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Entry version 42 (29 Sep 2021)
Sequence version 1 (16 Apr 2014)
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Protein

CTP synthase

Gene

pyrG

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 amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Is essential for M.tuberculosis growth in vitro and ex vivo (PubMed:26097035).

Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity).

UniRule annotation1 Publication

Miscellaneous

CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor.UniRule annotation

<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

Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition (By similarity). Is inhibited by the EthA-activated metabolites of compounds 7947882 (5-methyl-N-(4-nitrophenyl)thiophene-2-carboxamide) and 7904688 (3-phenyl-N-[(4-piperidin-1-ylphenyl)carbamothioyl]propanamide), that have been shown to have anti-tubercular activity against M.tuberculosis in its replicating, non-replicating, and intracellular states; active metabolites of 7947882 correspond to the S-dioxide and S-monoxide derivatives (PubMed:26097035). One active metabolite was shown to behave as a competitive inhibitor toward the ATP-binding site of PyrG (PubMed:26097035). Direct inhibition of PyrG decreases CTP levels, leading to disruption of the nucleotide metabolic network, characterized by increased levels of several intermediates in the biosynthesis of pyrimidines and purines (PubMed:26097035).UniRule annotation1 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 22.9 sec(-1).1 Publication
  1. KM=0.18 mM for ATP1 Publication
  2. KM=0.14 mM for UTP1 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: CTP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes CTP from UDP.UniRule annotation This subpathway is part of the pathway CTP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CTP from UDP, the pathway CTP biosynthesis via de novo pathway and in Pyrimidine metabolism.

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 sitei20CTP; allosteric inhibitor; alternateBy similarity1 Publication1
Binding sitei20UTP; alternate1 Publication1
Binding sitei46ATP1 Publication1
<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 bindingi78MagnesiumUniRule annotation1
Binding sitei78ATP1 Publication1
Metal bindingi152MagnesiumUniRule annotation1
Binding sitei235CTP; allosteric inhibitor; alternateUniRule annotation1
Binding sitei235UTP; alternateUniRule annotation1
Binding sitei253ATP; via amide nitrogen1 Publication1
Binding sitei366L-glutamine; via carbonyl oxygenUniRule annotation1
<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 sitei393Nucleophile; for glutamine hydrolysisUniRule annotation1 Publication1
Binding sitei416L-glutamineUniRule annotation1
Binding sitei477L-glutamine; via amide nitrogenUniRule annotation1
Active sitei524UniRule annotation1 Publication1
Active sitei526UniRule annotation1 Publication1

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 bindingi21 – 26ATP1 Publication6
Nucleotide bindingi159 – 161CTP; allosteric inhibitorBy similarity1 Publication3
Nucleotide bindingi199 – 204CTP; allosteric inhibitor; alternateUniRule annotation6
Nucleotide bindingi199 – 204UTP; alternateUniRule annotation6

<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 functionLigase
Biological processPyrimidine biosynthesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P9WHK7

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

More...
UniPathwayi
UPA00159;UER00277

<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:
CTP synthaseUniRule annotation (EC:6.3.4.2UniRule annotation)
Alternative name(s):
Cytidine 5'-triphosphate synthaseUniRule annotation
Cytidine triphosphate synthetaseUniRule annotation
Short name:
CTP synthetase1 PublicationUniRule annotation
Short name:
CTPSUniRule annotation
UTP--ammonia ligaseUniRule 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:pyrG
Ordered Locus Names:Rv1699
ORF Names:MTCI125.21
<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
Rv1699

<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

<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>Mutagenesisi186V → G: 14-fold reduction in catalytic activity. 10-fold decrease in affinity for ATP but no change in affinity for UTP. Causes resistance to the anti-tubercular compounds 7947882 and 7904688. Catalytic activity cannot be inhibited by the active metabolite of 7947882. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001382021 – 586CTP synthaseAdd BLAST586

Proteomic databases

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

More...
PaxDbi
P9WHK7

<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

Homotetramer.

UniRule annotation1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
83332.Rv1699

<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

1586
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
P9WHK7

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>Domaini303 – 551Glutamine amidotransferase type-1UniRule annotationAdd BLAST249

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>Regioni1 – 278Amidoligase domainUniRule annotationAdd BLAST278
Regioni394 – 397L-glutamine bindingUniRule annotation4
Regioni560 – 586DisorderedSequence analysisAdd BLAST27

<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 CTP synthase family.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0504, Bacteria

Identification of Orthologs from Complete Genome Data

More...
OMAi
EFNNAYR

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P9WHK7

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03113, CTPS_N, 1 hit
cd01746, GATase1_CTP_Synthase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.300, 1 hit
3.40.50.880, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01227, PyrG, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029062, Class_I_gatase-like
IPR004468, CTP_synthase
IPR017456, CTP_synthase_N
IPR017926, GATASE
IPR033828, GATase1_CTP_Synthase
IPR027417, P-loop_NTPase

The PANTHER Classification System

More...
PANTHERi
PTHR11550, PTHR11550, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06418, CTP_synth_N, 1 hit
PF00117, GATase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52317, SSF52317, 1 hit
SSF52540, SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00337, PyrG, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51273, GATASE_TYPE_1, 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.

