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Protein

Dihydroorotate dehydrogenase (quinone)

Gene

pyrD

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.By similarity

Catalytic activityi

(S)-dihydroorotate + a quinone = orotate + a quinol.

Cofactori

FMNBy similarityNote: Binds 1 FMN per subunit.By similarity

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes orotate from (S)-dihydroorotate (quinone route).
Proteins known to be involved in this subpathway in this organism are:
  1. Dihydroorotate dehydrogenase (quinone) (pyrD)
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 orotate from (S)-dihydroorotate (quinone route), the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei70SubstrateBy similarity1
Binding sitei90FMN; via amide nitrogenBy similarity1
Binding sitei143FMNBy similarity1
Binding sitei176FMNBy similarity1
Binding sitei176SubstrateBy similarity1
Active sitei179NucleophileBy similarity1
Binding sitei181SubstrateBy similarity1
Binding sitei212FMNBy similarity1
Binding sitei240FMN; via carbonyl oxygenBy similarity1
Binding sitei264FMN; via amide nitrogenBy similarity1
Binding sitei293FMN; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi66 – 70FMNBy similarity5
Nucleotide bindingi314 – 315FMNBy similarity2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

UniPathwayiUPA00070; UER00946.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroorotate dehydrogenase (quinone) (EC:1.3.5.2)
Alternative name(s):
DHOdehase
Short name:
DHOD
Short name:
DHODase
Dihydroorotate oxidase
Gene namesi
Name:pyrD
Ordered Locus Names:ML1293
ORF Names:B2126_F3_143
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML1293.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001484551 – 356Dihydroorotate dehydrogenase (quinone)Add BLAST356

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi272631.ML1293.

Structurei

3D structure databases

ProteinModelPortaliP46727.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni115 – 119Substrate bindingBy similarity5
Regioni241 – 242Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107QYT. Bacteria.
COG0167. LUCA.
HOGENOMiHOG000225103.
OMAiERIKMGA.
OrthoDBiPOG091H018H.

Family and domain databases

CDDicd04738. DHOD_2_like. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00225. DHO_dh_type2. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01036. pyrD_sub2. 1 hit.
PROSITEiPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46727-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRVVRRLLF LTPPERIHTL VFAMLRCVTS IAVLRRLLRW VLGPTDPVLA
60 70 80 90 100
STVFGVRFPG PLGLAAGFDK DGMGLLAWGA LGFGYAEVGT VTAYPQPGNP
110 120 130 140 150
APRMFRLPAD RALLNRMGFN NNGAGALAIQ LAHHRPEVPI GVNISKTKAT
160 170 180 190 200
PASHTVDDYR ASARLVGPLA SYLVVNVSSP NTPGLRDLQA VESLRAILLG
210 220 230 240 250
VLAETSVPVL VKIAPDISDS EIDDITDLAV ELRLAGIVAT NTTVSRDCLV
260 270 280 290 300
TPGIDALGAG GISGPPVARR AVEVLRRLYG RVGDRLVLIS VGGIETADDA
310 320 330 340 350
WDRITAGASL LQGYTGFIYG GGFWPKHIHD GIARRLHDGG FASLRDAVGS

ATAKSE
Length:356
Mass (Da):37,749
Last modified:April 27, 2001 - v3
Checksum:i9CB10455ADEBC731
GO

Sequence cautioni

The sequence AAA17221 differs from that shown. Reason: Frameshift at position 40.Curated
The sequence CAC31674 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00017 Genomic DNA. Translation: AAA17221.1. Frameshift.
AL583921 Genomic DNA. Translation: CAC31674.1. Different initiation.
PIRiG87070.
S72881.
RefSeqiWP_010908249.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC31674; CAC31674; CAC31674.
PATRICi18054916. VBIMycLep78757_2395.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00017 Genomic DNA. Translation: AAA17221.1. Frameshift.
AL583921 Genomic DNA. Translation: CAC31674.1. Different initiation.
PIRiG87070.
S72881.
RefSeqiWP_010908249.1. NC_002677.1.

3D structure databases

ProteinModelPortaliP46727.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML1293.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC31674; CAC31674; CAC31674.
PATRICi18054916. VBIMycLep78757_2395.

Organism-specific databases

LepromaiML1293.

Phylogenomic databases

eggNOGiENOG4107QYT. Bacteria.
COG0167. LUCA.
HOGENOMiHOG000225103.
OMAiERIKMGA.
OrthoDBiPOG091H018H.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00946.

Family and domain databases

CDDicd04738. DHOD_2_like. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00225. DHO_dh_type2. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01036. pyrD_sub2. 1 hit.
PROSITEiPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPYRD_MYCLE
AccessioniPrimary (citable) accession number: P46727
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 27, 2001
Last modified: November 30, 2016
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.