[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Rasko D.A., Rosovitz M.J., Kaper J.B., Nataro J.P., Myers G.S.A., Seshadri R., Cer R.Z., Ravel J.; Submitted (AUG-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

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Cross-references

Sequence databases

EMBL

CP000802; ABV05524.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001457907.1; -.

3D structure databases

PDB

2Z27; X-ray; 1.87 A; A=2-348.

[ExPASy / RCSB / EBI]

PDBsum

2Z27; -.

ModBase

A7ZZ20.

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

A7ZZ20.

Genome annotation databases

GeneID

5594408; -.

GenomeReviews

CP000802_GR; EcHS_A1185.

KEGG

ecx:EcHS_A1185; -.

CMR

A7ZZ20; EcHS_A1185.

Other

ProtoNet

A7ZZ20.

UniRef

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

Keywords

3D-structure; Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 348`	`348`	`Dihydroorotase.`	`PRO_1000058649`
`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: 38813 Da [This is the MW of the unprocessed precursor]

CRC64: 2EFEA36B232519A0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR 

        70         80         90        100        110        120 
QRILDAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEGVFT AAKLYPANAT TNSSHGVTSV 

       130        140        150        160        170        180 
DAIMPVLERM EKIGMPLLVH GEVTHADIDI FDREARFIES VMEPLRQRLT ALKVVFEHIT 

       190        200        210        220        230        240 
TKDAADYVRD GNERLAATIT PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVA 

       250        260        270        280        290        300 
SGFNRVFLGT DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG 

       310        320        330        340 
PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ

A7ZZ20 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