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Database: UniProt
Entry: B8PQ01_POSPM
LinkDB: B8PQ01_POSPM
Original site: B8PQ01_POSPM 
ID   B8PQ01_POSPM            Unreviewed;       258 AA.
AC   B8PQ01;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EED77045.1};
DE   Flags: Fragment;
GN   ORFNames=POSPLDRAFT_28674 {ECO:0000313|EMBL:EED77045.1};
OS   Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS   (Poria monticola).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Postiaceae; Postia.
OX   NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN   [1] {ECO:0000313|EMBL:EED77045.1, ECO:0000313|Proteomes:UP000001743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX   PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA   Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA   Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA   Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA   Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA   Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA   Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA   Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA   Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA   Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA   Brettin T., Rokhsar D., Berka R., Cullen D.;
RT   "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT   placenta supports unique mechanisms of lignocellulose conversion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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DR   EMBL; EQ967280; EED77045.1; -; Genomic_DNA.
DR   RefSeq; XP_002477756.1; XM_002477711.1.
DR   AlphaFoldDB; B8PQ01; -.
DR   KEGG; ppl:POSPLDRAFT_28674; -.
DR   HOGENOM; CLU_010194_2_9_1; -.
DR   InParanoid; B8PQ01; -.
DR   OMA; YMGLPFR; -.
DR   OrthoDB; 4558660at2759; -.
DR   Proteomes; UP000001743; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd05374; 17beta-HSD-like_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR44169; NADPH-DEPENDENT 1-ACYLDIHYDROXYACETONE PHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR44169:SF6; NADPH-DEPENDENT 1-ACYLDIHYDROXYACETONE PHOSPHATE REDUCTASE; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001743}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EED77045.1"
FT   NON_TER         258
FT                   /evidence="ECO:0000313|EMBL:EED77045.1"
SQ   SEQUENCE   258 AA;  28308 MW;  6C8E1623E01DF9BA CRC64;
     LSPGCSKGGI GFALCQEFAA NGCKVYATAR RVEAMEGFTH EAIEKLRLDV TDDGNIEEAI
     KSIIDREGRI DVLVNNAGAP CFGPLAEMPI ERIKSTFDVN TFAILRLVNA VFPHMASRKR
     GTIVNIGSIV GEIPTAWGGT YSASKAAVRS ISESLYMECA PFGINVVHVS PGGIRSNIST
     NSRAEFRLSS DTLYTPFLDS MLRRMGMSQQ NALSAEEFSR RVVRQVLSKR PPRYMTLGKA
     SRIFVICSWL PRALVLWL
//
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