NameMethylmalonic aciduria type A protein, mitochondrial
Synonyms
  • 3.6.-.-
Gene NameMMAA
OrganismHuman
Amino acid sequence
>lcl|BSEQ0010245|Methylmalonic aciduria type A protein, mitochondrial
MPMLLPHPHQHFLKGLLRAPFRCYHFIFHSSTHLGSGIPCAQPFNSLGLHCTKWMLLSDG
LKRKLCVQTTLKDHTEGLSDKEQRFVDKLYTGLIQGQRACLAEAITLVESTHSRKKELAQ
VLLQKVLLYHREQEQSNKGKPLAFRVGLSGPPGAGKSTFIEYFGKMLTERGHKLSVLAVD
PSSCTSGGSLLGDKTRMTELSRDMNAYIRPSPTRGTLGGVTRTTNEAILLCEGAGYDIIL
IETVGVGQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVAVTKSDGDLIVPAR
RIQAEYVSALKLLRKRSQVWKPKVIRISARSGEGISEMWDKMKDFQDLMLASGELTAKRR
KQQKVWMWNLIQESVLEHFRTHPTVREQIPLLEQKVLIGALSPGLAADFLLKAFKSRD
Number of residues418
Molecular Weight46537.865
Theoretical pI9.83
GO Classification
Functions
  • hydrolase activity
  • GTP binding
Processes
  • cobalamin metabolic process
  • cobalamin biosynthetic process
  • short-chain fatty acid catabolic process
  • fatty acid beta-oxidation
  • small molecule metabolic process
  • vitamin metabolic process
  • water-soluble vitamin metabolic process
  • cellular lipid metabolic process
Components
  • mitochondrial matrix
General FunctionHydrolase activity
Specific FunctionProbable GTPase. May function as chaperone. May be involved in the transport of cobalamin (Cbl) into mitochondria for the final steps of adenosylcobalamin (AdoCbl) synthesis.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID26006421
UniProtKB IDQ8IVH4
UniProtKB Entry NameMMAA_HUMAN
Cellular LocationMitochondrion
Gene sequence
>lcl|BSEQ0010246|Methylmalonic aciduria type A protein, mitochondrial (MMAA)
ATGCCCATGCTGCTACCACATCCTCACCAGCATTTCCTAAAAGGCCTTTTAAGAGCACCT
TTCCGATGTTACCACTTCATCTTTCACTCAAGTACTCATCTCGGATCAGGAATCCCATGT
GCTCAGCCGTTTAATTCTCTTGGACTCCATTGTACAAAGTGGATGCTGCTGTCAGATGGC
TTAAAGAGAAAATTATGTGTACAAACAACCTTAAAGGACCACACAGAAGGACTTTCTGAT
AAAGAGCAAAGATTTGTGGATAAACTTTATACTGGTTTAATCCAAGGGCAAAGGGCCTGT
TTAGCAGAGGCCATAACTCTTGTAGAATCAACTCACAGCAGGAAAAAGGAGTTAGCCCAG
GTGCTTCTTCAGAAAGTATTACTTTACCACAGAGAACAAGAACAATCAAATAAAGGAAAA
CCACTAGCATTTCGAGTAGGATTGTCTGGGCCCCCTGGTGCTGGAAAATCAACATTTATA
GAATATTTTGGAAAAATGCTTACTGAGAGAGGGCACAAATTATCTGTGCTAGCTGTGGAC
CCTTCTTCTTGTACTAGTGGTGGATCACTCTTAGGTGATAAAACCCGAATGACTGAGTTA
TCAAGAGATATGAATGCATACATCAGGCCATCTCCTACTAGAGGAACTTTAGGAGGCGTG
ACAAGGACCACAAATGAAGCTATTCTGTTGTGTGAAGGAGCGGGATATGACATAATTCTT
ATTGAAACCGTTGGTGTGGGTCAGTCGGAGTTTGCTGTTGCTGACATGGTTGACATGTTT
GTTTTACTACTGCCACCAGCAGGAGGAGATGAGCTGCAGGGTATCAAAAGGGGTATAATC
GAGATGGCAGATCTGGTAGCTGTAACTAAATCTGATGGAGACTTGATTGTGCCAGCTCGA
AGGATACAAGCGGAATATGTGAGTGCACTGAAATTACTCCGCAAACGTTCACAAGTCTGG
AAACCAAAGGTAATTCGTATTTCTGCCCGAAGTGGAGAGGGGATCTCTGAAATGTGGGAT
AAAATGAAAGATTTCCAGGACCTAATGCTTGCCAGTGGGGAGCTGACTGCCAAACGACGG
AAGCAACAGAAAGTTTGGATGTGGAATCTCATTCAGGAAAGTGTGTTAGAGCATTTCAGG
ACCCACCCCACAGTCCGGGAACAGATTCCACTTCTGGAACAAAAGGTTCTCATTGGGGCC
CTGTCCCCAGGACTAGCAGCAGACTTCTTGTTAAAAGCTTTTAAAAGCAGAGACTAA
GenBank Gene IDAF524846
GeneCard IDNot Available
GenAtlas IDMMAA
HGNC IDHGNC:18871
Chromosome Location4
Locus4q31.22
References
  1. Dobson CM, Wai T, Leclerc D, Wilson A, Wu X, Dore C, Hudson T, Rosenblatt DS, Gravel RA: Identification of the gene responsible for the cblA complementation group of vitamin B12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15554-9. Epub 2002 Nov 15. 12438653
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  6. Froese DS, Kochan G, Muniz JR, Wu X, Gileadi C, Ugochukwu E, Krysztofinska E, Gravel RA, Oppermann U, Yue WW: Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation. J Biol Chem. 2010 Dec 3;285(49):38204-13. doi: 10.1074/jbc.M110.177717. Epub 2010 Sep 28. 20876572
  7. Lerner-Ellis JP, Dobson CM, Wai T, Watkins D, Tirone JC, Leclerc D, Dore C, Lepage P, Gravel RA, Rosenblatt DS: Mutations in the MMAA gene in patients with the cblA disorder of vitamin B12 metabolism. Hum Mutat. 2004 Dec;24(6):509-16. 15523652
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