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Reviewed, UniProtKB/Swiss-Prot Q732I5 (PYRD_BACC1)

Last modified June 16, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydroorotate dehydrogenase
    EC=1.3.3.1
Alternative name(s):
    Dihydroorotate oxidase
    DHOdehase
      Short name=DHODase
      Short name=DHOD
Gene names
Name: pyrD
Ordered Locus Names: BCE_3929
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + O2 = orotate + H2O2. HAMAP MF_00224

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6. HAMAP MF_00224

Subunit structure

Heterotetramer of 2 pyrK and 2 pyrD subunits By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
   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

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Dihydroorotate dehydrogenase HAMAP MF_00224
PRO_1000024124

Sites

Active site1301Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q732I5-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 70E308F9028EAA27

FASTA30932,990
        10         20         30         40         50         60 
MNRLQVELPG LSLKNPIIPA SGCFGFGREY AQFYDLSVLG SIMIKATTEQ PRYGNPTPRV 

        70         80         90        100        110        120 
AETPGGMLNA IGLQNPGLEK VMNSELPWLE QFDLPIIANV AGSQAEDYVA VAKEISKAPN 

       130        140        150        160        170        180 
VHALELNISC PNVKTGGIAF GTNPEIAADL TKRVKEVSEV PVYVKLSPNV ANIVEIAKAI 

       190        200        210        220        230        240 
ENAGADGLTM INTLLGMRLD LKTAKPILAN RTGGLSGPAI KPVAIRMVHE VSQAVNIPII 

       250        260        270        280        290        300 
GMGGIETAED VIEFFYAGAS AVAVGTANFI DPFVCPTIIE ELPALLDELG FDHISECQGR 


SWKQTCHSR 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE017194 Genomic DNA. Translation: AAS42832.1.
RefSeqNP_980224.1.

3D structure databases

SMRQ732I5. Positions 2-288.
ModBaseSearch...

Genome annotation databases

GeneID2751832.
GenomeReviewsGene locus BCE_3929 in contig AE017194_GR.
KEGGbca:BCE_3929.
TIGRBCE_3929.

Phylogenomic databases

HOGENOMQ732I5.
OMAQ732I5. NSIGLQN.

Family and domain databases

HAMAPMF_00224.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005720. Dihydroorotate_DH_1_core.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_BACC1
AccessionPrimary (citable) accession number: Q732I5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents