NameMethylmalonyl-CoA carboxyltransferase 5S subunit
Synonyms
  • 2.1.3.1
  • Transcarboxylase 5S subunit
Gene NameNot Available
OrganismPropionibacterium freudenreichii subsp. shermanii
Amino acid sequence
>lcl|BSEQ0003255|Methylmalonyl-CoA carboxyltransferase 5S subunit
MSPREIEVSEPREVGITELVLRDAHQSLMATRMAMEDMVGACADIDAAGYWSVECWGGAT
YDSCIRFLNEDPWERLRTFRKLMPNSRLQMLLRGQNLLGYRHYNDEVVDRFVDKSAENGM
DVFRVFDAMNDPRNMAHAMAAVKKAGKHAQGTICYTISPVHTVEGYVKLAGQLLDMGADS
IALKDMAALLKPQPAYDIIKAIKDTYGQKTQINLHCHSTTGVTEVSLMKAIEAGVDVVDT
AISSMSLGPGHNPTESVAEMLEGTGYTTNLDYDRLHKIRDHFKAIRPKYKKFESKTLVDT
SIFKSQIPGGMLSNMESQLRAQGAEDKMDEVMAEVPRVRKAAGFPPLVTPSSQIVGTQAV
FNVMMGEYKRMTGEFADIMLGYYGASPADRDPKVVKLAEEQSGKKPITQRPADLLPPEWE
KQSKEAATLKGFNGTDEDVLTYALFPQVAPVFFEHRAEGPHSVALTDAQLKAEAEGDEKS
LAVAGPVTYNVNVGGTVREVTVQQA
Number of residues505
Molecular Weight55649.06
Theoretical pI5.51
GO Classification
Functions
  • metal ion binding
  • methylmalonyl-CoA carboxytransferase activity
General FunctionMethylmalonyl-coa carboxytransferase activity
Specific FunctionThe 5S subunit specifically catalyzes the transfer of the carboxyl group from biotin of the 1.3S subunit to pyruvate to form oxaloacetate and 1.3S biotin.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID38304072
UniProtKB IDQ70AC7
UniProtKB Entry Name5S_PROFR
Cellular LocationNot Available
Gene sequence
>lcl|BSEQ0003254|1560 bp
ATGAGTCCGCGAGAAATTGAGGTTTCCGAGCCGCGCGAGGTTGGTATCACCGAGCTCGTG
CTGCGCGATGCCCATCAGAGCCTGATGGCCACACGAATGGCAATGGAAGACATGGTCGGC
GCCTGTGCAGACATTGATGCTGCCGGGTACTGGTCAGTGGAGTGTTGGGGTGGTGCCACG
TATGACTCGTGTATCCGCTTCCTCAACGAGGATCCTTGGGAGCGTCTGCGCACGTTCCGC
AAGCTGATGCCCAACAGCCGTCTCCAGATGCTGCTGCGTGGCCAGAACCTGCTGGGTTAC
CGCCACTACAACGACGAGGTCGTCGATCGTTTCGTCGACAAGTCCGCTGAGAACGGCATG
GACGTGTTCCGTGTCTTCGACGCCATGAATGATCCCCGCAATATGGCGCACGCCATGGCT
GCCGTCAAGAAGGCCGGCAAGCACGCGCAGGGCACCATTTGCTACACGATCAGCCCGGTC
CACACCGTTGAGGGCTATGTCAAGCTTGCTGGTCAGCTGCTCGACATGGGTGCTGATTCC
ATCGCCCTGAAGGACATGGCCGCCCTGCTCAAGCCGCAGCCGGCCTACGACATCATCAAG
GCCATCAAGGACATACGGCCAGAAGACGCAGATCAACCTGCACTGCACTCCACCACGGGT
GTCACCGAGGTCTCCCTCATGAAGGCCATCGAGGCCGGCGTCGACACCGCCATCTCGTCC
ATGTCGCTCGGCCCGGGCCACAACCCCACCGAGTCGGTTGCCGAGATGCTCGAGGGCACC
GGGTACACCACCAACCTTGACTACGATCGCCTGCACAAGATCCGCGATCACTTCAAGGCC
ATCCGCCCGAAGTACAAGAAGTTCGAGTCGAAGACGCTTGTCGACACCTCGATCTTCAAG
TCGCAGATCCCCGGCGGCATGCTGTCCAACATGGAGTCGCAGCTGCGCGCCCAGGGCGCC
GAGGACAAGATGGACGAGGTCATGGCAGAGGTGCCGCGCGTCCGAAGGCCGGCGCCGGTT
TTCCCCGCCCCTGGTCACCCCGTCCAGCCAGATCGTCGGCACGCAGGCCTGTTCAACGTG
ATGATGGGCGAGTACAAGAGGATGACCGGCGAGTTCGCAGATATCATGCTCGGCTACTAC
GGCGCCACGCCGGCCGATCGCGATCCGAAGTGGTCAGTTGGCGAGGAGCATCGCAGAGCG
ATCACCCAGCGCCCGGCCGATCACGATCCGAAGGTGGTCAAGTTGGCCGAGGAGCAGTCC
GGCAAGAAGCCGATCACCCAGCGCCCGGCCGATCTGCTGCCCCCCGAGTGGGAGGAGCAG
TCCAAGGAGCCGCGCCCTAAGGGCTTCAACGGCACCGACGAGGACGTGCTCACCTATGCA
CTGTTCCCGCAGGTCGCTCCGGTCTTCTTCGAGAGTCGGCCGAGGGCCGCAGAGGTGGCT
CTCACCGATGCCCAGCTGAAGGCCGAGGCGAGGGCGACGAGAAGTGTCGCCGTGGCCGGT
CCCGTCACCTACAACGTGAACGTGCGGAACCGTCCGCAAGTCACCGTTCAGCAGGCGTGA
GenBank Gene IDAJ606310
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
References
  1. Thornton CG, Kumar GK, Shenoy BC, Haase FC, Phillips NF, Park VM, Magner WJ, Hejlik DP, Wood HG, Samols D: Primary structure of the 5 S subunit of transcarboxylase as deduced from the genomic DNA sequence. FEBS Lett. 1993 Sep 13;330(2):191-6. 8365490
  2. Hall PR, Zheng R, Pusztai-Carey M, van den Akker F, Carey PR, Yee VC: Expression and crystallization of several forms of the Propionibacterium shermanii transcarboxylase 5S subunit. Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):521-3. Epub 2004 Feb 25. 14993680
  3. Hall PR, Zheng R, Antony L, Pusztai-Carey M, Carey PR, Yee VC: Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit. EMBO J. 2004 Sep 15;23(18):3621-31. Epub 2004 Aug 26. 15329673