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P25971 (PYRF_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Orotidine 5'-phosphate decarboxylase
EC=4.1.1.23
Alternative name(s):
OMP decarboxylase
Short name=OMPDCase
Short name=OMPdecase
Gene names
Name:pyrF
Ordered Locus Names:BSU15550
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). HAMAP-Rule MF_01200_B

Catalytic activity

Orotidine 5'-phosphate = UMP + CO2. HAMAP-Rule MF_01200_B

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. HAMAP-Rule MF_01200_B

Subunit structure

Homodimer. Ref.3

Sequence similarities

Belongs to the OMP decarboxylase family. Type 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 239239Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200_B
PRO_0000134527

Regions

Region60 – 6910Substrate binding HAMAP-Rule MF_01200_B

Sites

Active site621Proton donor
Binding site111Substrate
Binding site331Substrate
Binding site1231Substrate
Binding site1851Substrate
Binding site1941Substrate
Binding site2141Substrate; via amide nitrogen
Binding site2151Substrate

Secondary structure

1 ............................................. 239
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25971 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: DB1743714ED052E7

FASTA23925,992
        10         20         30         40         50         60 
MKNNLPIIAL DFASAEETLA FLAPFQQEPL FVKVGMELFY QEGPSIVKQL KERNCELFLD 

        70         80         90        100        110        120 
LKLHDIPTTV NKAMKRLASL GVDLVNVHAA GGKKMMQAAL EGLEEGTPAG KKRPSLIAVT 

       130        140        150        160        170        180 
QLTSTSEQIM KDELLIEKSL IDTVVHYSKQ AEESGLDGVV CSVHEAKAIY QAVSPSFLTV 

       190        200        210        220        230 
TPGIRMSEDA ANDQVRVATP AIAREKGSSA IVVGRSITKA EDPVKAYKAV RLEWEGIKS

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase."
Appleby T.C., Kinsland C., Begley T.P., Ealick S.E.
Proc. Natl. Acad. Sci. U.S.A. 97:2005-2010(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH UMP, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M59757 Genomic DNA. Translation: AAA21273.1.
AL009126 Genomic DNA. Translation: CAB13429.1.
PIRI39845.
RefSeqNP_389438.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DBTX-ray2.40A/B/C1-239[»]
ProteinModelPortalP25971.
SMRP25971. Positions 1-237.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU15550.

Proteomic databases

PaxDbP25971.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13429; CAB13429; BSU15550.
GeneID935960.
KEGGbsu:BSU15550.
PATRIC18974917. VBIBacSub10457_1650.

Organism-specific databases

GenoListBSU15550. [Micado]

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMANFKIFLD.
ProtClustDBPRK00230.

Enzyme and pathway databases

BioCycBSUB:BSU15550-MONOMER.
UniPathwayUPA00070; UER00120.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01200_B. OMPdecase_type1_B.
InterProIPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
IPR018089. OMPdecase_AS.
IPR001754. OMPdeCOase_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00215. OMPdecase. 1 hit.
[Graphical view]
SMARTSM00934. OMPdecase. 1 hit.
[Graphical view]
SUPFAMSSF51366. RibP_bind_barrel. 1 hit.
TIGRFAMsTIGR01740. pyrF. 1 hit.
PROSITEPS00156. OMPDECASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25971.

Entry information

Entry namePYRF_BACSU
AccessionPrimary (citable) accession number: P25971
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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