NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153;
DOI=10.1093/nar/28.21.4317; PubMed=11058132 [NCBI, ExPASy, EBI, Israel, Japan]
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis.";
Nucleic Acids Res. 28:4317-4331(2000).

Comments

CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 2/6 .
SIMILARITY: Belongs to the ATCase/OTCase family.

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

BA000004; BAB06258.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C83967; C83967.

RefSeq

NP_243405.1; -.

3D structure databases

HSSP

P77918; 1ML4. [HSSP ENTRY / PDB]

ModBase

Q9K9V6.

Enzyme and pathway databases

BioCyc

BHAL272558:BH2539-MON; -.

Ontologies

GO:0004070;	Molecular function: aspartate carbamoyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0006221;	Biological process: pyrimidine nucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00001; -; 1.
PBIL [Tree]

InterPro

IPR006130; Asp/Orn_carbamoyltranf.
IPR006132; Asp/Orn_carbamoyltranf_P_bd.
IPR006131; Asp_carbamoyltransf_Asp/Orn_bd.
IPR002082; Aspartate_carbamoyltransf_euk.
Graphical view of domain structure.

Pfam

PF00185; OTCace; 1.
PF02729; OTCace_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00100; AOTCASE.
PR00101; ATCASE.

TIGRFAMs

TIGR00670; asp_carb_tr; 1.

PROSITE

PS00097; CARBAMOYLTRANSFERASE; 1.

Genome annotation databases

891505; -.

BA000004_GR; BH2539.

bha:BH2539; -.

fig|272558.1.peg.2539; -.

Phylogenomic databases

HOGENOM

Q9K9V6; -.

Genome annotation databases

CMR

Q9K9V6; BH2539.

Other

UniRef

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

Keywords

Complete proteome; Pyrimidine biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 305`	`305`		`Aspartate carbamoyltransferase.`	`PRO_0000113095`

Sequence information

Length: 305 AA [This is the length of the unprocessed precursor]

Molecular weight: 34829 Da [This is the MW of the unprocessed precursor]

CRC64: 974D09A8D5410074 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVPFLQDHD TKHDLLTMSH LSLEEIEHIL HDAQQFENGA LWSPEEKLFV ANLFFEPSTR 

        70         80         90        100        110        120 
TRVSFEVAEQ RLGLHVVNVD GERSSVQKGE TLYDTAKTLE SIGVNALVIR HRQDRYFEEL 

       130        140        150        160        170        180 
KDRINIPIIN AGDGCGHHPT QSLLDLWTIQ QEFGRFSNLI TVISGDLRHS RVARSNAETL 

       190        200        210        220        230        240 
TRLGARVYIS GPREWMEGYE GVYPYVTMDE AVELADVIML LRVQHERHDG TVSFTQASYH 

       250        260        270        280        290        300 
EQFGLTVKRE ARMKPKSIVM HPAPVNRNVE IASELVECPR SRIFKQMKNG VAIRMAVLKR 


ALTDE

Q9K9V6 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