Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

CTP synthase

Gene

pyrG

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.UniRule annotation

Catalytic activityi

ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate.UniRule annotation

Enzyme 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.UniRule annotation

Pathwayi: CTP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes CTP from UDP.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. CTP synthase (pyrG)
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
Binding sitei20Allosteric inhibitor CTP; alternateUniRule annotation1
Binding sitei20UTP; alternateUniRule annotation1
Metal bindingi78MagnesiumUniRule annotation1
Binding sitei78ATPUniRule annotation1
Metal bindingi152MagnesiumUniRule annotation1
Binding sitei235Allosteric inhibitor CTP; alternateUniRule annotation1
Binding sitei235UTP; alternateUniRule annotation1
Binding sitei366L-glutamine; via carbonyl oxygenUniRule annotation1
Active sitei393Nucleophile; for glutamine hydrolysisUniRule annotation1
Binding sitei416L-glutamineUniRule annotation1
Binding sitei477L-glutamine; via amide nitrogenUniRule annotation1
Active sitei524UniRule annotation1
Active sitei526UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi21 – 26ATPUniRule annotation6
Nucleotide bindingi159 – 161Allosteric inhibitor CTPUniRule annotation3
Nucleotide bindingi199 – 204Allosteric inhibitor CTP; alternateUniRule annotation6
Nucleotide bindingi199 – 204UTP; alternateUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00159; UER00277.

Protein family/group databases

MEROPSiC26.964.

Names & Taxonomyi

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 synthetaseUniRule annotation
Short name:
CTPSUniRule annotation
UTP--ammonia ligaseUniRule annotation
Gene namesi
Name:pyrGUniRule annotation
Ordered Locus Names:MMAR_2504
OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)
Taxonomic identifieri216594 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000001190 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001394951 – 583CTP synthaseAdd BLAST583

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi216594.MMAR_2504.

Structurei

3D structure databases

ProteinModelPortaliB2HR69.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini303 – 551Glutamine amidotransferase type-1UniRule annotationAdd BLAST249

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 278Amidoligase domainUniRule annotationAdd BLAST278
Regioni394 – 397L-glutamine bindingUniRule annotation4

Sequence similaritiesi

Belongs to the CTP synthase family.UniRule annotation
Contains 1 glutamine amidotransferase type-1 domain.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4105C8D. Bacteria.
COG0504. LUCA.
HOGENOMiHOG000077515.
KOiK01937.
OMAiTMRLGEY.
OrthoDBiPOG091H02IX.

Family and domain databases

CDDicd01746. GATase1_CTP_Synthase. 1 hit.
Gene3Di3.40.50.300. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_01227. PyrG. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
IPR033828. GATase1_CTP_Synthase.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11550. PTHR11550. 1 hit.
PfamiPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00337. PyrG. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2HR69-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRHPQTATK HLFVSGGVAS SLGKGLTASS LGQLLTARGL RVTMQKLDPY
60 70 80 90 100
LNVDPGTMNP FQHGEVFVTE DGAETDLDVG HYERFLDRDL SGSANVTTGQ
110 120 130 140 150
VYSTVIAKER RGEYLGDTVQ VIPHITDEIK RRIMAMAEPN ADGRRPDVVI
160 170 180 190 200
TEIGGTVGDI ESQPFLEAAR QVRHDLGREN VFFLHVSLVP YLAPSGELKT
210 220 230 240 250
KPTQHSVAAL RSIGITPDAL ILRCDRDVPE ALKNKIALMC DVDIDGIIST
260 270 280 290 300
PDAPSIYDIP KVLHREELDA FVVRRLNLPF RDVDWTEWDD LLRRVHEPKE
310 320 330 340 350
TVRIALVGKY VELSDAYLSV IEAIRAGGFK HRAKVEISWV GSDDCQTDGG
360 370 380 390 400
VASALGDVHG VLIPGGFGIR GIEGKISAIS YARSRGLPVF GLCLGLQCIV
410 420 430 440 450
IEAARSVGLT EANSAEFEPG TPDPVISTMA DQEHIVSGQA DLGGTMRLGA
460 470 480 490 500
YPAVLESGSI VAEAYQSTKV SERHRHRYEV NNAYRDRIAE SGLRFSGTSP
510 520 530 540 550
DGHLVEFVEY PPEQHPFVVG TQAHPELKSR PTRPHPLFAA FVKAAIDYKE
560 570 580
GELLPVEMPE RVSNGAERRD QVGQSIPEPA NRG
Length:583
Mass (Da):63,717
Last modified:June 10, 2008 - v1
Checksum:iBE4F70D2D5951864
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC40955.1.
RefSeqiWP_012394244.1. NC_010612.1.

Genome annotation databases

EnsemblBacteriaiACC40955; ACC40955; MMAR_2504.
KEGGimmi:MMAR_2504.
PATRICi18065973. VBIMycMar75906_2667.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC40955.1.
RefSeqiWP_012394244.1. NC_010612.1.

3D structure databases

ProteinModelPortaliB2HR69.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi216594.MMAR_2504.

Protein family/group databases

MEROPSiC26.964.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACC40955; ACC40955; MMAR_2504.
KEGGimmi:MMAR_2504.
PATRICi18065973. VBIMycMar75906_2667.

Phylogenomic databases

eggNOGiENOG4105C8D. Bacteria.
COG0504. LUCA.
HOGENOMiHOG000077515.
KOiK01937.
OMAiTMRLGEY.
OrthoDBiPOG091H02IX.

Enzyme and pathway databases

UniPathwayiUPA00159; UER00277.

Family and domain databases

CDDicd01746. GATase1_CTP_Synthase. 1 hit.
Gene3Di3.40.50.300. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_01227. PyrG. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
IPR033828. GATase1_CTP_Synthase.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11550. PTHR11550. 1 hit.
PfamiPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00337. PyrG. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPYRG_MYCMM
AccessioniPrimary (citable) accession number: B2HR69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: November 30, 2016
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.