Formyl-CoA:oxalate CoA-transferase

Details

Name
Formyl-CoA:oxalate CoA-transferase
Synonyms
  • 2.8.3.16
  • FCOCT
  • Formyl-CoA transferase
  • Formyl-coenzyme A transferase
Gene Name
frc
Organism
Shigella flexneri
Amino acid sequence
>lcl|BSEQ0011360|Formyl-CoA:oxalate CoA-transferase
MSTPLQGIKVLDFTGVQSGPSCTQMLAWFGADVIKIERPGVGDVTRHQLRDIPDIDALYF
TMLNSNKRSIELNTKTAEGKEVMEKLIREADILVENFHPGAIDHMGFTWEHIQEINPRLI
FGSIKGFDECSPYVNVKAYENVAQAAGGAASTTGFWDGPPLVSAAALGDSNTGMHLLIGL
LAALLHREKTGRGQRVTMSMQDAVLNLCRVKLRDQQRLDKLGYLEEYPQYPNGTFGDAVP
RGGNAGGGGQPGWILKCKGWETDPNAYIYFTIQEQNWENTCKAIGKPEWITDPAYSTAHA
RQPHIFDIFAEIEKYTVTIDKHEAVAYLTQFDIPCAPVLSMKEISLDPSLRQSGSVVEVE
QPLRGKYLTVGCPMKFSAFTPDIKAAPLLGEHTAAVLQELGYSDDEIAAMKQNHAI
Number of residues
416
Molecular Weight
45827.825
Theoretical pI
5.28
GO Classification
Functions
formyl-CoA transferase activity
Processes
oxalate catabolic process
General Function
Formyl-coa transferase activity
Specific Function
Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate (By similarity).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011361|Formyl-CoA:oxalate CoA-transferase (frc)
ATGTCAACTCCACTTCAAGGAATTAAAGTTCTCGATTTCACCGGTGTGCAATCTGGCCCA
TCTTGTACTCAAATGCTGGCCTGGTTTGGCGCTGACGTTATTAAAATTGAACGTCCCGGC
GTTGGTGACGTAACGCGTCACCAACTGCGAGATATTCCTGATATCGATGCGCTTTACTTC
ACCATGCTTAACAGTAACAAACGTTCTATTGAGTTAAATACCAAAACAGCGGAAGGCAAA
GAGGTAATGGAAAAGCTGATCCGCGAAGCTGATATCTTAGTCGAGAACTTTCATCCAGGG
GCCATTGATCACATGGGCTTCACCTGGGAGCATATTCAAGAAATCAATCCACGTCTGATT
TTTGGTTCGATCAAAGGGTTTGATGAGTGTTCGCCTTATGTGAATGTAAAAGCCTATGAA
AACGTTGCTCAGGCAGCGGGTGGCGCGGCATCCACTACGGGTTTTTGGGATGGTCCGCCG
CTGGTAAGCGCTGCAGCGTTGGGTGACAGCAACACCGGAATGCATTTGCTGATCGGTTTA
CTTGCTGCTTTGCTGCATCGCGAAAAAACGGGGCGTGGGCAACGAGTCACCATGTCAATG
CAGGATGCCGTATTGAACCTTTGCCGCGTGAAATTACGTGACCAGCAGCGTCTCGATAAA
TTGGGTTATCTGGAAGAATACCCGCAGTATCCGAATGGTACATTTGGTGATGCAGTTCCC
CGCGGTGGTAATGCAGGTGGTGGCGGTCAGCCTGGCTGGATCCTGAAATGTAAAGGCTGG
GAAACCGATCCTAACGCCTATATTTATTTCACTATTCAGGAGCAAAACTGGGAAAACACC
TGTAAAGCCATCGGCAAACCAGAATGGATTACCGATCCGGCATACAGTACAGCCCATGCC
CGACAGCCACATATTTTCGATATTTTTGCTGAAATCGAAAAATACACTGTCACTATTGAT
AAACATGAAGCGGTGGCCTATTTGACTCAGTTTGATATTCCTTGTGCACCGGTTTTAAGT
ATGAAAGAAATTTCACTTGATCCCTCTTTGCGCCAAAGTGGCAGTGTTGTTGAAGTGGAA
CAACCGTTGCGTGGAAAATATCTGACCGTTGGTTGTCCAATGAAATTCTCTGCCTTTACG
CCGGATATTAAAGCTGCGCCGCTATTAGGTGAACATACCGCTGCTGTATTGCAGGAGCTG
GGTTATAGCGACGATGAAATTGCTGCAATGAAGCAAAACCACGCCATCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP69903
UniProtKB Entry NameFCTA_SHIFL
GenBank Protein ID24052809
GenBank Gene IDAE005674
General References
  1. Jin Q, Yuan Z, Xu J, Wang Y, Shen Y, Lu W, Wang J, Liu H, Yang J, Yang F, Zhang X, Zhang J, Yang G, Wu H, Qu D, Dong J, Sun L, Xue Y, Zhao A, Gao Y, Zhu J, Kan B, Ding K, Chen S, Cheng H, Yao Z, He B, Chen R, Ma D, Qiang B, Wen Y, Hou Y, Yu J: Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157. Nucleic Acids Res. 2002 Oct 15;30(20):4432-41. [Article]
  2. Wei J, Goldberg MB, Burland V, Venkatesan MM, Deng W, Fournier G, Mayhew GF, Plunkett G 3rd, Rose DJ, Darling A, Mau B, Perna NT, Payne SM, Runyen-Janecky LJ, Zhou S, Schwartz DC, Blattner FR: Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T. Infect Immun. 2003 May;71(5):2775-86. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01992Coenzyme Ainvestigational, nutraceuticalunknownDetails