Q9PJ84 (PYRG_CAMJE) 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:	Cj0027

Organism

Campylobacter jejuni

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	543 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 Reference 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 – 543	543	CTP synthase HAMAP MF_01227		PRO_0000138172
Regions
	Domain	292 – 543	252	Glutamine amidotransferase type-1
	Region	1 – 254	254	Aminator domain HAMAP MF_01227
Sites
	Active site	381	1	Nucleophile By similarity
	Active site	516	1	By similarity
	Active site	518	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PJ84 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 5DA89FA7D4C680EA	FASTA	543	60,401
	10 20 30 40 50 60 MKQTKYIFVT GGVLSSLGKG IAAASIATLL KNSGLKVSIL KADPYINVDP GTMSPFEHGE 70 80 90 100 110 120 VFVTDDGAET DLDLGHYERF LDESLSQDNN FTTGRVYQSV IEKERRGEYL GKTIQVIPHI 130 140 150 160 170 180 VGEIKDRIKK AGEGKDILIV EIGGTVGDIE GLPFLEAIRA LRLEVGKNNA MNIHLTLVPF 190 200 210 220 230 240 IKAAGELKTK PTQHSVGELR RIGISPDMII CRSEKALDRD LKDKIAISCG VEKNCVIESV 250 260 270 280 290 300 DAASIYQIPL NFLKQDILSP IAEILDLKNL KPNMENWDSL VKRVIAPSNE VKIAFVGKYV 310 320 330 340 350 360 DLKESYKSLT EAIIHAGAAL DTKVELKWVD SEKLENMESS EVFKDVSGIL VAGGFGYRGV 370 380 390 400 410 420 EGKIKAIQYA RENKIPFLGI CLGMQLALVE FARNVLKLKD VNSSEFNEKC QNPVVYLIDE 430 440 450 460 470 480 FMDTNGEKQI RTAKTPLGGT MRLGAYKCDI KEKSLLAKVY NEVKSVKERH RHRYEANPKY 490 500 510 520 530 540 RADFEKYGLI VSGESKGLIE AVELNCHPFF LAVQFHPEFT SRLEHVNPVI CSFIKAAINY EDN

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL34208.1.
PIR	F81418.
RefSeq	YP_002343499.1. NC_002163.1.
3D structure databases
ProteinModelPortal	Q9PJ84.
SMR	Q9PJ84. Positions 3-542.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PJ84. 50 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	904367.
GenomeReviews	Gene locus Cj0027 in contig AL111168_GR.
KEGG	cje:Cj0027.
PATRIC	20056975. VBICamJej33762_0027.
Phylogenomic databases
HOGENOM	HBG597806.
OMA	EQCSIAL.
ProtClustDB	PRK05380.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ0027-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_CAMJE

Accession

Primary (citable) accession number: Q9PJ84
Secondary accession number(s): Q0PC98

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program