Q57D05 (PYRG_BRUAB) 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:	BruAb1_1140

Organism

Brucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]

Taxonomic identifier

262698 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella abortus › Brucella abortus bv. 1

Protein attributes

Sequence length	542 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-Rule MF_01227
Catalytic activity	ATP + UTP + NH3 = ADP + phosphate + CTP. 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.
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	'de novo' CTP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glutamine metabolic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW CTP synthase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 542	542	CTP synthase HAMAP-Rule MF_01227		PRO_0000266079
Regions
	Domain	291 – 541	251	Glutamine amidotransferase type-1
	Region	1 – 252	252	Aminator domain HAMAP-Rule MF_01227
Sites
	Active site	380	1	Nucleophile By similarity
	Active site	514	1	By similarity
	Active site	516	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q57D05 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: BBA3FDE07C633A9A	FASTA	542	60,063
	10 20 30 40 50 60 MARYVFITGG VVSSLGKGIA AAALAALLQA RGYRVRIRKL DPYLNVDPGT MSPYQHGEVF 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 ADREIPESDR RKLSLFCNVR ESAVIQALDV 250 260 270 280 290 300 ATIYDVPIAY HKEGLDSEVL SAFGIDPAPK PRMDRWEEVS HRLHNPEGEV TIAVVGKYTG 310 320 330 340 350 360 LKDAYKSLIE ALHHGGLANK VKVNLDWIEA EVFESEDPAP 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

References

[1]

"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017223 Genomic DNA. Translation: AAX74479.1.
RefSeq	YP_221840.1. NC_006932.1.
3D structure databases
HSSP	HSSP built from PDB template 1S1M based on UniProtKB P0A7E5.
ProteinModelPortal	Q57D05.
SMR	Q57D05. Positions 2-540.
ModBase	Search...
Protein-protein interaction databases
STRING	262698.BruAb1_1140.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAX74479; AAX74479; BruAb1_1140.
GeneID	3341150.
KEGG	bmb:BruAb1_1140.
PATRIC	17823970. VBIBruAbo15061_1207.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0504.
HOGENOM	HOG000077515.
KO	K01937.
OMA	TNEIKDR.
ProtClustDB	PRK05380.
Enzyme and pathway databases
BioCyc	BABO262698:GJC2-1162-MONOMER.
UniPathway	UPA00159; UER00277.
Family and domain databases
HAMAP	MF_01227. PyrG.
InterPro	IPR004468. CTP_synthase. IPR017456. CTP_synthase_N. IPR017926. GATASE_1. [Graphical view]
PANTHER	PTHR11550. PTHR11550. 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_BRUAB

Accession

Primary (citable) accession number: Q57D05

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program