Reviewed, UniProtKB/Swiss-Prot Q6B940 (CARA_GRATL)

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:	Grc000013

Encoded on

Plastid; Chloroplast

Organism

Gracilaria tenuistipitata var. liui (Red alga)

Taxonomic identifier

285951 [NCBI]

Taxonomic lineage

Eukaryota › Rhodophyta › Florideophyceae › Gracilariales › Gracilariaceae › Gracilaria

Protein attributes

Sequence length	395 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. HAMAP MF_01209
Subcellular location	Plastid › chloroplast HAMAP MF_01209.
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
Cellular component	Chloroplast Plastid
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
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
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 395	395	Carbamoyl-phosphate synthase small chain HAMAP MF_01209		PRO_0000112370
Regions
	Domain	196 – 383	188	Glutamine amidotransferase type-1
	Region	1 – 192	192	CPSase HAMAP MF_01209
Sites
	Active site	273	1	Nucleophile By similarity
	Active site	356	1	By similarity
	Active site	358	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6B940-1 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: 0F25E4FC7AC61739	FASTA	395	45,003
	10 20 30 40 50 60 MTYNLHPAIL VLKDGKFYRG WTLINSIISF GEVVFNTGMT GYQEIMTDPS YAEQIITFTY 70 80 90 100 110 120 PEIGNTGINH EDNESNKIHV KGIITKNICF SPNNWRQQES FINYIFNNQI PHIFGIDTRA 130 140 150 160 170 180 LTKHLRKTGS MNGCISSQYL NPYLLSTKFK DRLSIESSDL VKQVTTSKNY EFQGYSHKHF 190 200 210 220 230 240 SYLQYKTDKM YGYGLKIILI DFGVKYNILS RLDNYGCSIQ ILPATSSYET INAYNPDGII 250 260 270 280 290 300 LSNGPGDPSI ITYAIKTVKK IIKYTNIPIF GICMGHQIIS LALEGTTFKL KFGHRGLNHP 310 320 330 340 350 360 AGMKQKAEVT SQNHGFAVNQ ESLYKDTINI THFNLNDTTV AGILHNKKPI FSVQYHPEAS 370 380 390 PGPHDSDYLF KYFINLIKHF KQYKNYKNSS LAQAR

References

[1]

"Comparative analysis of the complete plastid genome sequence of the red alga Gracilaria tenuistipitata var. liui provides insights into the evolution of rhodoplasts and their relationship to other plastids." Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C. J. Mol. Evol. 59:464-477(2004) [PubMed: 15638458] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY673996 Genomic DNA. Translation: AAT79595.1.
RefSeq	YP_063520.1.
3D structure databases
SMR	Q6B940. Positions 5-382.
ModBase	Search...
Genome annotation databases
GeneID	2944065.
Enzyme and pathway databases
BRENDA	6.3.5.5. 302087.
Family and domain databases
HAMAP	MF_01209_B. CPSase_S_chain_B. [Tree]
InterPro	IPR006220. Anth_synthII. IPR001317. CarbamoylP_synth_GATase_dom. 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_GRATL

Accession

Primary (citable) accession number: Q6B940

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	September 13, 2004
Last modified:	February 9, 2010
This is version 43 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)