NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=YCH46;
DOI=10.1073/pnas.0404172101; PubMed=15466707 [NCBI, ExPASy, EBI, Israel, Japan]
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation.";
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).

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

AP006841; BAD48955.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_099489.1; -.

3D structure databases

ModBase

Q64U74.

Enzyme and pathway databases

BioCyc

BFRA295405:BF2208-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.

BLOCKS

Q64U74.

Genome annotation databases

GeneID

3084062; -.

GenomeReviews

AP006841_GR; BF2208.

KEGG

bfr:BF2208; -.

Phylogenomic databases

HOGENOM

Q64U74; -.

Genome annotation databases

CMR

Q64U74; BF2208.

Other

ProtoNet

Q64U74.

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`	`1 308`	`308`		`Aspartate carbamoyltransferase.`	`PRO_0000113094`

Sequence information

Length: 308 AA [This is the length of the unprocessed precursor]

Molecular weight: 35578 Da [This is the MW of the unprocessed precursor]

CRC64: 042557C7969DCE38 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MENRSLVTIA EHSREKILYM LEMAKQFEKN PNRRLLEGKV VATLFFEPST RTRLSFETAA 

        70         80         90        100        110        120 
NRLGARVIGF SDPKATSSSK GETLKDTIMM VSNYADVIVM RHYLEGAARY ASEVAPVPIV 

       130        140        150        160        170        180 
NAGDGANQHP SQTMLDLYSI YKTQGTLENL NIYLVGDLKY GRTVHSLLMA MRHFNPTFHF 

       190        200        210        220        230        240 
IAPEELKMPE EYKIYCKEHN IKYVEHTDFN EEVIKDADIL YMTRVQRERF TDLMEYERVK 

       250        260        270        280        290        300 
NVYILKAKML ENTRSNLRIL HPLPRVNEIA YDVDDSPKAY YFQQAQNGLY ARQAILCDVL 


GITLQDIL

Q64U74 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