P9WHK7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRKHPQTATK HLFVSGGVAS SLGKGLTASS LGQLLTARGL HVTMQKLDPY
60 70 80 90 100
LNVDPGTMNP FQHGEVFVTE DGAETDLDVG HYERFLDRNL PGSANVTTGQ
110 120 130 140 150
VYSTVIAKER RGEYLGDTVQ VIPHITDEIK RRILAMAQPD ADGNRPDVVI
160 170 180 190 200
TEIGGTVGDI ESQPFLEAAR QVRHYLGRED VFFLHVSLVP YLAPSGELKT
210 220 230 240 250
KPTQHSVAAL RSIGITPDAL ILRCDRDVPE ALKNKIALMC DVDIDGVIST
260 270 280 290 300
PDAPSIYDIP KVLHREELDA FVVRRLNLPF RDVDWTEWDD LLRRVHEPHE
310 320 330 340 350
TVRIALVGKY VELSDAYLSV AEALRAGGFK HRAKVEICWV ASDGCETTSG
360 370 380 390 400
AAAALGDVHG VLIPGGFGIR GIEGKIGAIA YARARGLPVL GLCLGLQCIV
410 420 430 440 450
IEAARSVGLT NANSAEFDPD TPDPVIATMP DQEEIVAGEA DLGGTMRLGS
460 470 480 490 500
YPAVLEPDSV VAQAYQTTQV SERHRHRYEV NNAYRDKIAE SGLRFSGTSP
510 520 530 540 550
DGHLVEFVEY PPDRHPFVVG TQAHPELKSR PTRPHPLFVA FVGAAIDYKA
560 570 580
GELLPVEIPE IPEHTPNGSS HRDGVGQPLP EPASRG
Length:586
Mass (Da):63,635
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:iB49F607F9DC47E43
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: CCP44464.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B70503

NCBI Reference Sequences

More...
RefSeqi
NP_216215.1, NC_000962.3
WP_003408396.1, NZ_NVQJ01000010.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
45425668
885048

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv1699

<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: CCP44464.1
PIRiB70503
RefSeqiNP_216215.1, NC_000962.3
WP_003408396.1, NZ_NVQJ01000010.1

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
4ZDIX-ray3.52A/B/C/D/E/F/G/H1-586[»]
4ZDJX-ray1.99A1-586[»]
4ZDKX-ray3.49A/B1-586[»]
SMRiP9WHK7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1699

Proteomic databases

PaxDbiP9WHK7

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
885048

Genome annotation databases

GeneIDi45425668
885048
KEGGimtu:Rv1699

Organism-specific databases

TubercuListiRv1699

Phylogenomic databases

eggNOGiCOG0504, Bacteria
OMAiEFNNAYR
PhylomeDBiP9WHK7

Enzyme and pathway databases

UniPathwayiUPA00159;UER00277
SABIO-RKiP9WHK7

Family and domain databases

CDDicd03113, CTPS_N, 1 hit
cd01746, GATase1_CTP_Synthase, 1 hit
Gene3Di3.40.50.300, 1 hit
3.40.50.880, 1 hit
HAMAPiMF_01227, PyrG, 1 hit
InterProiView protein in InterPro
IPR029062, Class_I_gatase-like
IPR004468, CTP_synthase
IPR017456, CTP_synthase_N
IPR017926, GATASE
IPR033828, GATase1_CTP_Synthase
IPR027417, P-loop_NTPase
PANTHERiPTHR11550, PTHR11550, 1 hit
PfamiView protein in Pfam
PF06418, CTP_synth_N, 1 hit
PF00117, GATase, 1 hit
SUPFAMiSSF52317, SSF52317, 1 hit
SSF52540, SSF52540, 1 hit
TIGRFAMsiTIGR00337, PyrG, 1 hit
PROSITEiView protein in PROSITE
PS51273, GATASE_TYPE_1, 1 hit

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 nameiPYRG_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: P9WHK7
Secondary accession number(s): L0TA54, P0A5U2, P96351
<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 29, 2021
This is version 42 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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