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Protein

Dihydroorotase

Gene

pyrC

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

Functioni

Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.UniRule annotation2 Publications

Catalytic activityi

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.UniRule annotation2 Publications

Cofactori

Zn2+UniRule annotation4 PublicationsNote: Binds 1 Zn2+ ion per subunit (PubMed:15381710, PubMed:15826652, PubMed:19128030, PubMed:24314009). Fully functional with a mononuclear metal center. Does not require a second metal for activity, although the conservation of the second metal-binding site during evolution leaves open the possibility that a second ion might bind in vivo (PubMed:24314009).4 Publications

Enzyme regulationi

The monomer has very low activity by itself. Activated several thousandfold by formation of a complex with PyrB aspartate carbamoyltransferase (ATCase).1 Publication

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.UniRule annotationCurated
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; via tele nitrogenCombined sources3 Publications1
Metal bindingi63Zinc; via tele nitrogenCombined sources3 Publications1
Binding sitei95SubstrateUniRule annotationCombined sources1 Publication1
Metal bindingi153ZincCombined sources3 Publications1
Binding sitei278Substrate; via amide nitrogen and carbonyl oxygenUniRule annotationCombined sources1 Publication1
Active sitei305UniRule annotation1
Metal bindingi305ZincCombined sources2 Publications1
Binding sitei309SubstrateUniRule annotationCombined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processPyrimidine biosynthesis
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.2.3. 396.
SABIO-RKiO66990.
UniPathwayiUPA00070; UER00117.

Names & Taxonomyi

Protein namesi
Recommended name:
DihydroorotaseUniRule annotation (EC:3.5.2.3UniRule annotation2 Publications)
Short name:
DHOaseUniRule annotation
Gene namesi
Name:pyrCUniRule annotation
Ordered Locus Names:aq_806
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi180H → A: Does not affect activity. 1 Publication1
Mutagenesisi232H → A: Does not affect activity. 1 Publication1

PTM / Processingi

Molecule processing

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

Interactioni

Subunit structurei

Monomer. Forms a 1:1 stoichiometric complex with PyrB. The complex exists as an equilibrium mixture of heterohexamers, composed of 3 PyrC and 3 PyrB subunits, and dodecamers. The complex has both DHOase and ATCase activities.2 Publications

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni63 – 65Substrate bindingUniRule annotationCombined sources1 Publication3
Regioni322 – 323Substrate bindingUniRule annotationCombined sources1 Publication2

Sequence similaritiesi

Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105CD3. Bacteria.
COG0044. LUCA.
HOGENOMiHOG000219142.
InParanoidiO66990.
KOiK01465.
OMAiEYVKAFD.
OrthoDBiPOG091H02CH.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
HAMAPiMF_00220_B. PyrC_classI_B. 1 hit.
InterProiView protein in InterPro
IPR006680. Amidohydro-rel.
IPR004722. DHOase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
PfamiView protein in Pfam
PF01979. Amidohydro_1. 1 hit.
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR00857. pyrC_multi. 1 hit.
PROSITEiView protein in PROSITE
PS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.

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.
PATRICifig|224324.8.peg.636.

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.

Entry informationi

Entry nameiPYRC_AQUAE
AccessioniPrimary (citable) accession number: O66990
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: July 5, 2017
This is version 125 of the entry and version 1 of the sequence. See 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