[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.; Submitted (SEP-2006) 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

CP000647; ABR76507.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001334737.1; -.

3D structure databases

ModBase

A6T7D6.

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; FALSE_NEG.
PS00483; DIHYDROOROTASE_2; 1.

BLOCKS

A6T7D6.

Genome annotation databases

GeneID

5341622; -.

GenomeReviews

CP000647_GR; KPN78578_10460.

KEGG

kpn:KPN_01074; -.

CMR

A6T7D6; KPN78578_10460.

Other

ProtoNet

A6T7D6.

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_1000024020`
`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: 38821 Da [This is the MW of the unprocessed precursor]

CRC64: 2B841BB50B30506D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAQSQVLKI RRPDDWHIHL RDDDMLKTVV PYTSEFYGRA IVMPNLVPPV TTVAAAIAYR 

        70         80         90        100        110        120 
QRIMDAVPAG HDFTPLMTCY LTDSLDPAEL ERGFNEGVFT AAKLYPANAT TNSSHGVTST 

       130        140        150        160        170        180 
DAIMPVLERM EKLGMPLLVH GEVTHAEIDI FDREARFIET VMEPLRQRLP GLKVVFEHIT 

       190        200        210        220        230        240 
TKDAAEYVRD GNELLAATIT PQHLMFNRNH MLVGGIRPHL YCLPVLKRNI HQQALRELVA 

       250        260        270        280        290        300 
SGFSRAFLGT DSAPHARHRK EASCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSLNG 

       310        320        330        340 
PRFYGLPVNE SYVELVREET TVVDSIALPN DTLVPFLAGE TVRWTVKK

A6T7D6 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