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Q6SZS6 (PYRD2_KLUMA) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotate dehydrogenase (quinone), mitochondrial
Short name=DHOD
Short name=DHODase
Short name=DHOdehase
EC=1.3.5.2
Alternative name(s):
Dihydroorotate oxidase
Gene names
Name:URA9
OrganismKluyveromyces marxianus (Yeast) (Candida kefyr)
Taxonomic identifier4911 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.

Subcellular location

Mitochondrion inner membrane By similarity; Single-pass membrane protein Potential.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 446Dihydroorotate dehydrogenase (quinone), mitochondrialPRO_0000029894

Regions

Transmembrane42 – 5817Helical; Potential
Nucleotide binding124 – 1285FMN By similarity
Nucleotide binding408 – 4092FMN By similarity
Region173 – 1775Substrate binding By similarity
Region252 – 2576Substrate binding By similarity
Region332 – 3332Substrate binding By similarity

Sites

Active site2551Nucleophile By similarity
Binding site1281Substrate By similarity
Binding site1481FMN By similarity
Binding site2221FMN By similarity
Binding site2521FMN By similarity
Binding site3031FMN By similarity
Binding site3311FMN; via carbonyl oxygen By similarity
Binding site3571FMN; via amide nitrogen By similarity
Binding site3871FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6SZS6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: EE025A136B2DA82B

FASTA44648,346
        10         20         30         40         50         60 
MKYSFVSLLQ RGSIGSKQFI FFAKNEMSPL KAGVPGAKFL KYTVGFTLGT LAGFYLTNSR 

        70         80         90        100        110        120 
SAIHEYVSCP TVRLLTPDAE AGHKLGIWLL KYGLAPRLWF DKDEELLHVN VFGKTLTNPV 

       130        140        150        160        170        180 
GCAAGLDKDG EAIDGIFAGG FGYVEIGSVT PLPQPGNPKP RFFRLPMDEA VINRYGFNSS 

       190        200        210        220        230        240 
GHDSVVKNLQ NRVSRFINSY FCNDINAVDN LSLYQNKLLG INLGKNKNGD EVQDYLKGVE 

       250        260        270        280        290        300 
KFQKYADVLV INVSSPNTPG LRGLQKESIL TNLLSQVVAK RDSLVSSGNV LGAKTHRPPV 

       310        320        330        340        350        360 
LVKVAPDLEE EEIKAIAEAA KKSKVDGIIV SNTTIQRPAS LITEDKNLVA QAGGLSGKPL 

       370        380        390        400        410        420 
KPLSLKALKT MAHYTKGSGL VLVGCGGISS GADAIEFAKA GATMVELYTC YAYRGPGLIA 

       430        440 
RVKDEITEQL KRENKTWSQI IGEDVK

« Hide

References

[1]"Contribution of horizontal gene transfer to the evolution of Saccharomyces cerevisiae."
Hall C.R., Brachat S., Dietrich F.S.
Eukaryot. Cell 4:1102-1115(2005) [PubMed: 15947202] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 200963 / CBS 712 / NBRC 10005 / NRRL Y-8281 / HA 63.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY444339 Genomic DNA. Translation: AAR17522.1.

3D structure databases

ProteinModelPortalQ6SZS6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR01036. PyrD_sub2. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD2_KLUMA
AccessionPrimary (citable) accession number: Q6SZS6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
Last modified: September 21, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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