NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DSM 20076;
DOI=10.1016/0300-9084(96)88135-1; PubMed=8589056 [NCBI, ExPASy, EBI, Israel, Japan]
Schenk-Groeninger R., Becker J., Brendel M.;
"Cloning, sequencing, and characterizing the Lactobacillus leichmannii pyrC gene encoding dihydroorotase.";
Biochimie 77:265-272(1995).

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

X78999; CAA55633.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T46955; T46955.

3D structure databases

ModBase

P48795.

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.

TIGRFAMs

TIGR00857; pyrC_multi; 1.

PROSITE

PS00482; DIHYDROOROTASE_1; FALSE_NEG.
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_0000147236`
`METAL`	`58 58`		`Zinc 1 (By similarity).`
`METAL`	`60 60`		`Zinc 1 (By similarity).`
`METAL`	`140 140`		`Zinc 1; via carbamate group (By similarity).`
`METAL`	`140 140`		`Zinc 2; via carbamate group (By similarity).`
`METAL`	`177 177`		`Zinc 2 (By similarity).`
`METAL`	`230 230`		`Zinc 2 (By similarity).`
`METAL`	`303 303`		`Zinc 1 (By similarity).`
`MOD_RES`	`140 140`		`N6-carboxylysine (By similarity).`

Sequence information

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

Molecular weight: 46319 Da [This is the MW of the unprocessed precursor]

CRC64: 1AB5BC6163C57E30 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAILLKNGLV YQEGEFIKED VLISGSKIQA IGLDLPEEGA EVYDLKGKLL APGLVDIHEH 

        70         80         90        100        110        120 
YREPGFTYKE TIKTGSEAAS RGGFTTVCTM PNVDPIPDDL ETFEKQVALN EANSCVHLKQ 

       130        140        150        160        170        180 
YGAITEDLTS DKVVDMAALK EAGAFAFSND GHGIQQAGTM YEAMQEAAKV GLAICEHIQD 

       190        200        210        220        230        240 
DSLYHHGVMN AGKKAEELGL PGILGVSESA QLARDLVLAQ ATGVHYHACH VSTKESVELI 

       250        260        270        280        290        300 
RIAKEYGINV TAEATPHHLL LSEEEIDGNN GYYKMNPPLR SKEDQFALIE GMLDGTIDLI 

       310        320        330        340        350        360 
ATDHAPHSRE EKAGDMRKAA FGIIGNETAF ACLYTKFVKS GQMDLSLLLD LMSYQPAKLF 

       370        380        390        400        410        420 
GLDAGVLAPG KEADLAVFDL DHAEKLSEED YLSKGVNTPF TGQEVYGMTA LTFVSGKLVY 


KSKHFAD

P48795 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