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Database: UniProt
Entry: A0A2S5BI10_9BASI
LinkDB: A0A2S5BI10_9BASI
Original site: A0A2S5BI10_9BASI 
ID   A0A2S5BI10_9BASI        Unreviewed;       316 AA.
AC   A0A2S5BI10;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=NADP-dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF00248};
GN   ORFNames=BMF94_0617 {ECO:0000313|EMBL:POY76419.1};
OS   Rhodotorula taiwanensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=741276 {ECO:0000313|EMBL:POY76419.1, ECO:0000313|Proteomes:UP000237144};
RN   [1] {ECO:0000313|EMBL:POY76419.1, ECO:0000313|Proteomes:UP000237144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD1149 {ECO:0000313|EMBL:POY76419.1,
RC   ECO:0000313|Proteomes:UP000237144};
RX   PubMed=29375494;
RA   Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA   Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA   Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA   Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT   "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT   Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL   Front. Microbiol. 8:2528-2528(2018).
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family.
CC       {ECO:0000256|ARBA:ARBA00007905}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:POY76419.1}.
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DR   EMBL; PJQD01000005; POY76419.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5BI10; -.
DR   STRING; 741276.A0A2S5BI10; -.
DR   OrthoDB; 5305445at2759; -.
DR   Proteomes; UP000237144; 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:SF507; ALDO-KETO REDUCTASE FAMILY 1 MEMBER A1; 1.
DR   PANTHER; PTHR11732; ALDO/KETO REDUCTASE; 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; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000237144}.
FT   DOMAIN          18..285
FT                   /note="NADP-dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00248"
FT   ACT_SITE        61
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT   SITE            86
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ   SEQUENCE   316 AA;  35118 MW;  EE2E93B10F952E41 CRC64;
     MANFTRAYQA GKTKIPAVGL GTWQSDTGLV REAVKTAIGA GYRRVDPSAR SHEHIDCAWV
     YKNENEVGQG IKDSGIDRKE LWVTSKLWNS FHQPEKVQSA LEESLKNLQL DYLDLYLMHW
     PVAFAKGKSE DGKQNIDWDL TNDVMPTWRA MEKLVEAGLV KHIGVSNFTI GRCKKLLEQA
     KIKPLANQVE LNLHCAQPEL VKWSKENGIL VESYSPLGST GAPQMEDEVV QAIAKSHGAT
     PAQVLISWQA ARGVIVLPKS VTADRIKSNF KEVELTTEEV TRLEKRAAEF GTKRTVDPSG
     AWGVPDLWKD APSGKM
//
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