ID A0A2G4SG64_RHIZD Unreviewed; 372 AA.
AC A0A2G4SG64;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 ORFNames=RHIMIDRAFT_309635 {ECO:0000313|EMBL:PHZ07761.1};
OS Rhizopus microsporus ATCC 52813.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ07761.1, ECO:0000313|Proteomes:UP000242254};
RN [1] {ECO:0000313|EMBL:PHZ07761.1, ECO:0000313|Proteomes:UP000242254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ07761.1,
RC ECO:0000313|Proteomes:UP000242254};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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; KZ303871; PHZ07761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4SG64; -.
DR STRING; 1340429.A0A2G4SG64; -.
DR OrthoDB; 6213at2759; -.
DR Proteomes; UP000242254; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd08290; ETR; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000242254};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 39..370
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 372 AA; 41394 MW; 1AEF59CBCCF09AD6 CRC64;
MGFLVYSLRQ RVSVNQYVAR RYYTSDITAK AMVYSDYGQP SQVLRMHSFK LPALTADTVH
VKFLASPINP ADVNMIQGAY PIKPMMQKLG DSELAVGGNE GVAEVIAVGE QVKDLKVGDQ
VVMAKSGYGT WRTHAAGLAS DFQLLPKIEV PLIQKATMTV NPCTAYRMLK DFVKLNPGDY
VIQNGGNSAV GQAVIQIAKA WGLNTINIVR NRPELDQLVN ELEEIGATHV ITDEELGSHE
MRKRIKSWVG DKPPLLGLNC VGGKPATEMA RYLGTNGQYV TYGAMSKSPL TLPASLLIFK
NISFHGFWVS KWAEIHKPEE RYAMFEDVME LMKQGKLREP KWTRVEFEQE EMKKAVDLGI
SGFSKGKQVV MF
//
