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Database: UniProt
Entry: Q1DE16_MYXXD
LinkDB: Q1DE16_MYXXD
Original site: Q1DE16_MYXXD 
ID   Q1DE16_MYXXD            Unreviewed;       328 AA.
AC   Q1DE16;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   24-JAN-2024, entry version 107.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase, mitochondrial {ECO:0000256|ARBA:ARBA00041058};
DE            EC=1.3.1.104 {ECO:0000256|ARBA:ARBA00038963};
DE   AltName: Full=2-enoyl thioester reductase {ECO:0000256|ARBA:ARBA00042123};
GN   OrderedLocusNames=MXAN_0845 {ECO:0000313|EMBL:ABF92060.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF92060.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF92060.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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:0000256|ARBA:ARBA00035831};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010371}.
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DR   EMBL; CP000113; ABF92060.1; -; Genomic_DNA.
DR   RefSeq; WP_011550967.1; NC_008095.1.
DR   AlphaFoldDB; Q1DE16; -.
DR   STRING; 246197.MXAN_0845; -.
DR   EnsemblBacteria; ABF92060; ABF92060; MXAN_0845.
DR   GeneID; 41358305; -.
DR   KEGG; mxa:MXAN_0845; -.
DR   eggNOG; COG0604; Bacteria.
DR   HOGENOM; CLU_026673_17_2_7; -.
DR   OMA; YGYTQSK; -.
DR   OrthoDB; 9788224at2; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd05282; ETR_like; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43981; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43981:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          10..322
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   328 AA;  34649 MW;  6614B81BE8CC90F0 CRC64;
     MKAVRFSAFG QPLKVVEVVE QPDVALKPGE ARVEVLATPI NPSDILTLSG QYGQLPKLPA
     VPGNEGVGRV VEVQDSSAVK VGDIVFLPLG AGTWCTHLVA PADSLLRVPP GTDLRQAAML
     FINPPTADLL LRDFIALQPG EWVIQNAANS AVGRSIITLA KQAGFKTLNV VRREELAPEL
     TALGADAVLL DSDELPERVR EVTGGAKVRL AIDAVGGEST QRLGDALARG GVVVNYGAMS
     GKGPRLSAAA TIFKDITLRG FWLVTWTKKT PREEQGALFA RLAKQVAEGA LHVPVEGTFP
     LESIQEALTR AMEGGRAGKV LLTPNGPL
//
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