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Database: UniProt
Entry: K5VSV4_PHACS
LinkDB: K5VSV4_PHACS
Original site: K5VSV4_PHACS 
ID   K5VSV4_PHACS            Unreviewed;       311 AA.
AC   K5VSV4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=NADP-dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF00248};
GN   ORFNames=PHACADRAFT_106246 {ECO:0000313|EMBL:EKM49830.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM49830.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM49830.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM49830.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
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DR   EMBL; JH930480; EKM49830.1; -; Genomic_DNA.
DR   RefSeq; XP_007401882.1; XM_007401820.1.
DR   AlphaFoldDB; K5VSV4; -.
DR   GeneID; 18907388; -.
DR   KEGG; pco:PHACADRAFT_106246; -.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   InParanoid; K5VSV4; -.
DR   OrthoDB; 5305445at2759; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd19071; AKR_AKR1-5-like; 1.
DR   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR11732; ALDO/KETO REDUCTASE; 1.
DR   PANTHER; PTHR11732:SF459; ALDO_KET_RED DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370}.
FT   DOMAIN          58..297
FT                   /note="NADP-dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00248"
FT   ACT_SITE        83
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT   SITE            108
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ   SEQUENCE   311 AA;  34777 MW;  7E6DD71F818ED7FE CRC64;
     MFAGFKGLKA YIKSTVQWLH KQPCNRTQGN YNTELPSYYL LPSGDQIPSV ALGVSKASPG
     DVGQAVTAAL KTGYRHIDGA WTYRNEEEIG KAIKESGIPR DQIWLTSKLW TTFHAPDDVE
     PALDESLTKL GTEYLDLYII HWPIAHKKGG KDELDVALTA NPYPTWKKLE EMVDKGKVRN
     IGISNFNIGR VKNLTGNPLK YQPAVNQVEL NFWNPQPELI EWARDNKLLL QSFSPLGGSK
     RAKETLNVPE ITEIAKKLNI TPAQVIISWH VQRGTVVLPK SVTPSRIEEN FKIFALPGDL
     FDMLETAAEG I
//
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