ID A0A165HJS2_9APHY Unreviewed; 338 AA.
AC A0A165HJS2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Aldo/keto reductase {ECO:0000313|EMBL:KZT11820.1};
GN ORFNames=LAESUDRAFT_754375 {ECO:0000313|EMBL:KZT11820.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT11820.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT11820.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT11820.1,
RC ECO:0000313|Proteomes:UP000076871};
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).
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DR EMBL; KV427606; KZT11820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165HJS2; -.
DR STRING; 1314785.A0A165HJS2; -.
DR InParanoid; A0A165HJS2; -.
DR OrthoDB; 5305445at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor; IEA:InterPro.
DR CDD; cd19120; AKR_AKR3C2-3; 1.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044494; AKR3C2/3.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR11732; ALDO/KETO REDUCTASE; 1.
DR PANTHER; PTHR11732:SF512; ALDO_KET_RED DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00248; Aldo_ket_red; 3.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 316..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..130
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT DOMAIN 151..209
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT DOMAIN 224..283
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 51
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 76
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 338 AA; 37311 MW; E42E6EFE2D2A160C CRC64;
MPFGKVLLSD GNQMPTIAFG TGSKWKGHDV TDYVLEAIEA GFSHIDTAQY YANEESVAAA
IRQSGLTRSE FFVTTKWSGQ AGVRESLEAS LSKLELKQID LYLVHSPVFI HDMEKDWREF
ERAKEDGLVK LALYPSTEIF GVHRANQQIR RSIGVSNFKL GQLQQLMKIA KFKPVANQIL
FHPYNYSQNK ELLSYCASHG VVVEAYGSLT PITIYPGGPV DKPVQAAADR LGATPTQVIL
SWVRSKGVVI VTTSSNPEHM REYIAVGDLP PLTEEEIEAI DAAGATGPPK LAILSHALTS
HLPVSVTSRA PALGRFLRII WLILSLLFFG WSFNRGRA
//
