NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DSM 405 / IFO 15313 / YP-T;
PubMed=8206848 [NCBI, ExPASy, EBI, Israel, Japan]
Ghim S.Y., Neuhard J.;
"The pyrimidine biosynthesis operon of the thermophile Bacillus caldolyticus includes genes for uracil phosphoribosyltransferase and uracil permease.";
J. Bacteriol. 176:3698-3707(1994).

Comments

CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO₃^- + H₂O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.
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.
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

X73308; CAA51738.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I40168; I40168.

3D structure databases

HSSP

P00907; 1A9X. [HSSP ENTRY / PDB]

ModBase

P52557.

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).

Other

ProtoNet

P52557.

UniRef

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

Keywords

Glutamine amidotransferase; Ligase; Pyrimidine biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 364`	`364`	`Carbamoyl-phosphate synthase pyrimidine-specific small chain.`	`PRO_0000112248`
`DOMAIN`	`171 358`	`188`	`Glutamine amidotransferase type-1.`
`REGION`	`1 167`	`167`	`CPSase.`
`ACT_SITE`	`246 246`		`Nucleophile (By similarity).`
`ACT_SITE`	`331 331`		`By similarity.`
`ACT_SITE`	`333 333`		`By similarity.`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 40289 Da [This is the MW of the unprocessed precursor]

CRC64: 383A54A839F6631F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKRQLILEDG SFFVGERFGS LKETTGEVVF NTGMTGYQEI LSDPSYCGQI VTMTYPLIGN 

        70         80         90        100        110        120 
YGINRDDFEA IRPHVHGFIV KEACVKPSNW RGELTLDEYL KEKGIPGLSG IDTRKLTRLI 

       130        140        150        160        170        180 
RQYGTLKGMI CGLDVDPVEA AAKLRAMEWP RDQVRRVSTK SAYPSPGRGE RIVLIDFGMK 

       190        200        210        220        230        240 
HGILRELNKR NCDVIVLPYN ATAEEVLGWH PDGVMLSNGP GDPKDVPEAI EMIRGILGKV 

       250        260        270        280        290        300 
PLFGICLGHQ LFALACGANT EKMKFGHRGS NHPVKDLRTG KVAITSQNHG YTVTHESLSG 

       310        320        330        340        350        360 
TRLEVTHIAL NDGTVEGLRH LDVPAFTVQY HPEASPGPED ANPLFDEFLA LIREFNKKGE 


VIHA

P52557 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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