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UniProtKB - P9WPA5 (COAD_MYCTU)

Entry version 36 (07 Oct 2020)
Sequence version 1 (16 Apr 2014)
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Protein

Phosphopantetheine adenylyltransferase

Gene

coaD

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

Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.UniRule annotation2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Mg2+UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Regulated by Coenzyme A (CoA) through feedback inhibition.2 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 288.5 min(-1) for the reverse reaction, with diphosphate and 3'-dephospho-CoA as substrates, which is nearly identical to that of the forward reaction fitted to the Hill equation. The enzyme seems to utilize a nonrapid-equilibrium random bi-bi mechanism with a preferred pathway to the ternary complex. A sigmoidal response is observed when ATP was varied at different fixed concentrations of pantetheine 4'-phosphate. Also exhibits nonhyperbolic kinetics when pantetheine 4'-phosphate was varied at a fixed saturating concentration of ATP.1 Publication
  1. KM=6.7 µM for 3'-dephospho-CoA1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: coenzyme A biosynthesis

    This protein is involved in step 4 of the subpathway that synthesizes CoA from (R)-pantothenate.UniRule annotation
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Type III pantothenate kinase (coaX), Pantothenate kinase (coaA)
    2. Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
    3. Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
    4. Phosphopantetheine adenylyltransferase (coaD)
    5. Dephospho-CoA kinase (coaE)
    This subpathway is part of the pathway coenzyme A 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 CoA from (R)-pantothenate, the pathway coenzyme A biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei9SubstrateUniRule annotationCombined sources1 Publication1
    Binding sitei17ATPUniRule annotationCombined sources1 Publication1 Publication1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei17Transition state stabilizerUniRule annotation1
    Binding sitei41SubstrateUniRule annotation1
    Binding sitei73Substrate; via amide nitrogenUniRule annotationCombined sources1 Publication1
    Binding sitei87SubstrateUniRule annotation1
    Binding sitei98ATPUniRule annotationCombined sources1 Publication1
    Binding sitei105SubstrateCombined sources1 Publication1
    Binding sitei118ATPCombined sources1 Publication1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi9 – 10ATPUniRule annotationCombined sources1 Publication1 Publication2
    Nucleotide bindingi88 – 90ATPUniRule annotationCombined sources1 Publication1 Publication3
    Nucleotide bindingi122 – 128ATPUniRule annotationCombined sources1 Publication1 Publication7

    <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

    • ATP binding Source: UniProtKB-KW
    • pantetheine-phosphate adenylyltransferase activity Source: MTBBASE
    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 functionNucleotidyltransferase, Transferase
    Biological processCoenzyme A biosynthesis
    LigandATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

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

    More...    UniPathwayi    		UPA00241;UER00355

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Phosphopantetheine adenylyltransferase2 PublicationsUniRule annotation (EC:2.7.7.3UniRule annotation2 Publications)
    Alternative name(s):
    Dephospho-CoA pyrophosphorylaseUniRule annotation
    Pantetheine-phosphate adenylyltransferaseUniRule annotation
    Short name:
    PPAT2 PublicationsUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:coaDUniRule annotation
    Synonyms:kdtB1 Publication
    Ordered Locus Names:Rv2965c
    ORF Names:MTCY349.22, u0002e
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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    		Rv2965c

    <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 ...

    Keywords - Cellular componenti

    Cytoplasm

    <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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001562422 – 161Phosphopantetheine adenylyltransferaseAdd BLAST160

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylthreonineCombined sources1

    Keywords - PTMi

    Acetylation

    Proteomic databases

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

    More...    PaxDbi    		P9WPA5

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P9WPA5

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homohexamer; dimer of trimers.

