NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
DOI=10.1038/32831; PubMed=9537320 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
Nature 392:353-358(1998).

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

AE000657; AAC06948.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C70370; C70370.

RefSeq

NP_213551.1; -.

3D structure databases

PDB

1XRF; X-ray; 1.65 A; A=1-422.	[ExPASy / RCSB / EBI]
1XRT; X-ray; 1.61 A; A/B=1-422.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1XRF; -.
1XRT; -.

ModBase

O66990.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_806-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_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; 1.
PS00483; DIHYDROOROTASE_2; 1.

BLOCKS

O66990.

Genome annotation databases

1193440; -.

AE000657_GR; aq_806.

aae:aq_806; -.

fig|224324.1.peg.566; -.

Phylogenomic databases

HOGENOM

O66990; -.

Genome annotation databases

CMR

O66990; aq_806.

Other

ProtoNet

O66990.

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`	`1 422`	`422`	`Dihydroorotase.`	`PRO_0000147226`
`METAL`	`61 61`		`Zinc 1 (By similarity).`
`METAL`	`63 63`		`Zinc 1 (By similarity).`
`METAL`	`143 143`		`Zinc 1; via carbamate group (By similarity).`
`METAL`	`143 143`		`Zinc 2; via carbamate group (By similarity).`
`METAL`	`180 180`		`Zinc 2 (By similarity).`
`METAL`	`232 232`		`Zinc 2 (By similarity).`
`METAL`	`305 305`		`Zinc 1 (By similarity).`
`MOD_RES`	`143 143`		`N6-carboxylysine.`
`STRAND`	`3 8`	`6`
`STRAND`	`10 13`	`4`
`HELIX`	`14 16`	`3`
`STRAND`	`18 21`	`4`
`STRAND`	`23 27`	`5`
`STRAND`	`30 37`	`8`
`STRAND`	`41 47`	`7`
`STRAND`	`52 55`	`4`
`STRAND`	`57 62`	`6`
`TURN`	`66 68`	`3`
`TURN`	`70 72`	`3`
`HELIX`	`75 84`	`10`
`STRAND`	`87 92`	`6`
`STRAND`	`96 98`	`3`
`HELIX`	`103 116`	`14`
`STRAND`	`118 123`	`6`
`HELIX`	`129 131`	`3`
`STRAND`	`133 136`	`4`
`HELIX`	`139 145`	`7`
`HELIX`	`160 173`	`14`
`STRAND`	`177 179`	`3`
`HELIX`	`210 224`	`15`
`STRAND`	`228 230`	`3`
`HELIX`	`236 247`	`12`
`STRAND`	`252 256`	`5`
`HELIX`	`258 261`	`4`
`HELIX`	`287 295`	`9`
`HELIX`	`327 329`	`3`
`HELIX`	`330 339`	`10`
`HELIX`	`345 352`	`8`
`HELIX`	`354 359`	`6`
`STRAND`	`375 385`	`11`
`TURN`	`388 390`	`3`
`TURN`	`399 402`	`4`
`STRAND`	`404 414`	`11`
`STRAND`	`417 421`	`5`

Sequence information

Length: 422 AA [This is the length of the unprocessed precursor]

Molecular weight: 46380 Da [This is the MW of the unprocessed precursor]

CRC64: 7004E6A48B0165EB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLKLIVKNGY VIDPSQNLEG EFDILVENGK IKKIDKNILV PEAEIIDAKG LIVCPGFIDI 

        70         80         90        100        110        120 
HVHLRDPGQT YKEDIESGSR CAVAGGFTTI VCMPNTNPPI DNTTVVNYIL QKSKSVGLCR 

       130        140        150        160        170        180 
VLPTGTITKG RKGKEIADFY SLKEAGCVAF TDDGSPVMDS SVMRKALELA SQLGVPIMDH 

       190        200        210        220        230        240 
CEDDKLAYGV INEGEVSALL GLSSRAPEAE EIQIARDGIL AQRTGGHVHI QHVSTKLSLE 

       250        260        270        280        290        300 
IIEFFKEKGV KITCEVNPNH LLFTEREVLN SGANARVNPP LRKKEDRLAL IEGVKRGIID 

       310        320        330        340        350        360 
CFATDHAPHQ TFEKELVEFA MPGIIGLQTA LPSALELYRK GIISLKKLIE MFTINPARII 

       370        380        390        400        410        420 
GVDLGTLKLG SPADITIFDP NKEWILNEET NLSKSRNTPL WGKVLKGKVI YTIKDGKMVY 


KD

O66990 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