MECR_XENTR
ID MECR_XENTR Reviewed; 350 AA.
AC Q28GQ2;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase, mitochondrial;
DE EC=1.3.1.104;
DE AltName: Full=2-enoyl thioester reductase;
DE Flags: Precursor;
GN Name=mecr; ORFNames=TEgg103l11.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18472403; DOI=10.1016/j.mod.2008.03.001;
RA Kyuno J., Masse K., Jones E.A.;
RT "A functional screen for genes involved in Xenopus pronephros
RT development.";
RL Mech. Dev. 125:571-586(2008).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of trans-2-enoyl
CC thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis
CC type II). Fatty acid chain elongation in mitochondria uses acyl carrier
CC protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP
CC and CoA thioesters as substrates in vitro (By similarity). Functions in
CC pronephros development, regulating late differentiation of all
CC pronephric tubule segments (PubMed:18472403).
CC {ECO:0000250|UniProtKB:Q9BV79, ECO:0000269|PubMed:18472403}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.104;
CC Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9BV79}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BV79}.
CC -!- TISSUE SPECIFICITY: Expressed in the developing pronephros.
CC {ECO:0000269|PubMed:18472403}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000255}.
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DR EMBL; CR761275; CAJ83709.1; -; mRNA.
DR RefSeq; NP_001016371.1; NM_001016371.2.
DR AlphaFoldDB; Q28GQ2; -.
DR SMR; Q28GQ2; -.
DR STRING; 8364.ENSXETP00000031439; -.
DR PaxDb; Q28GQ2; -.
DR GeneID; 549125; -.
DR KEGG; xtr:549125; -.
DR CTD; 51102; -.
DR Xenbase; XB-GENE-1007523; mecr.
DR eggNOG; KOG0025; Eukaryota.
DR HOGENOM; CLU_026673_17_1_1; -.
DR InParanoid; Q28GQ2; -.
DR OMA; RNSKHTE; -.
DR OrthoDB; 1269870at2759; -.
DR PhylomeDB; Q28GQ2; -.
DR TreeFam; TF312886; -.
DR Reactome; R-XTR-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000014371; Expressed in mesonephros and 31 other tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0039020; P:pronephric nephron tubule development; IMP:UniProtKB.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Mitochondrion; NADP; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 13..350
FT /note="Enoyl-[acyl-carrier-protein] reductase,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000391692"
FT ACT_SITE 68
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 141
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 167..170
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 190..192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 259..262
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 284..286
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 345
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
SQ SEQUENCE 350 AA; 38669 MW; 48814881CBDED83B CRC64;
MWLGLRLFHR PFSSLAARGL VYEKHGEPLQ VLRLKNVNIT HPADNEVRVK MLAAPINPSD
INMVQGTYAL LPQLPAVGGN EGVGVVVEIG RHVSSMRPGD WVVPVDAGLG TWCTEAVFSE
DSLVRVPSDI PVAGAATVSV NPCTAYRLLS DFETLRPGDT IIQNASNSGV GQAVIQIATS
LGITTINVVR DREDLSSLIQ RLRDLGADHV ITEEQLRKPE MKDLFKNCPR PRLALNCVGG
KSTTEMLRHL DYGGTMVTYG GMSKQPVTVP VSALIFKNVK LCGFWVTQWK KERAQTDREE
IVKMIRDLCD LIRRGKLVPP PSTQRPLEDF SRALQDSQTP FLSRKQILIM
