ID B8MG49_TALSN Unreviewed; 305 AA.
AC B8MG49;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=3-oxoacyl-[acyl-carrier-protein] reductase, putative {ECO:0000313|EMBL:EED15916.1};
GN ORFNames=TSTA_010340 {ECO:0000313|EMBL:EED15916.1};
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:EED15916.1, 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ962656; EED15916.1; -; Genomic_DNA.
DR RefSeq; XP_002483150.1; XM_002483105.1.
DR AlphaFoldDB; B8MG49; -.
DR STRING; 441959.B8MG49; -.
DR GeneID; 8105673; -.
DR VEuPathDB; FungiDB:TSTA_010340; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_8_2_1; -.
DR InParanoid; B8MG49; -.
DR OMA; MAVYRLW; -.
DR OrthoDB; 2513531at2759; -.
DR PhylomeDB; B8MG49; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 CDD; cd05233; 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; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR42901; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR42901:SF1; ALCOHOL DEHYDROGENASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SMART; SM00822; PKS_KR; 1.
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}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 305 AA; 33107 MW; 1420708E5797C882 CRC64;
MAAPFPSPTA KWHTTTYPTL SPARPELSAK GRTVLITGGG TGIGAETARY FAQAGASRIA
LLGRREQPLL DTKASIEQIN GDVDVFVAPT DITNKEQVDA AFDRFVGGDQ PGKIDILISN
AAIVGPLNPI SSVDADQFLD AINVIIKGSL YVAQAFLRHA VPQDAVIVET NSSAAHLNFA
PAFVSYSVAK LAVYRLWDSL GFEFEKAGMR VYHVQPGVVN TDMNKEAGGV KAVGFEDHVS
LPASFNLWLT SPEAKFLKGK FLWANWDVDE LKIRAKEIEE GSEFNIQVVG WPFGEKNWKS
GWQVS
//
