[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=DSM 405 / IFO 15313 / YP-T; PubMed=7516791 [NCBI, ExPASy, EBI, Israel, Japan] Ghim S.Y., Nielsen P., Neuhard J.; "Molecular characterization of pyrimidine biosynthesis genes from the thermophile Bacillus caldolyticus."; Microbiology 140:479-491(1994).

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 2 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

X73308; CAA51737.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I40167; I40167.

3D structure databases

HSSP

P81006; 1GKR. [HSSP ENTRY / PDB]

ModBase

P46538.

Protein family/group databases

MEROPS

M38.972; -.

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_00220; -; 1.
PBIL [Tree]

InterPro

IPR006680; Amidohydro_1.
IPR004722; DHOmult.
IPR002195; Dihydroorotase_CS.
Graphical view of domain structure.

Pfam

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

ProDom

PD000518; DHOase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00857; pyrC_multi; 1.

PROSITE

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

Other

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

Keywords

Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 427`	`427`	`Dihydroorotase.`	`PRO_0000147227`
`METAL`	`60 60`		`Zinc 1 (By similarity).`
`METAL`	`62 62`		`Zinc 1 (By similarity).`
`METAL`	`142 142`		`Zinc 1; via carbamate group (By similarity).`
`METAL`	`142 142`		`Zinc 2; via carbamate group (By similarity).`
`METAL`	`179 179`		`Zinc 2 (By similarity).`
`METAL`	`232 232`		`Zinc 2 (By similarity).`
`METAL`	`305 305`		`Zinc 1 (By similarity).`
`MOD_RES`	`142 142`		`N6-carboxylysine (By similarity).`

Sequence information

Length: 427 AA [This is the length of the unprocessed precursor]

Molecular weight: 46048 Da [This is the MW of the unprocessed precursor]

CRC64: 759A2AA99F733F4E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGVWLKNGMS FNKDGELMRT HIKIEHGTIA AILYEQPLEA NEDVIDVGGR LIVPGLIDLH 

        70         80         90        100        110        120 
VHLREPGGEA KETIETGTLA AAKGGFTTVA AMPNTNPAPD RKEQMEWLQA RIRETARVNV 

       130        140        150        160        170        180 
LPYAAITIGQ KGEELTDFAA LKEAGAFAFT DDGVGVQSAG MMFEAMKQAA ALDMAIVAHC 

       190        200        210        220        230        240 
EDDTLTNGGA VHDGEFARRY GLRGIPSVCE AVHIARDVLL AEAAGCHYHV CHISTKESVR 

       250        260        270        280        290        300 
VVRDAKRAGI RVTAEVTPHH LLLCDEDIPG LDANYKMNPP LRSREDRDAL IEGLLDGTID 

       310        320        330        340        350        360 
FIATDHAPHT AAEKAKGIEA APFGIVGLET AFPLLYTHFV KTGVFTLKQL VDWLTIKPAQ 

       370        380        390        400        410        420 
CFGLKAGRLA VGAPADIAVI DLETEEAIDP ETFASKGKNT PFAGWVCQGW PVMTFVGGTL 


VWEKGRA

P46538 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