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B0CA74 (PYRD_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:AM1_1640
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesAcaryochloris

Protein attributes

Sequence length374 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
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 – 374374Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000078153

Regions

Nucleotide binding78 – 825FMN By similarity
Nucleotide binding337 – 3382FMN By similarity
Region127 – 1315Substrate binding By similarity
Region259 – 2602Substrate binding By similarity

Sites

Active site1951Nucleophile By similarity
Binding site821Substrate By similarity
Binding site1021FMN; via amide nitrogen By similarity
Binding site1591FMN By similarity
Binding site1921FMN By similarity
Binding site1921Substrate By similarity
Binding site1971Substrate By similarity
Binding site2301FMN By similarity
Binding site2581FMN; via carbonyl oxygen By similarity
Binding site2871FMN; via amide nitrogen By similarity
Binding site3161FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B0CA74 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 32BF33B7ACCA9F72

FASTA37440,679
        10         20         30         40         50         60 
MDLYQQGLQP LLFSALKADP ETVHRQLMRT CAWLDRNVDQ GLAQGLQRRL ASSLQVEDPR 

        70         80         90        100        110        120 
LSQSLWGLSF ANPIGLAAGF DKDGVATNIW PRFGFGFAEV GTVTFHAQPG NPQPRLFRLP 

       130        140        150        160        170        180 
EDQAALNRMG FNNQGAAAMA KVIAASLDRQ ARSYPLGINL GKSKVTPLEQ AVADYVGSFQ 

       190        200        210        220        230        240 
LLKTYGDYFV VNVSSPNTPG LRSLQAVEQL APILAGLQAE NTEGKPLLVK IAPDLEWKDI 

       250        260        270        280        290        300 
AAIVDLAQVH QLAGIIATNT TIRRDLKTER IAATGNVPSE EAGGISGAPV RSRSTDVIRF 

       310        320        330        340        350        360 
IHKQTQGQLP IIGVGGIFTA EDAWEKLCAG ASLLQVYTGW VYEGPWMVRR ILEGLLVKMQ 

       370 
EEGIQQLSEI VGQK 

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000828 Genomic DNA. Translation: ABW26661.1.
RefSeqYP_001515975.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0CA74.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0CA74.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5680456.
GenomeReviewsGene locus AM1_1640 in contig CP000828_GR.
KEGGamr:AM1_1640.
PATRIC20617668. VBIAcaMar40141_1472.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG351027.
OMAAALNRMG.
PhylomeDBB0CA74.
ProtClustDBCLSK2475789.

Enzyme and pathway databases

BioCycAMAR329726:AM1_1640-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_ACAM1
AccessionPrimary (citable) accession number: B0CA74
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 31 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