ID A0A0C9MR31_9FUNG Unreviewed; 355 AA.
AC A0A0C9MR31;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=MAM1_0303c09452 {ECO:0000313|EMBL:GAN09919.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN09919.1};
RN [1] {ECO:0000313|EMBL:GAN09919.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN09919.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; DF836592; GAN09919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9MR31; -.
DR STRING; 91626.A0A0C9MR31; -.
DR OrthoDB; 5353053at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 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.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 69..353
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 355 AA; 39701 MW; C694A01FB3C23393 CRC64;
MLSTSKKDTL TGWACTAKGE PLKEMELPLK TWDENCVDME IICCGMCGTD IHTLEEKFGS
CTNWPCVIGM YFNIEWHLTH VLNLHQGHEI VGKVTRVGKN VTNVCVGDRG GVGFQADSCG
KCEECLKGNE NMCTVRLVQT YNDNWYNGDK TYGGYANRWR GDYRFICKIP DSMTSEIAAS
FMCAGLTMYA PLKRAVSSKS VVGIMGIGGL GHFAILFAKA MGAKVVAMSQ TASKRSVALE
LGADEFLVTS DLKAMGSYKK QWIDYFNLLK AKGHFINLML GDWEFPPIDP ALLCFHQVYI
HGTLIGSPKE IEEMLAFADE HEIKPWITTY PMSKANEALE YFKARKPRFR LVLKN
//