ID A0A166LI84_9AGAM Unreviewed; 377 AA.
AC A0A166LI84;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=GroES-like protein {ECO:0000313|EMBL:KZV76907.1};
GN ORFNames=PENSPDRAFT_621820 {ECO:0000313|EMBL:KZV76907.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV76907.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV76907.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV76907.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; KV424461; KZV76907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166LI84; -.
DR STRING; 1314672.A0A166LI84; -.
DR InParanoid; A0A166LI84; -.
DR OrthoDB; 3017546at2759; -.
DR Proteomes; UP000077086; 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; cd05285; sorbitol_DH; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR045306; SDH-like.
DR PANTHER; PTHR43161:SF25; ALCOHOL DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14390)-RELATED; 1.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000077086};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 16..373
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 377 AA; 40343 MW; DC1F7A7F3BBB0EF6 CRC64;
MSPVSLPTQH AAVLYGSKDL RYEQRTLVAP QFDQAQVAVQ ATGLCGSDLH YYMHGRNGDF
ALQAPLVLGH EAAGIVTAVG SGVTDLTVGQ RVAIEAGIMC KKCDYCSKGR YNLCKELRFA
SSAKTFPHLD GTLQERMNHP AHVLHPLPDS CTFEQAALAE PLSVILHAAR RAQLEAGQTV
LVYGAGAIGL LACALAKARG ARRVVVVDIN QARLSFAQEN GFAQQTFCLP AAARPKTPEE
QLQRAKESGE LILEAFKEAD GFDCIFECTG AEPCIQMAIH TAITGGKLML IGMGTRSTTL
PLSAAALREV DIQGSFRYAN TYPEALELLG SGKLANLDKL VTHRFSLADT AKAFDLLSKG
VDEQGQMALK VVIGSSE
//
