Reviewed, UniProtKB/Swiss-Prot Q2GLS9 (PYRG_ANAPZ)

Names and origin

Protein names

Recommended name:
    CTP synthase
    EC=6.3.4.2
Alternative name(s):
    UTP--ammonia ligase
    CTP synthetase

Gene names

Name:	pyrG
Ordered Locus Names:	APH_0038

Organism

Anaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP]

Taxonomic identifier

212042 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group

Protein attributes

Sequence length	541 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Pathway	Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. HAMAP 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	glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pyrimidine nucleotide biosynthetic 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 – 541	541	CTP synthase HAMAP MF_01227		PRO_0000266055
Regions
	Domain	296 – 537	242	Glutamine amidotransferase type-1
	Region	1 – 258	258	Aminator domain HAMAP MF_01227
Sites
	Active site	382	1	Nucleophile By similarity
	Active site	510	1	By similarity
	Active site	512	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2GLS9-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: CBB6A8950CB6809E	FASTA	541	59,454
	10 20 30 40 50 60 MVGKLNPTRF IFVTGGVVSS LGKGLAAASI GALLQARGFS VRLRKLDPYL NVDPGTMSPA 70 80 90 100 110 120 QHGEVFVTSD GGETDLDLGH YERFTGVMKT RADNVTAGKI YHELIVKERR GDYLGQTVQV 130 140 150 160 170 180 IPHVIDLIIS CILHNDAGAD FVICEIGGTV GDIESQPFLE AIRQVSYRLS KNLTIFVHLT 190 200 210 220 230 240 LVPYIGAVGE LKTKPTQHSV KELSSLGIQP DIVLYRSRAQ LPQYQCAKIA NFCNVAEDNI 250 260 270 280 290 300 IAALDVSNIY MLPVMYHEHR LDTQILKHFD VDSPEPDLTQ WENVLRMSET ASDRIVIAIV 310 320 330 340 350 360 GKYVTSLDAY TSLEEALRHA GLHSGIRVEI KWVDARLPAS EIDLTDADAI LIPGGFGDNG 370 380 390 400 410 420 IGTKICAIEY ARVNNIPMLG ICLGMQLAVI EFALNVAGIE DANSTEFKSD CKNPVVCELP 430 440 450 460 470 480 GLQVGDEYKM GGSMRLGSYT CNLAPGSRIM SIYDSSTVVE RRRHRYGINP EYRDVLSKCG 490 500 510 520 530 540 LAFTGAAEDR DLPEVLELPD HPWFIGVQFH PEFQSTPFKS HPLFLSFVTS TLQVKKASSR S

References

[1]

"Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. , Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H. PLoS Genet. 2:208-222(2006) [PubMed: 16482227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000235 Genomic DNA. Translation: ABD43636.1.
RefSeq	YP_504672.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3930011.
GenomeReviews	Gene locus APH_0038 in contig CP000235_GR.
KEGG	aph:APH_0038.
NMPDR	fig|212042.5.peg.33.
TIGR	APH_0038.
Phylogenomic databases
HOGENOM	Q2GLS9.
OMA	Q2GLS9. EFNNAYR.
Enzyme and pathway databases
BioCyc	APHA212042:APH_0038-MON.
Family and domain databases
HAMAP	MF_01227. [Tree]
InterPro	IPR004468. CTP_synthase. IPR017456. CTP_synthase_N. IPR017926. GATASE_1. IPR000991. GATase_class1_C. [Graphical view]
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_ANAPZ

Accession

Primary (citable) accession number: Q2GLS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	March 21, 2006
Last modified:	June 16, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)