Methylmalonyl-CoA carboxyltransferase 12S subunit

Details

Name
Methylmalonyl-CoA carboxyltransferase 12S subunit
Synonyms
  • 2.1.3.1
  • Transcarboxylase 12S subunit
Gene Name
Not Available
Organism
Propionibacterium freudenreichii subsp. shermanii
Amino acid sequence
>lcl|BSEQ0003529|Methylmalonyl-CoA carboxyltransferase 12S subunit
MAENNNLKLASTMEGRVEQLAEQRQVIEAGGGERRVEKQHSQGKQTARERLNNLLDPHSF
DEVGAFRKHRTTLFGMDKAVVPADGVVTGRGTILGRPVHAASQDFTVMGGSAGETQSTKV
VETMEQALLTGTPFLFFYDSGGARIQEGIDSLSGYGKMFFANVKLSGVVPQIAIIAGPCA
GGASYSPALTDFIIMTKKAHMFITGPQVIKSVTGEDVTADELGGAEAHMAISGNIHFVAE
DDDAAELIAKKLLSFLPQNNTEEASFVNPNNDVSPNTELRDIVPIDGKKGYDVRDVIAKI
VDWGDYLEVKAGYATNLVTAFARVNGRSVGIVANQPSVMSGCLDINASDKAAEFVNFCDS
FNIPLVQLVDVPGFLPGVQQEYGGIIRHGAKMLYAYSEATVPKITVVLRKAYGGSYLAMC
NRDLGADAVYAWPSAEIAVMGAEGAANVIFRKEIKAADDPDAMRAEKIEEYQNAFNTPYV
AAARGQVDDVIDPADTRRKIASALEMYATKRQTRPAKKPWKLPLLSEEEIMADEEEKDLM
IATLNKRVASLESELGSLQSDTQGVTEDVLTAISAVAAYLGNDGSAEVVHFAPSPNWVRE
GRRALQNHSIR
Number of residues
611
Molecular Weight
65926.0
Theoretical pI
4.86
GO Classification
Functions
acetyl-CoA carboxylase activity / methylmalonyl-CoA carboxytransferase activity
Processes
fatty acid biosynthetic process
Components
acetyl-CoA carboxylase complex
General Function
Methylmalonyl-coa carboxytransferase activity
Specific Function
The 12S subunit specifically catalyzes the transfer of the carboxyl group of methylmalonyl CoA to the biotin of the 1.3S subunit forming propanoyl-CoA and carboxylated 1.3S-biotin.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0003528|1818 bp
ATGGCTGAAAACAACAATTTGAAGCTCGCCAGCACCATGGAAGGTCGCGTGGAGCAGCTC
GCAGAGCAGCGCCAGGTGATCGAAGCCGGTGGCGGCGAACGTCTCGTCGAGAAGCAACAT
TCCCAGGGTAAGCAGACCGCTCGTGAGCGCCTGAACAACCTGCTCGATCCCCATTCGTTC
GACGAGGTCGGCGCTTTCCGCAAGCACCGCACCACGTTGTTCGGCATGGACAAGGCCGTC
GTCCCGGCAGATGGCGTGGTCACCGGCCGTGGCACCATCCTTGGTCGTCCCGTGCACGCC
GCGTCCCAGGACTTCACGGTCATGGGTGGTTCGGCTTGGCGAGACGCAGTCCACGAAGGT
CGTCGAGACGATGGAACAGCGCTGCTCACCGGCACGCCCTTCCTGTTCTTCTACGATTCG
GGCGGCCGGATCCAGGAGGGCATCGACTCGCTGAGCGGTTACGGCAAGATGTTCTTCGCC
AACGTGAAGCTGTCGGGCGTCGTGCCGCAGATCGCCATCATTGCCGGCCCCTGTGCGTGC
GCCTCGTATTCGCCGGCACTGACTGACTTCATCATCATGACCAAGAAGGCCCATATGTTC
ATCACGGGCCCCCAGGTCATCAAGTCGGTCACCGGCGAGGATGTCACCGCTGACGAACTC
GGTGGCGCTGAGCCCATATGGCCATCTCGGGCAATATACTTCGTGGCCGAGGACGACGAC
GCCGCGGAGCTCATTGCCAAGAAGCTGCTGAGCTTCCTTCCGCAGAACAACACTGAGGAA
GCATCCTTCGTCAACCCGAACAATGACGTCAGCCCCAATACCGAGCTGCGCGACATCGTT
CCGATTGACGGCAAGAAGGGCTATGACGTGCGCGATGTCATTGCCAAGATCGTCGACTGG
GGTGACTACCTCGAGGTCAAGGCCGGCTATGCCACCAACCTCGTGACCGCCTTCGCCCGG
GTCAATGGTCGTTCGGTGGGCATCGTGGCCAATCAGCCTTCGGTGATGTCGGGTTGCCTC
GACATCAACGCCTCTGACAAGGCCGCCGAATTCGTGAATTTCTGCGATTCGTTCAACATC
CCGCTGGTGCAGCTGGTCGACGTGCCGGGCTTCCTGCCCGTGCAGCAGGAGTACGGCGGC
ATCATTCGCCATGGGCGCAAGATGCTGTACGCCTACTCCGAGGCCACCGTGCCGAAGATC
ACGTGTCTCGCAACGCCTACGGCGGCTCCTACCTGGCCATGTGCAACCGTGACCTTGGTG
CCGACGCCGTGTACGCCTGTGCCCAGCGCCGAGATTGCGGTGATGGGCGCCGAGGGTGCG
GCAAATGTGATCTTCCGCAAGGAGATCAAGGCTGCCGACGATCCCGACGCCATGCGCGCC
GAGAAGATCGAGGAGTACCAGAACGGTTCAACACGCCGTACGTGGCGCGCCCGCGGTCAG
GTCGACGACGTGATTGACCCGGCTGATACCCGTCGAAAGATTGCTTCCGCCCTGGAGATG
TACGCCACCAAGCGTCAGACCCGCCCGGCGAAGAAGCCATGGAAACTTCCCCTGCTGAGC
GAGGAGGAAATTATGGCTGATGAGGAAGAGAAGGACCTGATGATCGCCACGCTCAACAAG
CGCGTCGCGTCATTGGAGTCTGAGTTGGGTTCACTCCAGAGCGATACCCAGGGTGTCACC
GAGGACGTACTGACGGCCATTTCGGCCGTTGCGGCCTATCTCGGCAACGATGGATCGGCT
GAGGTCGTCCATTTCGCCCCGAGCCCGAACTGGGTCCGCGAGGGTCGTCGGGCTCTGCAG
AACCATTCCATTCGTTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ8GBW6
UniProtKB Entry Name12S_PROFR
GenBank Protein ID150933
GenBank Gene IDL04196
General References
  1. Thornton CG, Kumar GK, Haase FC, Phillips NF, Woo SB, Park VM, Magner WJ, Shenoy BC, Wood HG, Samols D: Primary structure of the monomer of the 12S subunit of transcarboxylase as deduced from DNA and characterization of the product expressed in Escherichia coli. J Bacteriol. 1993 Sep;175(17):5301-8. [Article]
  2. Hall PR, Wang YF, Rivera-Hainaj RE, Zheng X, Pustai-Carey M, Carey PR, Yee VC: Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core. EMBO J. 2003 May 15;22(10):2334-47. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04045(R)-methylmalonyl-CoAexperimentalunknownDetails
DB04183Methylmalonic AcidexperimentalunknownDetails