Reviewed, UniProtKB/Swiss-Prot Q819S2 (CARA_BACCR)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 HCO(3)(-): step 1/1. HAMAP MF_01209 Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 1/6. 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
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP 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: HAMAP carbamoyl-phosphate synthase (glutamine-hydrolyzing) 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 – 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)
	Q819S2-1 [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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016877 Genomic DNA. Translation: AAP10808.1. Different initiation.
RefSeq	NP_833607.1.
3D structure databases
HSSP	HSSP built from PDB template 1JDB based on UniProtKB P00907.
ModBase	Search...
Genome annotation databases
GeneID	1206232.
GenomeReviews	Gene locus BC_3887 in contig AE016877_GR.
KEGG	bce:BC3887.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q819S2.
Enzyme and pathway databases
BioCyc	BCER226900:BC_3887-MON.
Family and domain databases
HAMAP	MF_01209. [Tree]
InterPro	IPR006220. Anth_synthII. IPR001317. CarbamoylP_synth_GATase. IPR006274. CarbamoylP_synth_ssu. IPR002474. CarbamoylP_synth_ssu_N. IPR011702. GATASE. IPR017926. GATASE_1. IPR000991. GATase_class1_C. [Graphical view]
PANTHER	PTHR11405:SF4. CarA_synth_small. 1 hit.
Pfam	PF00988. CPSase_sm_chain. 1 hit. PF00117. GATase. 1 hit. [Graphical view]
PRINTS	PR00097. ANTSNTHASEII. PR00099. CPSGATASE. PR00096. GATASE.
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:	June 16, 2009
This is version 46 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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