Methylmalonyl-CoA carboxyltransferase 5S subunit
Details
- Name
- Methylmalonyl-CoA carboxyltransferase 5S subunit
- Synonyms
- 2.1.3.1
- Transcarboxylase 5S subunit
- Gene Name
- Not Available
- 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
- 505
- Molecular Weight
- 55649.06
- Theoretical pI
- 5.51
- GO Classification
- Functionsmetal ion binding / methylmalonyl-CoA carboxytransferase activity
- 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.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not 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
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q70AC7 UniProtKB Entry Name 5S_PROFR GenBank Protein ID 38304072 GenBank Gene ID AJ606310 - General 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. [Article]
- 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. [Article]
- 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. [Article]