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Database: UniProt
Entry: A0A0M9Y8M6_9ACTN
LinkDB: A0A0M9Y8M6_9ACTN
Original site: A0A0M9Y8M6_9ACTN 
ID   A0A0M9Y8M6_9ACTN        Unreviewed;       268 AA.
AC   A0A0M9Y8M6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Ketoacyl reductase {ECO:0000313|EMBL:KOU35029.1};
GN   ORFNames=ADK51_05845 {ECO:0000313|EMBL:KOU35029.1};
OS   Streptomyces sp. WM6368.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415554 {ECO:0000313|EMBL:KOU35029.1, ECO:0000313|Proteomes:UP000037718};
RN   [1] {ECO:0000313|EMBL:KOU35029.1, ECO:0000313|Proteomes:UP000037718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6368 {ECO:0000313|EMBL:KOU35029.1,
RC   ECO:0000313|Proteomes:UP000037718};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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:KOU35029.1}.
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DR   EMBL; LGDA01000028; KOU35029.1; -; Genomic_DNA.
DR   RefSeq; WP_030390252.1; NZ_LGDA01000028.1.
DR   AlphaFoldDB; A0A0M9Y8M6; -.
DR   PATRIC; fig|1415554.3.peg.1218; -.
DR   Proteomes; UP000037718; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; PTHR42879; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE; 1.
DR   PANTHER; PTHR42879:SF2; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE FABG; 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;
SQ   SEQUENCE   268 AA;  27717 MW;  E6F7BA918F2B7ACA CRC64;
     MTAKAMDKAP ERPVALVTGA TSGIGLAVAR DLAARGHRVF VCARTEVKVK QTVADLQAEG
     LSVQGTAADV RDRTAVRDLV AAAVAAYGAP VSILVNNAGR SGGGATAHIT DELWHDVIDT
     NLNSVFLLTR EVLTSGGLGA EPWGRIINIA STAGKQGVLL GAPYSASKHA VVGFTKALGK
     ELAPTGTTVN AVCPGYVETP MAARVRTGYA QVWDTTEDYV QEQLESKIPL GRYSTPQEVA
     GLVGYLTTDL AASITAQALN VCGGLGNF
//
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