[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton B., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.; Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: (S)-dihydroorotate + H₂O = N-carbamoyl-L-aspartate.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 3/6 .
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the DHOase family. Type 1 subfamily.

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

CP000783; ABU77535.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001438371.1; -.

3D structure databases

ModBase

A7MG30.

Ontologies

GO:0004151;	Molecular function: dihydroorotase activity (inferred from electronic annotation from HAMAP).
GO:0008270;	Molecular function: zinc ion binding (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_00219; -; 1.
PBIL [Tree]

InterPro

IPR006680; Amidohydro_1.
IPR004721; DHOdimr.
IPR002195; Dihydroorotase_CS.
Graphical view of domain structure.

Pfam

PF01979; Amidohydro_1; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001237; DHOdimr; 1.

TIGRFAMs

TIGR00856; pyrC_dimer; 1.

PROSITE

PS00482; DIHYDROOROTASE_1; 1.
PS00483; DIHYDROOROTASE_2; 1.

Genome annotation databases

GeneID

5551627; -.

GenomeReviews

CP000783_GR; ESA_02286.

KEGG

esa:ESA_02286; -.

CMR

A7MG30; ESA_02286.

Other

UniRef

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

Keywords

Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 348`	`348`	`Dihydroorotase.`	`PRO_1000024012`
`METAL`	`17 17`		`Zinc 1 (By similarity).`
`METAL`	`19 19`		`Zinc 1 (By similarity).`
`METAL`	`103 103`		`Zinc 1; via carbamate group (By similarity).`
`METAL`	`103 103`		`Zinc 2; via carbamate group (By similarity).`
`METAL`	`140 140`		`Zinc 2 (By similarity).`
`METAL`	`178 178`		`Zinc 2 (By similarity).`
`METAL`	`251 251`		`Zinc 1 (By similarity).`
`MOD_RES`	`103 103`		`N6-carboxylysine (By similarity).`

Sequence information

Length: 348 AA [This is the length of the unprocessed precursor]

Molecular weight: 38591 Da [This is the MW of the unprocessed precursor]

CRC64: 7E2E81788657B6B2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAQPQVLTI RRPDDWHVHL RDGDMLKTVV PYTSETYGRA IVMPNLAPPV TTVEAAIAYR 

        70         80         90        100        110        120 
QRILDAVPEH HAFEPLMTCY LTDTLDADEL ERGFQQGVFT AAKLYPANAT TNSSHGVTSV 

       130        140        150        160        170        180 
DNIMTVLERM EKLGMPLLVH GEVTHSEVDI FDREARFIET VMEPLRKRLQ GLKVVFEHIT 

       190        200        210        220        230        240 
TKDAADYVRE GNSLLGATIT PQHLMFNRNH MLAGGIRPHL YCLPILKRNV HQQALRELVA 

       250        260        270        280        290        300 
SGCERVFLGT DSAPHARHRK ETSCGCAGCF NAPSALGAYA TVFEEMNALA HFEAFASLNG 

       310        320        330        340 
PGFYGLPVNE GTVTLVREES VMPETIAIAD DTLVPFLAGE AVRWTVKR

A7MG30 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