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UniProtKB/Swiss-Prot entry P25996


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PYRD_BACSU
Primary accession number P25996
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on May 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 76)
Name and origin of the protein
Protein name Dihydroorotate dehydrogenase, catalytic subunit
Synonyms EC 1.3.3.1
Dihydroorotate oxidase
DHOdehase
DHODase
DHOD
Gene name
Name: pyrD
Synonyms: pyrDA, pyrDI
OrderedLocusNames: BSU15540
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1709162 [NCBI, ExPASy, EBI, Israel, Japan]
Quinn C.L., Stephenson B.T., Switzer R.L.;
"Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon.";
J. Biol. Chem. 266:9113-9127(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[3]
CHARACTERIZATION.
DOI=10.1006/abbi.1999.1455; PubMed=10545205 [NCBI, ExPASy, EBI, Israel, Japan]
Kahler A.E., Nielsen F.S., Switzer R.L.;
"Biochemical characterization of the heteromeric Bacillus subtilis dihydroorotate dehydrogenase and its isolated subunits.";
Arch. Biochem. Biophys. 371:191-201(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M59757; AAA21272.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99112; CAB13428.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H39845; H39845.
RefSeq NP_389437.1; -.
3D structure databases
HSSP P54322; 1EP2. [HSSP ENTRY / PDB]
ModBase P25996.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1556-MON; -.
Organism-specific databases
SubtiList BG10718; pyrD. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004158; Molecular function: dihydroorotate oxidase activity (inferred from electronic annotation from HAMAP).
GO:0006207; Biological process: 'de novo' pyrimidine base biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006222; Biological process: UMP biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
HAMAP MF_00224; -; 1.
PBIL [Tree]
InterPro IPR013785; Aldolase_TIM.
IPR012135; DHO_DHase_1_2.
IPR005720; DHO_DHase_1_core.
IPR001295; Dihydroorotate_DHase_core.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF01180; DHO_dh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000164; DHO_oxidase; 1.
TIGRFAMs TIGR01037; pyrD_sub1_fam; 1.
PROSITE PS00911; DHODEHASE_1; 1.
PS00912; DHODEHASE_2; 1.
ProtoNet P25996.
Genome annotation databases
GeneID 938008; -.
GenomeReviews AL009126_GR; BSU15540.
KEGG bsu:BSU15540; -.
NMPDR fig|224308.1.peg.1556; -.
Phylogenomic databases
HOGENOM P25996; -.
Genome annotation databases
CMR P25996; BSU15540.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Flavoprotein; FMN; Oxidoreductase; Pyrimidine biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   311  311     Dihydroorotate dehydrogenase, catalytic subunit. PRO_0000148389
ACT_SITE   128   128        Nucleophile (By similarity). 
Sequence information
Length: 311 AA [This is the length of the unprocessed precursor] Molecular weight: 33091 Da [This is the MW of the unprocessed precursor] CRC64: F55F9842C87D0DEA [This is a checksum on the sequence]
        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 

P25996 in FASTA format

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