ID J4H299_9APHY Unreviewed; 354 AA.
AC J4H299;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=FIBRA_03202 {ECO:0000313|EMBL:CCM01154.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM01154.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM01154.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM01154.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={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; HE797020; CCM01154.1; -; Genomic_DNA.
DR RefSeq; XP_012180437.1; XM_012325047.1.
DR AlphaFoldDB; J4H299; -.
DR STRING; 599839.J4H299; -.
DR GeneID; 24096065; -.
DR HOGENOM; CLU_026673_20_2_1; -.
DR InParanoid; J4H299; -.
DR OrthoDB; 5353053at2759; -.
DR Proteomes; UP000006352; 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; IPR029752; D-isomer_DH_CS1.
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:SF39; NADP-DEPENDENT 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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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:UP000006352};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 21..347
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 354 AA; 38822 MW; 1C79F2D87D7729C7 CRC64;
MSNTIQFKGY ALTGKYPRKW SDLQVLSYQP KTFQPDDVEI AITHCGVCGS DVHTLTQGWG
KSKLPLVVGH EIVGKVVRVG DNVKDIKAGD RVGVGAQIGS CMHCKSCESD YENYCPKGIP
TYNGEYPDGV ISQGGYSTAI RAHQQFVFPI PHEIESRHAA SMMCAGLTVY SPLKTHGAGP
GKKVGVVGIG GLGHYAVLWA KAMGAEVYAF THDSSKMDDI KKMGADHIDF HKPLSRALDL
IISTRDVFDQ NMSLDTYLSM LFVHGKFVTV GLPDANNVLP ETHAFSFVPS GCFLGGSAIG
SKKECLEMLD LARSKKIKPW IEEMPMCDVK KALEGVKQNK VRYRYILTQD IENK
//
