Hmdb loader
Identification
HMDB Protein ID HMDBP00398
Secondary Accession Numbers
  • 5635
Name Malonyl-CoA-acyl carrier protein transacylase, mitochondrial
Synonyms
  1. MCT
  2. Mitochondrial malonyltransferase
  3. [Acyl-carrier-protein] malonyltransferase
  4. Mitochondrial malonyl CoA:ACP acyltransferase
Gene Name MCAT
Protein Type Enzyme
Biological Properties
General Function Involved in transferase activity
Specific Function Catalyzes the transfer of a malonyl moiety from malonyl-CoA to the free thiol group of the phosphopantetheine arm of the mitochondrial ACP protein (NDUFAB1). This suggests the existence of the biosynthesis of fatty acids in mitochondrias.
Pathways
  • fatty acid biosynthesis
Reactions
Malonyl-CoA + [acyl-carrier-protein] → Coenzyme A + malonyl-[acyl-carrier-protein] details
Malonyl-CoA + Acyl-carrier protein → Coenzyme A + Malonyl-[acyl-carrier protein] details
GO Classification
Biological Process
fatty acid biosynthetic process
Cellular Component
mitochondrion
Function
binding
catalytic activity
transferase activity
Molecular Function
[acyl-carrier-protein] S-malonyltransferase activity
Process
metabolic process
Cellular Location
  1. Mitochondrion
Gene Properties
Chromosome Location 22
Locus 22q13.31
SNPs MCAT
Gene Sequence
>1173 bp
ATGAGCGTCCGGGTCGCACGGGTAGCGTGGGTCAGGGGCTTGGGCGCCAGCTACCGCCGC
GGCGCCTCGAGCTTCCCGGTGCCTCCGCCGGGCGCCCAGGGTGTAGCGGAGCTGCTGCGA
GATGCGACCGGGGCGGAGGAGGAGGCGCCCTGGGCGGCGACGGAGCGGCGAATGCCGGGC
CAGTGCTCCGTGCTGCTCTTCCCGGGCCAGGGCAGCCAGGTGGTGGGCATGGGCCGCGGT
CTGCTCAACTACCCGCGCGTCCGCGAACTCTACGCCGCCGCCCGCCGCGTGCTGGGCTAC
GACCTGCTGGAACTGAGCCTGCACGGGCCGCAGGAGACCCTGGACCGCACCGTGCACTGT
CAGCCCGCGATCTTCGTGGCATCGCTGGCCGCTGTCGAGAAACTACATCACCTGCAGCCC
TCGGTGATTGAGAACTGTGTTGCTGCTGCTGGATTCAGTGTGGGAGAGTTTGCAGCCCTA
GTGTTTGCCGGAGCCATGGAATTTGCTGAAGGTTTGTATGCAGTGAAAATCCGAGCTGAG
GCCATGCAGGAAGCTTCAGAAGCTGTCCCCAGTGGGATGCTGTCTGTCCTCGGCCAGCCT
CAGTCCAAGTTCAACTTCGCCTGTTTGGAAGCCCGGGAACACTGCAAGTCTTTAGGCATA
GAGAACCCCGTATGTGAAGTGTCCAACTACCTCTTTCCAGATTGCAGGGTGATTTCAGGA
CACCAAGAGGCTCTACGGTTTCTCCAGAAGAATTCCTCTAAGTTTCATTTCAGACGCACC
AGGATGTTGCCGGTTAGTGGCGCATTCCACACCCGCCTCATGGAGCCAGCCGTGGAGCCC
CTGACGCAAGCTTTAAAGGCAGTCGACATTAAGAAGCCTCTGGTTTCTGTCTACTCCAAC
GTCCACGCGCATAGATACAGGCATCCCGGGCACATCCACAAGCTGCTGGCCCAGCAGCTG
GTCTCCCCAGTGAAGTGGGAGCAGACGATGCATGCCATATACGAAAGGAAAAAGGGCAGG
GGGTTCCCCCAAACTTTCGAAGTAGGCCCTGGCAGGCAGCTGGGAGCCATCCTGAAGAGC
TGTAACATGCAGGCCTGGAAGTCCTACAGCGCCGTGGATGTGCTGCAGACCCTCGAACAT
GTGGACCTGGACCCTCAGGAGCCCCCGAGATGA
Protein Properties
Number of Residues 390
Molecular Weight 19175.775
Theoretical pI 6.169
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Malonyl-CoA-acyl carrier protein transacylase, mitochondrial
MSVRVARVAWVRGLGASYRRGASSFPVPPPGAQGVAELLRDATGAEEEAPWAATERRMPG
QCSVLLFPGQGSQVVGMGRGLLNYPRVRELYAAARRVLGYDLLELSLHGPQETLDRTVHC
QPAIFVASLAAVEKLHHLQPSVIENCVAAAGFSVGEFAALVFAGAMEFAEGLYAVKIRAE
AMQEASEAVPSGMLSVLGQPQSKFNFACLEAREHCKSLGIENPVCEVSNYLFPDCRVISG
HQEALRFLQKNSSKFHFRRTRMLPVSGAFHTRLMEPAVEPLTQALKAVDIKKPLVSVYSN
VHAHRYRHPGHIHKLLAQQLVSPVKWEQTMHAIYERKKGRGFPQTFEVGPGRQLGAILKS
CNMQAWKSYSAVDVLQTLEHVDLDPQEPPR
GenBank ID Protein 8574364
UniProtKB/Swiss-Prot ID Q8IVS2
UniProtKB/Swiss-Prot Entry Name FABD_HUMAN
PDB IDs
GenBank Gene ID AL359401
GeneCard ID MCAT
GenAtlas ID MCAT
HGNC ID HGNC:29622
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. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed:10591208 ]
  3. Collins JE, Goward ME, Cole CG, Smink LJ, Huckle EJ, Knowles S, Bye JM, Beare DM, Dunham I: Reevaluating human gene annotation: a second-generation analysis of chromosome 22. Genome Res. 2003 Jan;13(1):27-36. [PubMed:12529303 ]
  4. Zhang L, Joshi AK, Smith S: Cloning, expression, characterization, and interaction of two components of a human mitochondrial fatty acid synthase. Malonyltransferase and acyl carrier protein. J Biol Chem. 2003 Oct 10;278(41):40067-74. Epub 2003 Jul 25. [PubMed:12882974 ]