Reviewed, UniProtKB/Swiss-Prot Q6NH15 (CARA_CORDI)

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:	DIP1332

Organism

Corynebacterium diphtheriae [Complete proteome] [HAMAP]

Taxonomic identifier

1717 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	379 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
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 – 379	379	Carbamoyl-phosphate synthase small chain HAMAP MF_01209		PRO_0000112269
Regions
	Domain	185 – 379	195	Glutamine amidotransferase type-1
	Region	1 – 183	183	CPSase HAMAP MF_01209
Sites
	Active site	263	1	Nucleophile By similarity
	Active site	353	1	By similarity
	Active site	355	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6NH15-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 3929EE9440F27FFD	FASTA	379	40,772
	10 20 30 40 50 60 MTSQDRSEAV LVLADGRIFK GESFGAEGAT LGEAVFTTAM SGYQETMTDP SYHRQIVVAT 70 80 90 100 110 120 APQIGNTGWN DEDGESHGDK IWVAGLVIRD LSTAVSNWRA KRSLEDEMRE QNIVGISGVD 130 140 150 160 170 180 TRAIVRHLRN FGSVAAGIFS GEAAKQPHDE LIEIVKSQPS MAGADLASEV STQEAYVVEP 190 200 210 220 230 240 DGEALYTVVA YDMGIKTNTP RNFSRRGIRT VVVPANTPAE DIAQYNPDGV FVSNGPGDPA 250 260 270 280 290 300 TADVMVGIVQ EILAQKIPFF GICFGNQILG RALGMNTYKM KFGHRGINVP VLNHLTGKID 310 320 330 340 350 360 ITAQNHGFAL EGTALEQFDT PFGPAHVTHT CLNDDTVEGV ALVNGLAYSV QYHPEAAAGP 370 HDANPLFDQF VELIQANKK

References

[1]

"The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129." Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K., Moule S. , Quail M.A., Rabbinowitsch E., Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G., Parkhill J. Nucleic Acids Res. 31:6516-6523(2003) [PubMed: 14602910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700971 / NCTC 13129 / Biotype gravis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248357 Genomic DNA. Translation: CAE49860.1.
RefSeq	NP_939685.1.
3D structure databases
SMR	Q6NH15. Positions 8-379.
ModBase	Search...
Genome annotation databases
GeneID	2649886.
KEGG	cdi:DIP1332.
NMPDR	fig|257309.1.peg.1276.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG286341.
OMA	IFISETY.
PhylomeDB	Q6NH15.
Enzyme and pathway databases
BioCyc	CDIP257309:DIP1332-MONOMER.
BRENDA	6.3.5.5. 20483.
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_CORDI

Accession

Primary (citable) accession number: Q6NH15

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	July 5, 2004
Last modified:	February 9, 2010
This is version 49 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)