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Identification
HMDB Protein ID HMDBP01010
Secondary Accession Numbers
  • 6298
Name Trans-2-enoyl-CoA reductase, mitochondrial
Synonyms
  1. HsNrbf-1
  2. NRBF-1
  3. Nuclear receptor-binding factor 1
Gene Name MECR
Protein Type Unknown
Biological Properties
General Function Involved in zinc ion binding
Specific Function Catalyzes the reduction of trans-2-enoyl-CoA to acyl-CoA with chain length from C6 to C16 in an NADPH-dependent manner with preference to medium chain length substrate. May have a role in the mitochondrial synthesis of fatty acids.
Pathways
  • Fatty acid elongation
  • Fatty Acid Elongation In Mitochondria
  • Long-chain-3-hydroxyacyl-coa dehydrogenase deficiency (LCHAD)
Reactions
Acyl-CoA + NADP → trans-2,3-dehydroacyl-CoA + NADPH details
hexadecanoyl-CoA + NADP → (2E)-Hexadecenoyl-CoA + NADPH + Hydrogen Ion details
Octanoyl-CoA + NADP → (2E)-Octenoyl-CoA + NADPH + Hydrogen Ion details
Lauroyl-CoA + NADP → (2E)-Dodecenoyl-CoA + NADPH + Hydrogen Ion details
Tetradecanoyl-CoA + NADP → (2E)-Tetradecenoyl-CoA + NADPH + Hydrogen Ion details
Decanoyl-CoA (n-C10:0CoA) + NADP → (2E)-Decenoyl-CoA + NADPH + Hydrogen Ion details
trans-2-Hexenoyl-CoA + NADPH + Hydrogen Ion → Hexanoyl-CoA + NADP details
Acyl-CoA + NADP → trans-2,3-Dehydroacyl-CoA + NADPH + Hydrogen Ion details
GO Classification
Biological Process
fatty acid metabolic process
fatty acid biosynthetic process
Cellular Component
mitochondrion
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
zinc ion binding
oxidoreductase activity
Molecular Function
zinc ion binding
trans-2-enoyl-CoA reductase (NADPH) activity
nucleotide binding
Process
metabolic process
oxidation reduction
Cellular Location
  1. Mitochondrion
Gene Properties
Chromosome Location 1
Locus 1p35.3
SNPs MECR
Gene Sequence
>1122 bp
ATGTGGGTCTGCAGTACCCTGTGGCGGGTGCGAACCCCGCCCGGCAGTGGCGGGGGCCTG
CTCCCAGCTTCTGGCTGTCACGGACCTGCCGCCTCCTCCTACTCCGCATCCGCCGAGCCT
GCCCGGGTCCGCGGCGTTGTCTATGGGCACCACGGGGATCCAGCCAAGGTCGTCGAACTC
AAGAACCTGGAGCTAGCTGCTGTGAGAGGATCAGATGTCCGTGTGAAGATGCTGGCGGCC
CCTATCAATCCATCTGACATAAATATGATCCAAGGAAACTACGGACTCCTTCCTGAACTG
CCTGCTGTTGGAGGGAACGAAGGTGTTGCACAGGTGGTAGCGGTGGGCAGCAATGTGACC
GGGCTGAAGCCAGGAGACTGGGTGATTCCAGCAAATGCTGGTTTAGGAACCTGGCGGACC
GAGGCTGTGTTCAGCGAGGAAGCACTGATCCAAGTTCCGAGTGACATCCCTCTTCAGAGC
GCTGCCACCCTGGGTGTCAATCCCTGCACAGCCTACAGGATGTTGATGGACTTCGAGCAA
CTGCAGCCAGGGGATTCTGTCATCCAGAATGCATCCAACAGCGGAGTGGGGCAAGCGGTC
ATCCAGATCGCCGCAGCCCTGGGCCTAAGAACCATCAATGTGGTCCGAGACAGACCTGAT
ATCCAGAAGCTGAGTGACAGACTGAAGAGTCTGGGGGCTGAGCATGTCATCACAGAAGAG
GAGCTAAGAAGGCCCGAAATGAAAAACTTCTTTAAGGACATGCCCCAGCCACGGCTTGCT
CTCAACTGTGTTGGTGGGAAAAGCTCCACAGAGCTGCTGCGCCAGTTAGCGCGTGGAGGA
ACCATGGTAACCTATGGGGGGATGGCCAAGCAGCCCGTCGTAGCCTCTGTGAGCCTGCTC
ATTTTTAAGGATCTCAAACTTCGAGGCTTTTGGTTGTCCCAGTGGAAGAAGGATCACAGT
CCAGACCAGTTCAAGGAGCTGATCCTCACACTGTGCGATCTCATCCGCCGAGGCCAGCTC
ACAGCCCCTGCCTGCTCCCAGGTCCCGCTGCAGGACTACCAGTCTGCCTTGGAAGCCTCC
ATGAAGCCCTTCATATCTTCAAAGCAGATTCTCACCATGTGA
Protein Properties
Number of Residues 373
Molecular Weight 32228.0
Theoretical pI 7.214
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Trans-2-enoyl-CoA reductase, mitochondrial
MWVCSTLWRVRTPARQWRGLLPASGCHGPAASSYSASAEPARVRALVYGHHGDPAKVVEL
KNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGLLPELPAVGGNEGVAQVVAVGSNVT
GLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQ
LQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEE
ELRRPEMKNFFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLL
IFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEAS
MKPFISSKQILTM
GenBank ID Protein 4929595
UniProtKB/Swiss-Prot ID Q9BV79
UniProtKB/Swiss-Prot Entry Name MECR_HUMAN
PDB IDs
GenBank Gene ID AF151821
GeneCard ID MECR
GenAtlas ID MECR
HGNC ID HGNC:19691
References
General References
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  3. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed:10810093 ]
  4. Miinalainen IJ, Chen ZJ, Torkko JM, Pirila PL, Sormunen RT, Bergmann U, Qin YM, Hiltunen JK: Characterization of 2-enoyl thioester reductase from mammals. An ortholog of YBR026p/MRF1'p of the yeast mitochondrial fatty acid synthesis type II. J Biol Chem. 2003 May 30;278(22):20154-61. Epub 2003 Mar 24. [PubMed:12654921 ]