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C4KYX1 (C4KYX1_EXISA) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
CTP synthase HAMAP-Rule MF_01227
EC=6.3.4.2 HAMAP-Rule MF_01227
Alternative name(s):
CTP synthetase HAMAP-Rule MF_01227
UTP--ammonia ligase HAMAP-Rule MF_01227
Gene names
Name:pyrG HAMAP-Rule MF_01227
Ordered Locus Names:EAT1b_1357
OrganismExiguobacterium sp. (strain ATCC BAA-1283 / AT1b) [Complete proteome] [HAMAP] EMBL ACQ70284.1
Taxonomic identifier360911 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillales Family XII. Incertae Sedis › Exiguobacterium

Protein attributes

Sequence length531 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 SAAS SAAS004468

Catalytic activity

ATP + UTP + NH3 = ADP + phosphate + CTP. HAMAP-Rule MF_01227 SAAS SAAS004468

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 SAAS SAAS004468

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01227

Sequence similarities

Belongs to the CTP synthase family. HAMAP-Rule MF_01227

Contains 1 glutamine amidotransferase type-1 domain. HAMAP-Rule MF_01227 SAAS SAAS004468

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain292 – 531240Glutamine amidotransferase type-1 By similarity HAMAP-Rule MF_01227
Region1 – 254254Aminator domain By similarity HAMAP-Rule MF_01227

Sites

Active site3811Nucleophile By similarity HAMAP-Rule MF_01227
Active site5071 By similarity HAMAP-Rule MF_01227
Active site5091 By similarity HAMAP-Rule MF_01227

Sequences

Sequence LengthMass (Da)Tools
C4KYX1 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: 142481A8377961A8

FASTA53159,534
        10         20         30         40         50         60 
MTKYIFVTGG VVSSLGKGIT AASLARLLKN RGLNVTIQKF DPYINIDPGT MSPYQHGEVF 

        70         80         90        100        110        120 
VTDDGAETDL DLGHYERFID INLSQNANVT SGRIYSTVLK KERRGDYNGG TVQVIPHITN 

       130        140        150        160        170        180 
EIKDRVFRAG RETNADVVIT EIGGTVGDIE SLPFIEAIRQ VKNDIGKENV MYVHCTLVPY 

       190        200        210        220        230        240 
LRAAGEMKTK PTQHSVKELR SYGIQPDIIV LRTEHDIPED MREKIALFCD TRKEAVIEAQ 

       250        260        270        280        290        300 
DASTLYEVPL NLQKQGMDQL VNDYFGFNTP AADMTAWKEL VHTVTHLEKK VKIALVGKYV 

       310        320        330        340        350        360 
ELRDAYISVA EALKHAGYAF NADIDIDWIN AEDVTAENVS DILGDADGIL VPGGFGERGI 

       370        380        390        400        410        420 
EGKIEATRFA RENNVPFFGI CLGMQLATVE FARNVLKLDG AHTAEIDPST PYPIIDLLPE 

       430        440        450        460        470        480 
QKDIEDLGGT LRLGLYPCKL EKGTKAHAAY DQELVYERHR HRYEFNNEYR EAFEAEGFKF 

       490        500        510        520        530 
SGTSPDGRLV EIIEIPEHKW FVASQFHPEL ISRPERPQRL FHDFIQASLG E

« Hide

References

[1]"Complete sequence of Exiguobacterium sp. AT1b."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G. expand/collapse author list , Ramaley R.F., Rodrigues D.F., Vishnivetskaya T.A., Kathariou S., Tiedje J.M., Richardson P.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1283 / AT1b.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001615 Genomic DNA. Translation: ACQ70284.1.
RefSeqYP_002885729.1. NC_012673.1.

3D structure databases

ProteinModelPortalC4KYX1.
ModBaseSearch...

Protein-protein interaction databases

STRING360911.EAT1b_1357.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ70284; ACQ70284; EAT1b_1357.
GeneID7870325.
KEGGeat:EAT1b_1357.
PATRIC21877802. VBIExiSp39724_1337.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0504.
HOGENOMHOG000077515.
KOK01937.
OMATNEIKDR.
ProtClustDBPRK05380.

Enzyme and pathway databases

BioCycESP360911:GI4R-1363-MONOMER.
UniPathwayUPA00159; UER00277.

Family and domain databases

HAMAPMF_01227. PyrG.
InterProIPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE_1.
[Graphical view]
PANTHERPTHR11550. PTHR11550. 1 hit.
PfamPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00337. PyrG. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC4KYX1_EXISA
AccessionPrimary (citable) accession number: C4KYX1
Entry history
Integrated into UniProtKB/TrEMBL: July 7, 2009
Last sequence update: July 7, 2009
Last modified: May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info