ID B8M1D3_TALSN Unreviewed; 357 AA.
AC B8M1D3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 13-SEP-2023, entry version 57.
DE SubName: Full=Short chain dehydrogenase/reductase family protein {ECO:0000313|EMBL:EED21829.1};
GN ORFNames=TSTA_090680 {ECO:0000313|EMBL:EED21829.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED21829.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962653; EED21829.1; -; Genomic_DNA.
DR RefSeq; XP_002478792.1; XM_002478747.1.
DR AlphaFoldDB; B8M1D3; -.
DR STRING; 441959.B8M1D3; -.
DR GeneID; 8101559; -.
DR VEuPathDB; FungiDB:TSTA_090680; -.
DR eggNOG; KOG1201; Eukaryota.
DR HOGENOM; CLU_010194_5_0_1; -.
DR InParanoid; B8M1D3; -.
DR OMA; NTLAHYW; -.
DR OrthoDB; 6845at2759; -.
DR PhylomeDB; B8M1D3; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR24322; PKSB; 1.
DR PANTHER; PTHR24322:SF736; RETINOL DEHYDROGENASE 10; 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.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
SQ SEQUENCE 357 AA; 39978 MW; A9F8D86EB0D57A51 CRC64;
MPNRILPREG FTADVIGSIL RQTVFDPVKT FLTILLFQYA PPNARYLPRH RETVLKWLRI
AFALGVIRRV NTFLGRRAIN RGISDEYDWP REIIVVTGGS NGFGKEQVLM LAKRARSKIA
ILDVMPPDYV LPGGVRFFKC DITSSDAIAA AATDIRREFG GDPTILINNA GIIYARPILE
NTDREIQKMF EVNTLSQYKL LHQFLPAIVR RNHGMIVTVA SQGGNCTTPG MTAYCASKAA
SINLHEGLAS ELVTRYNAPR VRTVLVTPAF AKTFVTRDLI PEDSFLSPLL EPETVAEAVV
DQVLKAESGY VGVSATANWF TFNLRSMPLW YQTGLRDRLD RTVQAPGKRH SWVKRDE
//
