ID F8NS50_SERL9 Unreviewed; 357 AA.
AC F8NS50;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=SERLADRAFT_464454 {ECO:0000313|EMBL:EGO26883.1};
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1] {ECO:0000313|EMBL:EGO26883.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO26883.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "Evolution of plant cell wall degrading machinery underlies the functional
RT diversity of forest fungi.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL945432; EGO26883.1; -; Genomic_DNA.
DR RefSeq; XP_007317056.1; XM_007316994.1.
DR AlphaFoldDB; F8NS50; -.
DR GeneID; 18818743; -.
DR KEGG; sla:SERLADRAFT_464454; -.
DR HOGENOM; CLU_026673_29_2_1; -.
DR OrthoDB; 179761at2759; -.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd05288; PGDH; 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; IPR041694; ADH_N_2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR045010; MDR_fam.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43205:SF19; AGL360WP; 1.
DR PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1.
DR Pfam; PF16884; ADH_N_2; 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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 24..352
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 357 AA; 38697 MW; CB880A87A7372829 CRC64;
MSHLPTTTKA WILQNPPVKN IILGNSESST FSIQEQTLPP LDKGDLLVQP IYLSNDPAQR
GWIQRKLDEG RLYVTPVLQG QAMATHAVAR VLATAGPTST WKEGDLVYTT TTGWRQYAVV
KEEDVRSLRS IPGLSPSLYV GLFGVPGLTA YFGVTEVLKL QRGQSLVVSA AAGAVGNVVV
QYAKKVIGAS KVIAIAGTPE KCAWIKEMGA DIALNYKAPS FKQDLNAATE GFVDAYFDNV
GGEILDQMLT RIKQHGRVAA CGAISNYTHD NLDAANLRNW FEIITSRLTV KGFIVLDYFP
RAGEAVEALS KAVEEGKMTV EGAETLVETD FSNIPEVWLR LFQGQNVGKL VTQIAGA
//