain databases

    CDDicd00553 NAD_synthase, 1 hit
    Gene3Di1.10.10.1140, 1 hit
    3.40.50.620, 1 hit
    3.60.110.10, 1 hit
    HAMAPiMF_02090 NadE_glutamine_dep, 1 hit
    InterProiView protein in InterPro
    IPR003010 C-N_Hydrolase
    IPR036526 C-N_Hydrolase_sf
    IPR014445 Gln-dep_NAD_synthase
    IPR041856 NAD+_synth_C
    IPR022310 NAD/GMP_synthase
    IPR003694 NAD_synthase
    IPR014729 Rossmann-like_a/b/a_fold
    PANTHERiPTHR23090 PTHR23090, 1 hit
    PfamiView protein in Pfam
    PF00795 CN_hydrolase, 1 hit
    PF02540 NAD_synthase, 1 hit
    PIRSFiPIRSF006630 NADS_GAT, 1 hit
    SUPFAMiSSF56317 SSF56317, 1 hit
    PROSITEiView protein in PROSITE
    PS50263 CN_HYDROLASE, 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 nameiNADE_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: P9WJJ3
    Secondary accession number(s): L0T9M3, P0A5L6, P71911
    <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: September 18, 2019
    This is version 33 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
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