Q726J4 (CARA_DESVH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbamoyl-phosphate synthase small chain
EC=6.3.5.5

Alternative name(s):
Carbamoyl-phosphate synthetase glutamine chain

Gene names

Name:	carA
Ordered Locus Names:	DVU_3113

Organism

Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)

Taxonomic identifier

882 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. HAMAP MF_01209
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. HAMAP MF_01209 Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. HAMAP MF_01209
Subunit structure	Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate By similarity.
Sequence similarities	Belongs to the CarA family. Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Pyrimidine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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 carbamoyl-phosphate synthase (glutamine-hydrolyzing) 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 – 375	375	Carbamoyl-phosphate synthase small chain HAMAP MF_01209		PRO_1000138859
Regions
	Domain	190 – 375	186	Glutamine amidotransferase type-1
	Region	1 – 186	186	CPSase HAMAP MF_01209
Sites
	Active site	265	1	Nucleophile By similarity
	Active site	348	1	By similarity
	Active site	350	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q726J4 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 53D76070C62B7BEA	FASTA	375	40,745
	10 20 30 40 50 60 MRALLALEDG FVLEGRSFTG PGETGGEAIF NTGMTGYQEV LTDPSYAGQM VCMTYPLVGN 70 80 90 100 110 120 YGVTREDMES GKVHVEAFIV KECCKVPSNW RSEISLPDYL KRHGVMGIEG IDTRALTRHL 130 140 150 160 170 180 RIHGAMRGVI STQETDPARL VERARALPSM EGQNLVTRVA PAAPYRWDGE RPQAVTLEPG 190 200 210 220 230 240 GCAWVGKGPR LVVYDFGIKW NILRLLAQQG FDMLVVPPSF KAADVAAVGA QAVFLSNGPG 250 260 270 280 290 300 DPATLKDEIA EIAKLAQTYP TAGICLGHQL LGHALGGRTM KLKFGHHGCN HPVKDLTTGR 310 320 330 340 350 360 IEISSQNHGF CVDIDSLTDV EITHVNLNDG TLEGFAHKTK PVIAVQHHPE ASPGPNDSRY 370 FFARFRNMVR EAAGC

References

[1]

"The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough." Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Fouts D.E. , Haft D.H., Selengut J., Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M. Nat. Biotechnol. 22:554-559(2004) [PubMed: 15077118] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hildenborough / ATCC 29579 / NCIMB 8303.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017285 Genomic DNA. Translation: AAS97584.1.
RefSeq	YP_012324.1. NC_002937.3.
3D structure databases
HSSP	HSSP built from PDB template 1CE8 based on UniProtKB P0A6F1.
ProteinModelPortal	Q726J4.
ModBase	Search...
Protein-protein interaction databases
STRING	Q726J4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2796605.
GenomeReviews	Gene locus DVU_3113 in contig AE017285_GR.
KEGG	dvu:DVU3113.
PATRIC	32065778. VBIDesVul119526_2824.
TIGR	DVU_3113.
Phylogenomic databases
eggNOG	COG0505.
HOGENOM	HBG286341.
OMA	FTYPELG.
PhylomeDB	Q726J4.
ProtClustDB	PRK12564.
Enzyme and pathway databases
BioCyc	DVUL882:DVU_3113-MONOMER.
Family and domain databases
HAMAP	MF_01209. CPSase_S_chain. [Tree]
InterPro	IPR006274. CarbamoylP_synth_ssu. IPR002474. CarbamoylP_synth_ssu_N. IPR017926. GATASE_1. [Graphical view]
Gene3D	G3DSA:3.50.30.20. G3DSA:3.50.30.20. 1 hit.
KO	K01956.
Pfam	PF00988. CPSase_sm_chain. 1 hit. PF00117. GATase. 1 hit. [Graphical view]
SMART	SM01097. CPSase_sm_chain. 1 hit. [Graphical view]
SUPFAM	SSF52021. CP_synthsmall. 1 hit.
TIGRFAMs	TIGR01368. CPSaseIIsmall. 1 hit.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CARA_DESVH

Accession

Primary (citable) accession number: Q726J4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program