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Q8DLB7 (PYRD_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. 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)
EC=1.3.5.2
Alternative name(s):
DHOdehase
Short name=DHOD
Short name=DHODase
Dihydroorotate oxidase
Gene names
Name:pyrD
Ordered Locus Names:tll0579
OrganismThermosynechococcus elongatus (strain BP-1)
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Thermosynechococcus

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor By similarity. HAMAP MF_00225

Catalytic activity

(S)-dihydroorotate + a quinone = orotate + a quinol. HAMAP MF_00225

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_00225

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP MF_00225

Subunit structure

Monomer By similarity. HAMAP MF_00225

Subcellular location

Cell membrane; Peripheral membrane protein By similarity HAMAP MF_00225.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCell membrane
Membrane
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological process'de novo' pyrimidine base biosynthetic process

Inferred from electronic annotation. Source: InterPro

UMP biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_0000148478

Regions

Nucleotide binding78 – 825FMN By similarity
Nucleotide binding335 – 3362FMN By similarity
Region127 – 1315Substrate binding By similarity
Region256 – 2572Substrate binding By similarity

Sites

Active site1921Nucleophile By similarity
Binding site821Substrate By similarity
Binding site1021FMN; via amide nitrogen By similarity
Binding site1561FMN By similarity
Binding site1891FMN By similarity
Binding site1891Substrate By similarity
Binding site1941Substrate By similarity
Binding site2271FMN By similarity
Binding site2551FMN; via carbonyl oxygen By similarity
Binding site2851FMN; via amide nitrogen By similarity
Binding site3141FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DLB7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 6BC5808D98AE83BD

FASTA36439,838
        10         20         30         40         50         60 
MAIDPYRHLL RPLLFSGLQA DPELLHQQFL SLCGWLNQDR SLCTWLRQQL QQWYALSDPR 

        70         80         90        100        110        120 
LERQVWGLRF PNPIGLAAGF DKNGVARSVW SAFGFGFAEL GTVTWHPQPG NPRPRLFRLG 

       130        140        150        160        170        180 
SDRAVINRMG FNNAGAEAMA ASLERSPPAS IPIGINLGKS KITPLAAAKE DYLASFRRLH 

       190        200        210        220        230        240 
PLGDYFVINV SSPNTPGLRD LQAKEQLAPI LETLQSANHP RKPLLLKIAP DLSWEQIAAI 

       250        260        270        280        290        300 
LDLVQAYELA GIVATNTTVA REGLKSQTIP QTGRSPAEEA GGLSGAPLRQ RATAVIRFIH 

       310        320        330        340        350        360 
EQTQGTLPII GVGGIFTPED VIEKLAAGAT LVQLYTGWIY QGPSLLRELL KGLLAAADQE 


TPEK

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed: 12240834] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000039 Genomic DNA. Translation: BAC08131.1.
RefSeqNP_681369.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DLB7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8DLB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1012541.
GenomeReviewsGene locus tll0579 in contig BA000039_GR.
KEGGtel:tll0579.
NMPDRfig|197221.1.peg.578.
PATRIC23926418. VBITheElo119873_0611.

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG351027.
OMAAALNRMG.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycTELO197221:TLL0579-MONOMER.

Family and domain databases

HAMAPMF_00225. DHO_dh_type2.
[Tree]
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.
KOK00226.
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsTIGR01036. PyrD_sub2. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_THEEB
AccessionPrimary (citable) accession number: Q8DLB7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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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