Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8G0G1 (PYRG_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CTP synthase

EC=6.3.4.2
Alternative name(s):
CTP synthetase
UTP--ammonia ligase
Gene names
Name:pyrG
Ordered Locus Names:BR1134, BS1330_I1130
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen By similarity. HAMAP-Rule MF_01227

Catalytic activity

ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate. HAMAP-Rule MF_01227

Enzyme regulation

Allosterically activated by GTP, when glutamine is the substrate. Inhibited by CTP By similarity. HAMAP-Rule MF_01227

Pathway

Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. HAMAP-Rule MF_01227

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01227

Sequence similarities

Belongs to the CTP synthase family.

Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   DomainGlutamine amidotransferase
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_process'de novo' CTP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

glutamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

CTP synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542CTP synthase HAMAP-Rule MF_01227
PRO_0000138168

Regions

Domain291 – 541251Glutamine amidotransferase type-1
Region1 – 252252Aminator domain HAMAP-Rule MF_01227

Sites

Active site3801Nucleophile By similarity
Active site5141 By similarity
Active site5161 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8G0G1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: B88F10406370B7B0

FASTA54260,058
        10         20         30         40         50         60 
MARYVFITGG VVSSLGKGIA AAALAALLQA RGYRVRIRKL DPYLNVDPGT ISPYQHGEVF 

        70         80         90        100        110        120 
VTDDGAETDL DLGHYERFTG RPANQQDNIT TGRIYRNIIE KERRGDYLGA TVQVIPHVTD 

       130        140        150        160        170        180 
EIKNFVLEGN EDYDFVLCEI GGTVGDIEAM PFLEAIRQLG NELPRGTAVY IHLTLMPYIP 

       190        200        210        220        230        240 
AAGELKTKPT QHSVKELRSI GIAPDILLVR ADREIPESER RKLSLFCNVR ESAVIQALDV 

       250        260        270        280        290        300 
ATIYDVPIAY HKEGLDSEVL SAFGIDPAPK PRMDRWEEVS HRLHNPEGEV TIAVVGKYTG 

       310        320        330        340        350        360 
LKDAYKSLIE ALHHGGLANK VKVNLDWIEA QVFESEDPAP YLEKVHGILV PGGFGERGAE 

       370        380        390        400        410        420 
GKILAAKFAR ERKVPYFGIC FGMQMACIEA ARNLVGIEDA SSSEFGPTRE PVVGLMTEWL 

       430        440        450        460        470        480 
KGNMLEKRAA AGDLGGTMRL GAYEAVLKPD SKIAQIYGST DIHERHRHRY EVNIDYKDRL 

       490        500        510        520        530        540 
EAAGLNFAGM SPDGVLPETV EYADHPWFIG VQYHPELKSR PFEPHPLFAS FIEAAIEQSR 


LV 

« Hide

References

[1]"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts."
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. expand/collapse author list , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.
[2]"Revised genome sequence of Brucella suis 1330."
Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.
J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014291 Genomic DNA. Translation: AAN30054.1.
CP002997 Genomic DNA. Translation: AEM18472.1.
RefSeqNP_698139.1. NC_004310.3.
YP_005615964.1. NC_017251.1.

3D structure databases

ProteinModelPortalQ8G0G1.
SMRQ8G0G1. Positions 2-540.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204722.BR1134.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN30054; AAN30054; BR1134.
AEM18472; AEM18472; BS1330_I1130.
GeneID1166810.
12138163.
KEGGbms:BR1134.
bsi:BS1330_I1130.
PATRIC17790601. VBIBruSui107850_1154.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0504.
HOGENOMHOG000077515.
KOK01937.
OMAYEFNNAY.
OrthoDBEOG6RC3NR.
ProtClustDBPRK05380.

Enzyme and pathway databases

UniPathwayUPA00159; UER00277.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_01227. PyrG.
InterProIPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11550. PTHR11550. 1 hit.
PfamPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00337. PyrG. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRG_BRUSU
AccessionPrimary (citable) accession number: Q8G0G1
Secondary accession number(s): G0KA56
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Brucella suis

Brucella suis (strain 1330): entries and gene names