NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1007/s00203-004-0742-9; PubMed=15551059 [NCBI, ExPASy, EBI, Israel, Japan]
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.;
"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1.";
Arch. Microbiol. 183:27-36(2005).

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

CR555306; CAI07077.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_157978.1; -.

3D structure databases

ModBase

Q5P6I4.

Enzyme and pathway databases

BioCyc

ASP76114:EBA1759-MON; -.

Ontologies

GO:0016597;	Molecular function: amino acid binding (inferred from electronic annotation from InterPro).
GO:0004070;	Molecular function: aspartate carbamoyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0006207;	Biological process: 'de novo' pyrimidine base biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006520;	Biological process: amino acid 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_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.

ProtoNet

Q5P6I4.

Genome annotation databases

GeneID

3180228; -.

GenomeReviews

CR555306_GR; AZOSEA09520.

KEGG

eba:ebA1759; -.

NMPDR

fig|76114.4.peg.393; -.

Phylogenomic databases

HOGENOM

Q5P6I4; -.

Genome annotation databases

CMR

Q5P6I4; AZOSEA09520.

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`	`1 323`	`323`		`Aspartate carbamoyltransferase.`	`PRO_0000113088`

Sequence information

Length: 323 AA [This is the length of the unprocessed precursor]

Molecular weight: 35268 Da [This is the MW of the unprocessed precursor]

CRC64: 5901B825CE352FBA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRNPQLNKHG ELQHLLTIDG LPRSILTAIL DTAAPFTEVA EREVKKLPLL RGKSIFNLFF 

        70         80         90        100        110        120 
ENSTRTRTTF EIAAKRLSAD VVNLNVSTSS AAKGESLLDT VDNLSAMQAD MFVVRHAASG 

       130        140        150        160        170        180 
APFLIAQHLF ATGRDHIHVV NAGDGRHAHP TQGLLDMYTI RHFKRDFTNL TIAIVGDVLH 

       190        200        210        220        230        240 
SRVARSQIGA LTTLGVPEVR VIGPKTLLPT DVERLGVRVF HDIREGLRGV DVVMMLRLQN 

       250        260        270        280        290        300 
ERMNGALLPT PQEFYKVWGL TAEKLALAKP DAIVMHPGPM NRGVEIDSSV ADGAQAVILP 

       310        320 
QVTFGIAVRM AVMSMLAGQQ GSK

Q5P6I4 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