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Reviewed, UniProtKB/Swiss-Prot P25996 (PYRD_BACSU)

Last modified June 16, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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Names and origin

Protein namesRecommended name:
    Dihydroorotate dehydrogenase, catalytic subunit
    EC=1.3.3.1
Alternative name(s):
    Dihydroorotate oxidase
    DHOdehase
      Short name=DHODase
      Short name=DHOD
Gene names
Name: pyrD
Synonyms: pyrDA, pyrDI
Ordered Locus Names: BSU15540
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 FMN per subunit. HAMAP MF_00224

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. HAMAP MF_00224

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 311311Dihydroorotate dehydrogenase, catalytic subunit HAMAP MF_00224
PRO_0000148389

Sites

Active site1281Nucleophile By similarity

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Sequences

Sequence LengthMass (Da)Tools
P25996-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: F55F9842C87D0DEA

FASTA31133,091
        10         20         30         40         50         60 
MLEVKLPGLD LKNPIIPASG CFGFGKEFSR FYDLSCLGAI MIKATTKEPR FGNPTPRVAE 

        70         80         90        100        110        120 
TGAGMLNAIG LQNPGLDSVL HHELPWLEQF DTPIIANVAG SQVDDYVEVA EHISKAPNVH 

       130        140        150        160        170        180 
ALELNISCPN VKTGGIAFGT NPEMAADLTK AVKEVSDVPV YVKLSPNVAN ITEIALAIEE 

       190        200        210        220        230        240 
AGADGLTMIN TLIGMRLDLK TGKPILANKT GGLSGPAVKP VAIRMVYEVS QMVNIPIIGM 

       250        260        270        280        290        300 
GGVQTAEDAL EFLLAGASAV AVGTANFVNP FACPEIIEQL PSVLLQYGYQ SIEECIGRSW 

       310 
NHEKQPAHHR A

« Hide

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References

« Hide 'large scale' references
[1]"Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon."
Quinn C.L., Stephenson B.T., Switzer R.L.
J. Biol. Chem. 266:9113-9127(1991) [PubMed: 1709162] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Biochemical characterization of the heteromeric Bacillus subtilis dihydroorotate dehydrogenase and its isolated subunits."
Kahler A.E., Nielsen F.S., Switzer R.L.
Arch. Biochem. Biophys. 371:191-201(1999) [PubMed: 10545205] [Abstract]
Cited for: CHARACTERIZATION.

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Cross-references

Sequence databases

M59757 Genomic DNA. Translation: AAA21272.1.
AL009126 Genomic DNA. Translation: CAB13428.1.
PIRH39845.
RefSeqNP_389437.1.

3D structure databases

HSSPHSSP built from PDB template 1EP2 based on UniProtKB P54322.
ModBaseSearch...

Genome annotation databases

GeneID938008.
GenomeReviewsGene locus BSU15540 in contig AL009126_GR.
KEGGbsu:BSU15540.
NMPDRfig|224308.1.peg.1556.

Organism-specific databases

SubtiListBG10718. pyrD. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP25996.
OMAP25996. NSIGLQN.

Enzyme and pathway databases

BioCycBSUB224308:BSU1556-MON.
BRENDA1.3.3.1. 150.

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...

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Entry information

Entry namePYRD_BACSU
AccessionPrimary (citable) accession number: P25996
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 16, 2009
This is version 80 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)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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