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Showing Protein Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial (HMDBP01012)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 11 metabolites
Identification
HMDB Protein ID HMDBP01012
Secondary Accession Numbers
  • 6300
Name Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial
Synonyms
  1. Cob(I)alamin adenosyltransferase
  2. Methylmalonic aciduria type B protein
Gene Name MMAB
Protein Type Enzyme
Biological Properties
General Function Involved in ATP binding
Specific Function Not Available
Pathways
  • adenosylcobalamin biosynthesis
  • Porphyrin and chlorophyll metabolism
Reactions
Adenosine triphosphate + Cob(I)yrinate a,c diamide → Triphosphate + adenosylcob(III)yrinic acid a,c-diamide details
Adenosine triphosphate + Cobinamide → Triphosphate + Adenosyl cobinamide details
Cob(I)yrinate a,c diamide + Adenosine triphosphate → Adenosyl cobyrinic acid a,c diamide + Triphosphate details
Adenosine triphosphate + Cobinamide → Triphosphate + Adenosyl cobinamide details
GO Classification
Biological Process
cobalamin biosynthetic process
Cellular Component
mitochondrion
Function
binding
catalytic activity
transferase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
cob(i)yrinic acid a,c-diamide adenosyltransferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
Molecular Function
ATP binding
cob(I)yrinic acid a,c-diamide adenosyltransferase activity
Process
metabolic process
nitrogen compound metabolic process
tetrapyrrole metabolic process
porphyrin metabolic process
cobalamin biosynthetic process
porphyrin biosynthetic process
Cellular Location
  1. Mitochondrion (Probable)
Gene Properties
Chromosome Location 12
Locus 12q24
SNPs MMAB
Gene Sequence 
>753 bp
ATGGCTGTGTGCGGCCTGGGGAGCCGTCTTGGCCTGGGGAGCCGTCTTGGCCTGCAAGGG
TGCTTCGGCGCCGCCAGGCTCCTGTATCCCCGTTTCCAGAGCCGCGGCCCTCAGGGCGTG
GAAGACGGGGACAGGCCACAGCCTTCCTCGAAGACACCCAGGATCCCCAAGATTTACACC
AAAACGGGAGACAAAGGGTTTTCTAGTACCTTCACAGGAGAAAGGAGACCCAAAGATGAC
CAAGTGTTTGAAGCCGTGGGAACTACAGATGAATTAAGTTCAGCTATTGGGTTTGCTCTG
GAATTAGTCACAGAAAAGGGCCATACATTTGCCGAAGAGCTTCAGAAAATCCAGTGCACA
TTGCAGGACGTCGGCTCGGCCCTGGCGACACCATGCTCCTCGGCCCGGGAGGCTCACTTA
AAGTATACCACGTTCAAGGCGGGGCCCATCCTGGAGCTGGAGCAGTGGATCGACAAGTAC
ACCAGCCAGCTCCCACCACTCACGGCCTTCATCCTGCCTTCGGGAGGCAAGATCAGCTCG
GCGCTGCATTTCTGCCGGGCCGTGTGCCGCCGGGCCGAGAGACGTGTGGTGCCTCTTGTC
CAGATGGGAGAGACCGATGCGAACGTGGCCAAGTTCTTAAACAGACTCAGTGACTATCTC
TTCACGCTAGCCAGATATGCAGCCATGAAGGAGGGGAATCAAGAGAAAATATACAAGAAA
AATGACCCATCGGCCGAGTCTGAGGGACTCTGA
Protein Properties
Number of Residues 250
Molecular Weight 27387.975
Theoretical pI 8.606
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial
MAVCGLGSRLGLGSRLGLRGCFGAARLLYPRFQSRGPQGVEDGDRPQPSSKTPRIPKIYT
KTGDKGFSSTFTGERRPKDDQVFEAVGTTDELSSAIGFALELVTEKGHTFAEELQKIQCT
LQDVGSALATPCSSAREAHLKYTTFKAGPILELEQWIDKYTSQLPPLTAFILPSGGKISS
ALHFCRAVCRRAERRVVPLVQMGETDANVAKFLNRLSDYLFTLARYAAMKEGNQEKIYMK
NDPSAESEGL
GenBank ID Protein 127802458
UniProtKB/Swiss-Prot ID Q96EY8
UniProtKB/Swiss-Prot Entry Name MMAB_HUMAN
PDB IDs
GenBank Gene ID BC005054
GeneCard ID MMAB
GenAtlas ID MMAB
HGNC ID HGNC:19331
References
General References
  1. 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. [PubMed:15489334 ]
  2. 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. [PubMed:15781192 ]
  3. 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. [PubMed:12471062 ]
  4. 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. [PubMed:12514191 ]
  5. Schubert HL, Hill CP: Structure of ATP-bound human ATP:cobalamin adenosyltransferase. Biochemistry. 2006 Dec 26;45(51):15188-96. [PubMed:17176040 ]