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Protein

Dihydroorotase

Gene

pyrC

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain, C-terminal section (carB2), Carbamoyl-phosphate synthase large chain, N-terminal section (carB1), Carbamoyl-phosphate synthase small chain (carA)
  2. Aspartate carbamoyltransferase (pyrB)
  3. Dihydroorotase (pyrC)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi61 – 611Zinc 1By similarity
Metal bindingi63 – 631Zinc 1By similarity
Metal bindingi143 – 1431Zinc 1; via carbamate groupBy similarity
Metal bindingi143 – 1431Zinc 2; via carbamate groupBy similarity
Metal bindingi180 – 1801Zinc 2By similarity
Metal bindingi232 – 2321Zinc 2By similarity
Metal bindingi305 – 3051Zinc 1By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-576-MONOMER.
BRENDAi3.5.2.3. 396.
SABIO-RKO66990.
UniPathwayiUPA00070; UER00117.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroorotase (EC:3.5.2.3)
Short name:
DHOase
Gene namesi
Name:pyrC
Ordered Locus Names:aq_806
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422DihydroorotasePRO_0000147226Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei143 – 1431N6-carboxylysineBy similarity

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi224324.aq_806.

Structurei

Secondary structure

1
422
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Beta strandi10 – 134Combined sources
Helixi14 – 163Combined sources
Beta strandi18 – 214Combined sources
Beta strandi23 – 275Combined sources
Beta strandi30 – 378Combined sources
Beta strandi41 – 477Combined sources
Beta strandi51 – 555Combined sources
Beta strandi57 – 626Combined sources
Turni66 – 683Combined sources
Turni70 – 723Combined sources
Helixi75 – 8410Combined sources
Beta strandi87 – 926Combined sources
Beta strandi96 – 983Combined sources
Helixi103 – 11614Combined sources
Beta strandi118 – 1236Combined sources
Helixi129 – 1313Combined sources
Beta strandi133 – 1364Combined sources
Helixi139 – 1457Combined sources
Helixi160 – 17314Combined sources
Beta strandi176 – 1794Combined sources
Helixi183 – 1864Combined sources
Beta strandi189 – 1946Combined sources
Helixi195 – 2006Combined sources
Helixi210 – 22415Combined sources
Beta strandi227 – 2315Combined sources
Helixi236 – 24712Combined sources
Beta strandi252 – 2565Combined sources
Helixi258 – 2614Combined sources
Helixi267 – 2715Combined sources
Helixi272 – 2754Combined sources
Helixi287 – 2959Combined sources
Helixi311 – 3133Combined sources
Beta strandi314 – 3163Combined sources
Helixi317 – 3193Combined sources
Helixi327 – 3293Combined sources
Helixi330 – 33910Combined sources
Helixi345 – 3528Combined sources
Helixi354 – 3607Combined sources
Beta strandi375 – 38511Combined sources
Turni388 – 3903Combined sources
Turni399 – 4024Combined sources
Beta strandi404 – 41411Combined sources
Beta strandi417 – 4215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XRFX-ray1.65A1-422[»]
1XRTX-ray1.61A/B1-422[»]
3D6NX-ray2.30A1-422[»]
4BJHX-ray2.20A1-422[»]
ProteinModelPortaliO66990.
SMRiO66990. Positions 1-422.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO66990.

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family. Type 2 subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105CD3. Bacteria.
COG0044. LUCA.
HOGENOMiHOG000219142.
InParanoidiO66990.
KOiK01465.
OMAiAFGEIFM.
OrthoDBiEOG6KHFW6.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_00220_B. PyrC_type2_B.
InterProiIPR006680. Amidohydro-rel.
IPR004722. DHOase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR00857. pyrC_multi. 1 hit.
PROSITEiPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O66990-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKLIVKNGY VIDPSQNLEG EFDILVENGK IKKIDKNILV PEAEIIDAKG
60 70 80 90 100
LIVCPGFIDI HVHLRDPGQT YKEDIESGSR CAVAGGFTTI VCMPNTNPPI
110 120 130 140 150
DNTTVVNYIL QKSKSVGLCR VLPTGTITKG RKGKEIADFY SLKEAGCVAF
160 170 180 190 200
TDDGSPVMDS SVMRKALELA SQLGVPIMDH CEDDKLAYGV INEGEVSALL
210 220 230 240 250
GLSSRAPEAE EIQIARDGIL AQRTGGHVHI QHVSTKLSLE IIEFFKEKGV
260 270 280 290 300
KITCEVNPNH LLFTEREVLN SGANARVNPP LRKKEDRLAL IEGVKRGIID
310 320 330 340 350
CFATDHAPHQ TFEKELVEFA MPGIIGLQTA LPSALELYRK GIISLKKLIE
360 370 380 390 400
MFTINPARII GVDLGTLKLG SPADITIFDP NKEWILNEET NLSKSRNTPL
410 420
WGKVLKGKVI YTIKDGKMVY KD
Length:422
Mass (Da):46,380
Last modified:August 1, 1998 - v1
Checksum:i7004E6A48B0165EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06948.1.
PIRiC70370.
RefSeqiNP_213551.1. NC_000918.1.
WP_010880489.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC06948; AAC06948; aq_806.
GeneIDi1193440.
KEGGiaae:aq_806.
PATRICi20959012. VBIAquAeo85532_0636.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06948.1.
PIRiC70370.
RefSeqiNP_213551.1. NC_000918.1.
WP_010880489.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XRFX-ray1.65A1-422[»]
1XRTX-ray1.61A/B1-422[»]
3D6NX-ray2.30A1-422[»]
4BJHX-ray2.20A1-422[»]
ProteinModelPortaliO66990.
SMRiO66990. Positions 1-422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_806.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC06948; AAC06948; aq_806.
GeneIDi1193440.
KEGGiaae:aq_806.
PATRICi20959012. VBIAquAeo85532_0636.

Phylogenomic databases

eggNOGiENOG4105CD3. Bacteria.
COG0044. LUCA.
HOGENOMiHOG000219142.
InParanoidiO66990.
KOiK01465.
OMAiAFGEIFM.
OrthoDBiEOG6KHFW6.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00117.
BioCyciAAEO224324:GJBH-576-MONOMER.
BRENDAi3.5.2.3. 396.
SABIO-RKO66990.

Miscellaneous databases

EvolutionaryTraceiO66990.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_00220_B. PyrC_type2_B.
InterProiIPR006680. Amidohydro-rel.
IPR004722. DHOase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR00857. pyrC_multi. 1 hit.
PROSITEiPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VF5.

Entry informationi

Entry nameiPYRC_AQUAE
AccessioniPrimary (citable) accession number: O66990
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.