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UniProtKB/Swiss-Prot entry P71811

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information

Entry name

CARA_MYCTU

Primary accession number

P71811

Secondary accession numbers

None

Integrated into Swiss-Prot on

December 1, 2000

Sequence was last modified on

February 1, 1997 (Sequence version 1)

Annotations were last modified on

November 25, 2008 (Entry version 73)

Name and origin of the protein

Protein name

Carbamoyl-phosphate synthase small chain

Synonyms

EC 6.3.5.5
Carbamoyl-phosphate synthetase glutamine chain

Gene name

	Name:	carA
	OrderedLocusNames:	Rv1383, MT1427
	ORFNames:	MTCY02B12.17

From

Mycobacterium tuberculosis

[TaxID: 1773]

[HAMAP proteome]

Taxonomy

Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
DOI=10.1038/31159; PubMed=9634230 [NCBI, ExPASy, EBI, Israel, Japan]
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.";
Nature 393:537-544(1998).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CDC 1551 / Oshkosh;
DOI=10.1128/JB.184.19.5479-5490.2002; PubMed=12218036 [NCBI, ExPASy, EBI, Israel, Japan]
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains.";
J. Bacteriol. 184:5479-5490(2002).

Comments

CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO₃^- + H₂O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from HCO(3)(-): step 1/1 .
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 1/6 .
SUBUNIT: 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).
SIMILARITY: Belongs to the carA family.
SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BX842576; CAB02644.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000516; AAK45692.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D70959; D70959.

RefSeq

NP_215899.1; -.
NP_335878.1; -.

3D structure databases

HSSP

P00907; 1CE8. [HSSP ENTRY / PDB]

ModBase

P71811.

Organism-specific databases

TubercuList

Rv1383; -.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004088;	Molecular function: carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity (inferred from electronic annotation from HAMAP).
GO:0006526;	Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0006541;	Biological process: glutamine metabolic process (inferred from electronic annotation from InterPro).
GO:0006221;	Biological process: pyrimidine nucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01209; -; 1.
PBIL [Tree]

InterPro

IPR006220; Anth_synthII.
IPR001317; CarbamoylP_synth_GATase.
IPR006274; CarbamoylP_synth_ssu.
IPR002474; CarbamoylP_synth_ssu_N.
IPR011702; GATASE.
IPR012998; GATase_1_AS.
IPR000991; GATase_class1_C.
Graphical view of domain structure.

PANTHER

PTHR11405:SF4; CarA_synth_small; 1.

Pfam

PF00988; CPSase_sm_chain; 1.
PF00117; GATase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00097; ANTSNTHASEII.
PR00099; CPSGATASE.
PR00096; GATASE.

TIGRFAMs

TIGR01368; CPSaseIIsmall; 1.

PROSITE

PS51273; GATASE_TYPE_1; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P71811.

Genome annotation databases

GeneID

886761; -.
924557; -.

GenomeReviews

AE000516_GR; MT1427.
AL123456_GR; Rv1383.

KEGG

mtc:MT1427; -.
mtu:Rv1383; -.

TIGR

MT1427; -.

Phylogenomic databases

HOGENOM

P71811; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; Glutamine amidotransferase; Ligase; Pyrimidine biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 376`	`376`	`Carbamoyl-phosphate synthase small chain.`	`PRO_0000112296`
`DOMAIN`	`184 376`	`193`	`Glutamine amidotransferase type-1.`
`REGION`	`1 181`	`181`	`CPSase.`
`ACT_SITE`	`260 260`		`Nucleophile (By similarity).`
`ACT_SITE`	`350 350`		`By similarity.`
`ACT_SITE`	`352 352`		`By similarity.`

Sequence information

Length: 376 AA [This is the length of the unprocessed precursor]

Molecular weight: 39767 Da [This is the MW of the unprocessed precursor]

CRC64: DF057465F47AE46D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKAVLVLED GRVFTGRPFG ATGQALGEAV FSTGMSGYQE TLTDPSYHRQ IVVATAPQIG 

        70         80         90        100        110        120 
NTGWNGEDSE SRGERIWVAG YAVRDPSPRA SNWRATGTLE DELIRQRIVG IAGIDTRAVV 

       130        140        150        160        170        180 
RHLRSRGSMK AGVFSDGALA EPADLIARVR AQQSMLGADL AGEVSTAEPY VVEPDGPPGV 

       190        200        210        220        230        240 
SRFTVAALDL GIKTNTPRNF ARRGIRCHVL PASTTFEQIA ELNPHGVFLS NGPGDPATAD 

       250        260        270        280        290        300 
HVVALTREVL GAGIPLFGIC FGNQILGRAL GLSTYKMVFG HRGINIPVVD HATGRVAVTA 

       310        320        330        340        350        360 
QNHGFALQGE AGQSFATPFG PAVVSHTCAN DGVVEGVKLV DGRAFSVQYH PEAAAGPHDA 

       370 
EYLFDQFVEL MAGEGR

P71811 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools