Q819S2 (CARA_BACCR) 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:	BC_3887

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31)

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	365 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.
Sequence caution	The sequence AAP10808.1 differs from that shown. Reason: Erroneous initiation.

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 – 365	365	Carbamoyl-phosphate synthase small chain HAMAP MF_01209		PRO_0000112249
Regions
	Domain	170 – 357	188	Glutamine amidotransferase type-1
	Region	1 – 166	166	CPSase HAMAP MF_01209
Sites
	Active site	245	1	Nucleophile By similarity
	Active site	330	1	By similarity
	Active site	332	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q819S2 [UniParc]. Last modified March 1, 2005. Version 2. Checksum: 0C08E19086E4665A	FASTA	365	40,362
	10 20 30 40 50 60 MKRQLILEDG TVLIGTGFGG EIEKSGEVVF TTGMTGYQET LSDPSYCGQI VTFTYPLIGN 70 80 90 100 110 120 YGINRDDFES IHPSVNGLIV NEICNHPSNF RNEISLNDYL KERNIPGLAG IDTRKLTRKI 130 140 150 160 170 180 RQYGTLRGRL CNMDADVEYI VSQLKATVFT DHVKRVSTKD PYPSPGRGHR VVLVDFGMKH 190 200 210 220 230 240 GILRELNKRD CDVIVVPYNT TAEEILRLSP DGIMLSNGPG DPKDVPEAIE MLKDIIGKVP 250 260 270 280 290 300 LFGICLGHQL FALASGANTS KLKFGHRGLN HPVKNLATGK VAITSQNHGY AVEEESVENT 310 320 330 340 350 360 DLEITHVALN DGTVEGLRHK KFPAFTVQYH PEASAGPEDA NDLFEDFLTM IENFKKEGEE LCQNA

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016877 Genomic DNA. Translation: AAP10808.1. Different initiation.
RefSeq	NP_833607.1. NC_004722.1.
3D structure databases
ProteinModelPortal	Q819S2.
ModBase	Search...
Protein-protein interaction databases
STRING	Q819S2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000033695; EBBACP00000032901; EBBACG00000033686.
GeneID	1206232.
GenomeReviews	Gene locus BC_3887 in contig AE016877_GR.
KEGG	bce:BC3887.
PATRIC	32603811. VBIBacCer54481_4009.
Phylogenomic databases
eggNOG	COG0505.
GeneTree	EBGT00070000032080.
HOGENOM	HBG286341.
OMA	FTYPELG.
PhylomeDB	Q819S2.
ProtClustDB	PRK12564.
Enzyme and pathway databases
BioCyc	BCER226900:BC_3887-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.
PANTHER	PTHR11405:SF4. CarA_synth_small. 1 hit.
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_BACCR

Accession

Primary (citable) accession number: Q819S2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	January 25, 2012
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program