Methylmalonyl-CoA carboxyltransferase 5S subunit

Name	Methylmalonyl-CoA carboxyltransferase 5S subunit
Synonyms	2.1.3.1 Transcarboxylase 5S subunit
Gene Name	None
Organism	Propionibacterium freudenreichii subsp. shermanii
Amino acid sequence	>lcl\|BSEQ0003255\|Methylmalonyl-CoA carboxyltransferase 5S subunit MSPREIEVSEPREVGITELVLRDAHQSLMATRMAMEDMVGACADIDAAGYWSVECWGGAT YDSCIRFLNEDPWERLRTFRKLMPNSRLQMLLRGQNLLGYRHYNDEVVDRFVDKSAENGM DVFRVFDAMNDPRNMAHAMAAVKKAGKHAQGTICYTISPVHTVEGYVKLAGQLLDMGADS IALKDMAALLKPQPAYDIIKAIKDTYGQKTQINLHCHSTTGVTEVSLMKAIEAGVDVVDT AISSMSLGPGHNPTESVAEMLEGTGYTTNLDYDRLHKIRDHFKAIRPKYKKFESKTLVDT SIFKSQIPGGMLSNMESQLRAQGAEDKMDEVMAEVPRVRKAAGFPPLVTPSSQIVGTQAV FNVMMGEYKRMTGEFADIMLGYYGASPADRDPKVVKLAEEQSGKKPITQRPADLLPPEWE KQSKEAATLKGFNGTDEDVLTYALFPQVAPVFFEHRAEGPHSVALTDAQLKAEAEGDEKS LAVAGPVTYNVNVGGTVREVTVQQA
Number of residues	None
Molecular Weight	55649.06
Theoretical pI	5.51
GO Classification	Functions metal ion binding methylmalonyl-CoA carboxytransferase activity Processes Components
General Function	Methylmalonyl-coa carboxytransferase activity
Specific Function	The 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.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	Q70AC7
UniProtKB Entry Name
Cellular Location	None
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 ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	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 ] 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 ] 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 ]

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