Orotidine 5'-phosphate decarboxylase

Details

Name
Orotidine 5'-phosphate decarboxylase
Synonyms
  • 4.1.1.23
  • OMP decarboxylase
  • OMPDCase
  • OMPdecase
Gene Name
pyrF
Organism
Bacillus subtilis (strain 168)
Amino acid sequence
>lcl|BSEQ0020574|Orotidine 5'-phosphate decarboxylase
MKNNLPIIALDFASAEETLAFLAPFQQEPLFVKVGMELFYQEGPSIVKQLKERNCELFLD
LKLHDIPTTVNKAMKRLASLGVDLVNVHAAGGKKMMQAALEGLEEGTPAGKKRPSLIAVT
QLTSTSEQIMKDELLIEKSLIDTVVHYSKQAEESGLDGVVCSVHEAKAIYQAVSPSFLTV
TPGIRMSEDAANDQVRVATPAIAREKGSSAIVVGRSITKAEDPVKAYKAVRLEWEGIKS
Number of residues
239
Molecular Weight
25991.84
Theoretical pI
6.15
GO Classification
Functions
orotidine-5'-phosphate decarboxylase activity
Processes
'de novo' pyrimidine nucleobase biosynthetic process / 'de novo' UMP biosynthetic process
General Function
Orotidine-5'-phosphate decarboxylase activity
Specific Function
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0020575|Orotidine 5'-phosphate decarboxylase (pyrF)
ATGAAAAACAACCTGCCCATCATCGCGCTTGATTTTGCGTCAGCTGAAGAAACACTTGCG
TTCTTAGCGCCTTTTCAGCAAGAACCGTTATTTGTAAAGGTTGGGATGGAGCTTTTTTAT
CAAGAAGGGCCATCTATCGTGAAACAACTAAAAGAAAGAAACTGCGAGCTATTTTTAGAT
CTAAAGCTTCATGACATCCCGACTACTGTAAACAAAGCGATGAAGCGCCTTGCCAGTCTT
GGAGTAGACCTCGTCAATGTTCATGCTGCCGGGGGCAAAAAAATGATGCAGGCAGCTCTC
GAAGGCTTAGAAGAAGGTACGCCGGCTGGAAAAAAACGTCCGTCACTTATCGCGGTAACC
CAGCTGACAAGCACATCTGAACAAATCATGAAAGATGAACTGCTGATCGAAAAGTCTCTG
ATTGATACGGTTGTGCACTACAGCAAACAGGCGGAAGAAAGCGGACTGGATGGAGTGGTC
TGCTCTGTTCATGAAGCAAAAGCCATTTACCAAGCGGTGTCGCCTTCATTTCTGACTGTC
ACTCCGGGGATCAGAATGTCAGAGGACGCTGCGAATGACCAAGTTCGCGTAGCGACGCCT
GCCATTGCAAGAGAGAAAGGTTCATCAGCGATTGTAGTAGGACGCTCGATTACAAAAGCG
GAAGACCCGGTAAAAGCCTATAAGGCTGTCAGACTTGAATGGGAGGGAATCAAATCTTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP25971
UniProtKB Entry NamePYRF_BACSU
GenBank Protein ID143392
GenBank Gene IDM59757
General References
  1. Quinn CL, Stephenson BT, Switzer RL: Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon. J Biol Chem. 1991 May 15;266(14):9113-27. [Article]
  2. Kunst F, Ogasawara N, Moszer I, Albertini AM, Alloni G, Azevedo V, Bertero MG, Bessieres P, Bolotin A, Borchert S, Borriss R, Boursier L, Brans A, Braun M, Brignell SC, Bron S, Brouillet S, Bruschi CV, Caldwell B, Capuano V, Carter NM, Choi SK, Cordani JJ, Connerton IF, Cummings NJ, Daniel RA, Denziot F, Devine KM, Dusterhoft A, Ehrlich SD, Emmerson PT, Entian KD, Errington J, Fabret C, Ferrari E, Foulger D, Fritz C, Fujita M, Fujita Y, Fuma S, Galizzi A, Galleron N, Ghim SY, Glaser P, Goffeau A, Golightly EJ, Grandi G, Guiseppi G, Guy BJ, Haga K, Haiech J, Harwood CR, Henaut A, Hilbert H, Holsappel S, Hosono S, Hullo MF, Itaya M, Jones L, 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 SM, Levine A, Liu H, Masuda S, Mauel C, Medigue C, Medina N, Mellado RP, Mizuno M, Moestl D, Nakai S, Noback M, Noone D, O'Reilly M, Ogawa K, Ogiwara A, Oudega B, Park SH, Parro V, Pohl TM, Portelle D, Porwollik S, Prescott AM, 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 SJ, Serror P, Shin BS, Soldo B, Sorokin A, Tacconi E, Takagi T, Takahashi H, Takemaru K, Takeuchi M, Tamakoshi A, Tanaka T, Terpstra P, Togoni A, Tosato V, Uchiyama S, Vandebol M, Vannier F, Vassarotti A, Viari A, Wambutt R, Wedler H, Weitzenegger T, Winters P, Wipat A, Yamamoto H, Yamane K, Yasumoto K, Yata K, Yoshida K, Yoshikawa HF, Zumstein E, Yoshikawa H, Danchin A: The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature. 1997 Nov 20;390(6657):249-56. [Article]
  3. Appleby TC, Kinsland C, Begley TP, Ealick SE: The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase. Proc Natl Acad Sci U S A. 2000 Feb 29;97(5):2005-10. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03685Uridine monophosphateexperimentalunknownDetails