NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
DOI=10.1101/gr.1285603; PubMed=12840036 [NCBI, ExPASy, EBI, Israel, Japan]
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens.";
Genome Res. 13:1572-1579(2003).

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

BA000035; BAC18540.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_738340.1; -.

3D structure databases

HSSP

P00907; 1CE8. [HSSP ENTRY / PDB]

ModBase

Q8FT41.

Enzyme and pathway databases

BioCyc

CEFF196164:CE1730-MON; -.

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).

Genome annotation databases

1034230; -.

BA000035_GR; CE1730.

cef:CE1730; -.

fig|196164.1.peg.1730; -.

Phylogenomic databases

HOGENOM

Q8FT41; -.

Genome annotation databases

CMR

Q8FT41; CE1730.

Other

ProtoNet

Q8FT41.

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`	`1 400`	`400`	`Carbamoyl-phosphate synthase small chain.`	`PRO_0000112270`
`DOMAIN`	`200 395`	`196`	`Glutamine amidotransferase type-1.`
`REGION`	`1 199`	`199`	`CPSase.`
`ACT_SITE`	`278 278`		`Nucleophile (By similarity).`
`ACT_SITE`	`368 368`		`By similarity.`
`ACT_SITE`	`370 370`		`By similarity.`

Sequence information

Length: 400 AA [This is the length of the unprocessed precursor]

Molecular weight: 42885 Da [This is the MW of the unprocessed precursor]

CRC64: CFEE077BA9504756 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSNETNANST DSRQGVTNIG SVPAYLVLAD GRTFKGFGFG AIGTTLGEAV FTTAMTGYQE 

        70         80         90        100        110        120 
TMTDPSYHRQ IVVATAPQIG NTGWNEEDNE SHDGSIWVAG LVIRDLAVRV SNWRATTTLQ 

       130        140        150        160        170        180 
EEMAKQGVVG IGGIDTRALV RHIRNEGAVP AGIFSGADAE RPIEELVEIV KSQPSMVGAN 

       190        200        210        220        230        240 
LAVEVSVDKP YVIEAEGEAR HTVVAYDLGI KQNTPRRFAA RGVRTVIVPA ETPFEEIKQY 

       250        260        270        280        290        300 
NPSGVFISNG PGDPAAADIM VNIVREVLAA DIPFFGICFG NQILGRAFGM ETYKLKFGHR 

       310        320        330        340        350        360 
GINVPVKNHI TGKIDITAQN HGFALKGEAG QEFETDFGTA VVTHTCLNDG VVEGVALKSG 

       370        380        390        400 
RAYSVQYHPE AAAGPNDASP LFDQFVALMD EDSENQKEEA

Q8FT41 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