Q0VQD8 (PYRG_ALCBS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CTP synthase
EC=6.3.4.2

Alternative name(s):
CTP synthetase
UTP--ammonia ligase

Gene names

Name:	pyrG
Ordered Locus Names:	ABO_1162

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	545 AA.
Sequence status	Complete.
Protein existence	Inferred 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 MF_01227
Catalytic activity	ATP + UTP + NH3 = ADP + phosphate + CTP. HAMAP MF_01227
Enzyme regulation	Allosterically activated by GTP, when glutamine is the substrate. Inhibited by CTP By similarity. HAMAP MF_01227
Pathway	Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. HAMAP MF_01227
Subunit structure	Homotetramer By similarity. HAMAP MF_01227
Sequence similarities	Belongs to the CTP synthase family. Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW CTP synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 545	545	CTP synthase HAMAP MF_01227		PRO_0000266050
Regions
	Domain	290 – 541	252	Glutamine amidotransferase type-1
	Region	1 – 252	252	Aminator domain HAMAP MF_01227
Sites
	Active site	378	1	Nucleophile By similarity
	Active site	514	1	By similarity
	Active site	516	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VQD8 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 8FA206D99BCCA6D8	FASTA	545	59,687
	10 20 30 40 50 60 MSRFIFVTGG VVSSLGKGIT SASLATLLEA RGLNVTLIKM DPYINVDPGT MSPYQHGEVF 70 80 90 100 110 120 VTEDGAETDL DLGHYERFIR TRLNRRNSFT TGRVYQHVLD KERRGEYLGA TVQVIPHITD 130 140 150 160 170 180 EIKLKIREGA GDADVAIVEI GGTAGDIESL PFLEAARQMR VELGSSQSLL VHLTLVPYIA 190 200 210 220 230 240 TAGEIKTKPT QHSVKELRSI GLQPDILVCR ADDPIPQSAR EKIALFTNVE ARAVISSPDC 250 260 270 280 290 300 KTIYQVPRGM HEQGLDAIVV EKFGLDLPEP DLGEWDRVVE AQLNPEHEVT VGMVGKYIEL 310 320 330 340 350 360 VDAYKSLNEA LIHAGISNRA KVNILYLDAE DIERDGTGVL ESLDAILVPG GFGDRGTEGK 370 380 390 400 410 420 IAAIRYAREN KVPYLGICLG MQLAVIEYAR HVAGIEKAHS SELNPNTPDP VVGLITEWIT 430 440 450 460 470 480 EDGQKELRSA DSDLGGTMRL GGQECVLEAD SRAAECYGST HIVERHRHRY EVNNNYLPQL 490 500 510 520 530 540 EAAGLKIVGR SADGELVEVI EVGDHPWFVA CQFHPEFTST PRDGHGLFKG YVAAALAEQK AHKET

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SK2 / ATCC 700651 / DSM 11573.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM286690 Genomic DNA. Translation: CAL16610.1.
RefSeq	YP_692882.1. NC_008260.1.
3D structure databases
ProteinModelPortal	Q0VQD8.
SMR	Q0VQD8. Positions 2-540.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0VQD8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4211642.
GenomeReviews	Gene locus ABO_1162 in contig AM286690_GR.
KEGG	abo:ABO_1162.
NMPDR	fig|393595.12.peg.1173.
PATRIC	20840063. VBIAlcBor124741_1222.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0504.
HOGENOM	HBG597806.
OMA	RVTMQKL.
PhylomeDB	Q0VQD8.
ProtClustDB	PRK05380.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_1162-MONOMER.
Family and domain databases
HAMAP	MF_01227. PyrG. [Tree]
InterPro	IPR004468. CTP_synthase. IPR017456. CTP_synthase_N. IPR017926. GATASE_1. [Graphical view]
KO	K01937.
PANTHER	PTHR11550. PyrG_synth. 1 hit.
Pfam	PF06418. CTP_synth_N. 1 hit. PF00117. GATase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00337. PyrG. 1 hit.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRG_ALCBS

Accession

Primary (citable) accession number: Q0VQD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	September 5, 2006
Last modified:	January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program