[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravits S., Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.; Submitted (SEP-2005) 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

CP000157; ABC62662.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_457459.1; -.

3D structure databases

ModBase

Q2NCC9.

Enzyme and pathway databases

BioCyc

ELIT314225:ELI_02850-MON; -.

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.

BLOCKS

Q2NCC9.

Genome annotation databases

GeneID

3869096; -.

GenomeReviews

CP000157_GR; ELI_02850.

KEGG

eli:ELI_02850; -.

NMPDR

fig|314225.3.peg.2511; -.

CMR

Q2NCC9; ELI_02850.

Other

ProtoNet

Q2NCC9.

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`	`1 344`	`344`	`Dihydroorotase.`	`PRO_1000024014`
`METAL`	`14 14`		`Zinc 1 (By similarity).`
`METAL`	`16 16`		`Zinc 1 (By similarity).`
`METAL`	`100 100`		`Zinc 1 (via carbamate group) (By similarity).`
`METAL`	`100 100`		`Zinc 2 (via carbamate group) (By similarity).`
`METAL`	`137 137`		`Zinc 2 (By similarity).`
`METAL`	`175 175`		`Zinc 2 (By similarity).`
`METAL`	`248 248`		`Zinc 1 (By similarity).`
`MOD_RES`	`100 100`		`N6-carboxylysine (By similarity).`

Sequence information

Length: 344 AA [This is the length of the unprocessed precursor]

Molecular weight: 37576 Da [This is the MW of the unprocessed precursor]

CRC64: A0E7989C2B46FD83 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTETLTIRRP DDWHLHFRDG AMMRGVVPYT ARQFARAIVM PNLTPPVTTT ALGAAYRERI 

        70         80         90        100        110        120 
LAAVPEGVDF RPLMTAYLTD ETDADDLIDG YTHGVFTAAK LYPANATTNS ASGVTDVEAL 

       130        140        150        160        170        180 
YPVFERMAAA GMVLCIHGEV TDADVDVFDR EKEFIERTMA PLHAAIPALK IAFEHITTSD 

       190        200        210        220        230        240 
AVDFVVGAND NIGATITPQH LHINRNAMLV GGIQPHNYCL PVAKRETHRL ALRQAATSGP 

       250        260        270        280        290        300 
PKFFLGTDSA PHEKHTKESA CGCAGIFGAP YALESYLAVF EEEDALDKFE AFASLNGPAF 

       310        320        330        340 
YGLPVNDETI TLERVPHNVP DSLETEGGKV VPFHAGQELN WRLK

Q2NCC9 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