    UniRule annotation1 Publication1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...    STRINGi    		83332.Rv2965c

    <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

    1161
    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    		P9WPA5

    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

    <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 bacterial CoaD family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0669, Bacteria

    KEGG Orthology (KO)

    More...    KOi    		K00954

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		EFQMALM

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P9WPA5

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd02163, PPAT, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.50.620, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_00151, PPAT_bact, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR004821, Cyt_trans-like
    IPR001980, PPAT
    IPR014729, Rossmann-like_a/b/a_fold

    The PANTHER Classification System

    More...    PANTHERi    		PTHR21342:SF1, PTHR21342:SF1, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01467, CTP_transf_like, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR01020, LPSBIOSNTHSS

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR01510, coaD_prev_kdtB, 1 hit
    TIGR00125, cyt_tran_rel, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P9WPA5-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTGAVCPGSF DPVTLGHVDI FERAAAQFDE VVVAILVNPA KTGMFDLDER 
            60         70         80         90        100
    IAMVKESTTH LPNLRVQVGH GLVVDFVRSC GMTAIVKGLR TGTDFEYELQ 
           110        120        130        140        150
    MAQMNKHIAG VDTFFVATAP RYSFVSSSLA KEVAMLGGDV SELLPEPVNR 
           160 
    RLRDRLNTER T
    Length:161
    Mass (Da):17,628
    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:iDE9F12E18D0C1721
    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
    		U00024 Genomic DNA Translation: AAA50946.1
    AL123456 Genomic DNA Translation: CCP45769.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		B70671

    NCBI Reference Sequences

    More...    RefSeqi    		NP_217481.1, NC_000962.3
    WP_003414998.1, NZ_NVQJ01000015.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		CCP45769; CCP45769; Rv2965c

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		23490791
    888423

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		mtu:Rv2965c
    mtv:RVBD_2965c

    <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
    		U00024 Genomic DNA Translation: AAA50946.1
    AL123456 Genomic DNA Translation: CCP45769.1
    PIRiB70671
    RefSeqiNP_217481.1, NC_000962.3
    WP_003414998.1, NZ_NVQJ01000015.1

    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
    1TFUX-ray1.99A1-157[»]
    3LCJX-ray2.10A1-161[»]
    3NBAX-ray2.68A/B/C/D1-157[»]
    3NBKX-ray1.58A/B/C/D1-157[»]
    3PNBX-ray2.11A/B/C/D1-157[»]
    3RBAX-ray1.59A1-157[»]
    3RFFX-ray1.76A1-157[»]
    3RHSX-ray1.59A1-157[»]
    3UC5X-ray1.70A1-157[»]
    4E1AX-ray1.62A1-161[»]
    4R0NX-ray2.00A/C/E/G/I/K2-157[»]
    6G6VX-ray1.94A1-161[»]
    6G7SX-ray1.77A1-161[»]
    6G7TX-ray1.65A1-161[»]
    6G7UX-ray1.84A1-161[»]
    6G7VX-ray1.78A1-161[»]
    6QMFX-ray1.77A1-161[»]
    6QMGX-ray1.65A1-161[»]
    6QMIX-ray1.78A1-161[»]
    SMRiP9WPA5
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv2965c

    PTM databases

    iPTMnetiP9WPA5

    Proteomic databases

    PaxDbiP9WPA5

    Genome annotation databases

    EnsemblBacteriaiCCP45769; CCP45769; Rv2965c
    GeneIDi23490791
    888423
    KEGGimtu:Rv2965c
    mtv:RVBD_2965c

    Organism-specific databases

    TubercuListiRv2965c

    Phylogenomic databases

    eggNOGiCOG0669, Bacteria
    KOiK00954
    OMAiEFQMALM
    PhylomeDBiP9WPA5

    Enzyme and pathway databases

    UniPathwayiUPA00241;UER00355

    Family and domain databases

    CDDicd02163, PPAT, 1 hit
    Gene3Di3.40.50.620, 1 hit
    HAMAPiMF_00151, PPAT_bact, 1 hit
    InterProiView protein in InterPro
    IPR004821, Cyt_trans-like
    IPR001980, PPAT
    IPR014729, Rossmann-like_a/b/a_fold
    PANTHERiPTHR21342:SF1, PTHR21342:SF1, 1 hit
    PfamiView protein in Pfam
    PF01467, CTP_transf_like, 1 hit
    PRINTSiPR01020, LPSBIOSNTHSS
    TIGRFAMsiTIGR01510, coaD_prev_kdtB, 1 hit
    TIGR00125, cyt_tran_rel, 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 nameiCOAD_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: P9WPA5
    Secondary accession number(s): L0TCR8
    , O08023, P0A530, Q50452
    <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%5Fand%5Fisoforms">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 7, 2020
    This is version 36 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, 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
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families
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