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Protein

Dihydroorotase

Gene

pyrC

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 3 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)DescriptionActionsGraphical viewLength
Metal bindingi61Zinc 1By similarity1
Metal bindingi63Zinc 1By similarity1
Metal bindingi143Zinc 1; via carbamate groupBy similarity1
Metal bindingi143Zinc 2; via carbamate groupBy similarity1
Metal bindingi180Zinc 2By similarity1
Metal bindingi232Zinc 2By similarity1
Metal bindingi305Zinc 1By similarity1

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

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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001472261 – 422DihydroorotaseAdd BLAST422

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei143N6-carboxylysineBy similarity1

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi224324.aq_806.

Structurei

Secondary structure

1422
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Beta strandi10 – 13Combined sources4
Helixi14 – 16Combined sources3
Beta strandi18 – 21Combined sources4
Beta strandi23 – 27Combined sources5
Beta strandi30 – 37Combined sources8
Beta strandi41 – 47Combined sources7
Beta strandi51 – 55Combined sources5
Beta strandi57 – 62Combined sources6
Turni66 – 68Combined sources3
Turni70 – 72Combined sources3
Helixi75 – 84Combined sources10
Beta strandi87 – 92Combined sources6
Beta strandi96 – 98Combined sources3
Helixi103 – 116Combined sources14
Beta strandi118 – 123Combined sources6
Helixi129 – 131Combined sources3
Beta strandi133 – 136Combined sources4
Helixi139 – 145Combined sources7
Helixi160 – 173Combined sources14
Beta strandi176 – 179Combined sources4
Helixi183 – 186Combined sources4
Beta strandi189 – 194Combined sources6
Helixi195 – 200Combined sources6
Helixi210 – 224Combined sources15
Beta strandi227 – 231Combined sources5
Helixi236 – 247Combined sources12
Beta strandi252 – 256Combined sources5
Helixi258 – 261Combined sources4
Helixi267 – 271Combined sources5
Helixi272 – 275Combined sources4
Helixi287 – 295Combined sources9
Helixi311 – 313Combined sources3
Beta strandi314 – 316Combined sources3
Helixi317 – 319Combined sources3
Helixi327 – 329Combined sources3
Helixi330 – 339Combined sources10
Helixi345 – 352Combined sources8
Helixi354 – 360Combined sources7
Beta strandi375 – 385Combined sources11
Turni388 – 390Combined sources3
Turni399 – 402Combined sources4
Beta strandi404 – 414Combined sources11
Beta strandi417 – 421Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XRFX-ray1.65A1-422[»]
1XRTX-ray1.61A/B1-422[»]
3D6NX-ray2.30A1-422[»]
4BJHX-ray2.20A1-422[»]
ProteinModelPortaliO66990.
SMRiO66990.
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.
OMAiSYVETVI.
OrthoDBiPOG091H02CH.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_00220_B. PyrC_type2_B. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XRFX-ray1.65A1-422[»]
1XRTX-ray1.61A/B1-422[»]
3D6NX-ray2.30A1-422[»]
4BJHX-ray2.20A1-422[»]
ProteinModelPortaliO66990.
SMRiO66990.
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.
OMAiSYVETVI.
OrthoDBiPOG091H02CH.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00117.
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. 1 hit.
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...

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 30, 2016
This is version 120 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.