Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial

NameCob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial
Synonyms2.5.1.17 Cob(I)alamin adenosyltransferase Methylmalonic aciduria type B protein
Gene NameMMAB
OrganismHuman
Amino acid sequence
>lcl|BSEQ0018952|Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial
MAVCGLGSRLGLGSRLGLRGCFGAARLLYPRFQSRGPQGVEDGDRPQPSSKTPRIPKIYT
KTGDKGFSSTFTGERRPKDDQVFEAVGTTDELSSAIGFALELVTEKGHTFAEELQKIQCT
LQDVGSALATPCSSAREAHLKYTTFKAGPILELEQWIDKYTSQLPPLTAFILPSGGKISS
ALHFCRAVCRRAERRVVPLVQMGETDANVAKFLNRLSDYLFTLARYAAMKEGNQEKIYMK
NDPSAESEGL
Number of residues250
Molecular Weight27387.975
Theoretical pI8.78
GO Classification
Functions
    cob(I)yrinic acid a,c-diamide adenosyltransferase activity
ATP binding
Processes
    cobalamin metabolic process
cobalamin biosynthetic process
small molecule metabolic process
vitamin metabolic process
water-soluble vitamin metabolic process
Components
    mitochondrial matrix
General FunctionCob(i)yrinic acid a,c-diamide adenosyltransferase activity
Specific FunctionNone
Transmembrane Regions
GenBank Protein ID26284726
UniProtKB IDQ96EY8
UniProtKB Entry NameMMAB_HUMAN
Cellular LocationMitochondrion
Gene sequence
>lcl|BSEQ0018953|Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial (MMAB)
ATGGCTGTGTGCGGCCTGGGGAGCCGTCTTGGCCTGGGGAGCCGTCTTGGCCTGCGCGGG
TGCTTCGGCGCCGCCAGGCTCCTGTATCCCCGTTTCCAGAGCCGCGGCCCTCAGGGCGTG
GAAGACGGGGACAGGCCACAGCCTTCCTCGAAGACACCCAGGATCCCCAAGATTTACACC
AAAACGGGAGACAAAGGGTTTTCTAGTACCTTCACAGGAGAAAGGAGACCCAAAGATGAC
CAAGTGTTTGAAGCCGTGGGAACTACAGATGAATTAAGTTCAGCTATTGGGTTTGCTCTG
GAATTAGTCACAGAAAAGGGCCATACATTTGCCGAAGAGCTTCAGAAAATCCAGTGCACA
TTGCAGGACGTCGGCTCGGCCCTGGCGACACCATGCTCCTCGGCCCGGGAGGCTCACTTA
AAGTATACCACGTTCAAGGCGGGGCCCATCCTGGAGCTGGAGCAGTGGATCGACAAGTAC
ACCAGCCAGCTCCCACCACTCACGGCCTTCATCCTGCCTTCGGGAGGCAAGATCAGCTCG
GCGCTGCATTTCTGCCGGGCCGTGTGCCGCCGGGCCGAGAGACGTGTGGTGCCTCTTGTC
CAGATGGGAGAGACCGATGCGAACGTGGCCAAGTTCTTAAACAGACTCAGTGACTATCTC
TTCACGCTAGCCAGATATGCAGCCATGAAGGAGGGGAATCAAGAGAAAATATACATGAAA
AATGACCCATCGGCCGAGTCTGAGGGACTCTGA
GenBank Gene IDAF550404
GeneCard IDNone
GenAtlas IDMMAB
HGNC IDHGNC:19331
Chromosome Location12
Locus12q24
References
  1. Leal NA, Park SD, Kima PE, Bobik TA: Identification of the human and bovine ATP:Cob(I)alamin adenosyltransferase cDNAs based on complementation of a bacterial mutant. J Biol Chem. 2003 Mar 14;278(11):9227-34. Epub 2003 Jan 3.[12514191 ]
  2. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17.[21269460 ]
  3. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22.[24275569 ]
  4. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8.[25944712 ]
  5. Schubert HL, Hill CP: Structure of ATP-bound human ATP:cobalamin adenosyltransferase. Biochemistry. 2006 Dec 26;45(51):15188-96.[17176040 ]
  6. Martinez MA, Rincon A, Desviat LR, Merinero B, Ugarte M, Perez B: Genetic analysis of three genes causing isolated methylmalonic acidemia: identification of 21 novel allelic variants. Mol Genet Metab. 2005 Apr;84(4):317-25. Epub 2005 Jan 22.[15781192 ]
  7. Dobson CM, Wai T, Leclerc D, Kadir H, Narang M, Lerner-Ellis JP, Hudson TJ, Rosenblatt DS, Gravel RA: Identification of the gene responsible for the cblB complementation group of vitamin B12-dependent methylmalonic aciduria. Hum Mol Genet. 2002 Dec 15;11(26):3361-9.[12471062 ]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7.[15489334 ]

Related FRC

FRCD ID Name Exact Mass Structure




F03812



Hydroxocobalamin


1346.377




F03808



Cyanocobalamin


1356.396