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Protein

Dihydroorotate dehydrogenase (quinone)

Gene

pyrD

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
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.UniRule annotation

Catalytic activityi

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

Cofactori

FMNUniRule annotationNote: Binds 1 FMN per subunit.UniRule annotation

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).UniRule annotation
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 sitei70SubstrateUniRule annotation1
Binding sitei90FMN; via amide nitrogenUniRule annotation1
Binding sitei143FMNUniRule annotation1
Binding sitei176FMNUniRule annotation1
Binding sitei176SubstrateUniRule annotation1
Active sitei179NucleophileUniRule annotation1
Binding sitei181SubstrateUniRule annotation1
Binding sitei212FMNUniRule annotation1
Binding sitei240FMN; via carbonyl oxygenUniRule annotation1
Binding sitei264FMN; via amide nitrogenUniRule annotation1
Binding sitei293FMN; via amide nitrogenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi66 – 70FMNUniRule annotation5
Nucleotide bindingi314 – 315FMNUniRule annotation2

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)UniRule annotation (EC:1.3.5.2UniRule annotation)
Alternative name(s):
DHOdehaseUniRule annotation
Short name:
DHODUniRule annotation
Short name:
DHODaseUniRule annotation
Dihydroorotate oxidaseUniRule annotation
Gene namesi
Name:pyrDUniRule annotation
Ordered Locus Names:MMAR_3120
OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)
Taxonomic identifieri216594 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000001190 Componenti: Chromosome

Subcellular locationi

  • Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001002721 – 360Dihydroorotate dehydrogenase (quinone)Add BLAST360

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi216594.MMAR_3120.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni115 – 119Substrate bindingUniRule annotation5
Regioni241 – 242Substrate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QYT. Bacteria.
COG0167. LUCA.
HOGENOMiHOG000225103.
KOiK00254.
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.

B2HFZ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYGLLRRLLF LLPPERVHKL VFAVLRGATA ATPVRRMLTR WLGPTDPVLA
60 70 80 90 100
STVFGVRFPG PLGLAAGFDK DGTGLDTWAA MGFGYAEVGT VTAHPQPGNP
110 120 130 140 150
APRLFRLPED RALLNRMGFN NHGAGALAIR LARHHPEVPV GVNIGKTKTT
160 170 180 190 200
PADQAVDDYR ASARLVGPLA SYLVVNVSSP NTPGLRDLQA VESLRPILAA
210 220 230 240 250
VLAETSTPVL VKIAPDLSDS DVDEVADLAV ELGLAGIVAT NTTVSRDGLL
260 270 280 290 300
TPGVGQLGAG GISGPPVAER SLEVLCRLYQ RVGDRLTLIS VGGIETAEDA
310 320 330 340 350
WDRITAGASL LQGYTGFIYG GGLWSKHIHD GIARRLHQGG FGSLHEAVGS
360
NAAERGRPPS
Length:360
Mass (Da):37,877
Last modified:June 10, 2008 - v1
Checksum:i5F1D5CBE07F21B7D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC41555.1.
RefSeqiWP_012394800.1. NC_010612.1.

Genome annotation databases

EnsemblBacteriaiACC41555; ACC41555; MMAR_3120.
KEGGimmi:MMAR_3120.
PATRICi18067313. VBIMycMar75906_3337.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC41555.1.
RefSeqiWP_012394800.1. NC_010612.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi216594.MMAR_3120.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACC41555; ACC41555; MMAR_3120.
KEGGimmi:MMAR_3120.
PATRICi18067313. VBIMycMar75906_3337.

Phylogenomic databases

eggNOGiENOG4107QYT. Bacteria.
COG0167. LUCA.
HOGENOMiHOG000225103.
KOiK00254.
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_MYCMM
AccessioniPrimary (citable) accession number: B2HFZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: November 2, 2016
This is version 56 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

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.