ID A0A1Q4X495_9ACTN Unreviewed; 234 AA.
AC A0A1Q4X495;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Beta-ketoacyl-ACP reductase {ECO:0000313|EMBL:OKI17140.1};
GN ORFNames=A6A08_07755 {ECO:0000313|EMBL:OKI17140.1};
OS Nocardiopsis sp. TSRI0078.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1718951 {ECO:0000313|EMBL:OKI17140.1, ECO:0000313|Proteomes:UP000185866};
RN [1] {ECO:0000313|EMBL:OKI17140.1, ECO:0000313|Proteomes:UP000185866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0078 {ECO:0000313|EMBL:OKI17140.1,
RC ECO:0000313|Proteomes:UP000185866};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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:OKI17140.1}.
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DR EMBL; LWLB01000023; OKI17140.1; -; Genomic_DNA.
DR RefSeq; WP_073703440.1; NZ_LWLB01000023.1.
DR AlphaFoldDB; A0A1Q4X495; -.
DR STRING; 1718951.A6A08_07755; -.
DR OrthoDB; 9804774at2; -.
DR Proteomes; UP000185866; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd05333; BKR_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; PTHR42879; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE; 1.
DR PANTHER; PTHR42879:SF2; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE FABG; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
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;
SQ SEQUENCE 234 AA; 24156 MW; AA15B28B350C281F CRC64;
MSRSVLVTGG NRGIGLAIAR ELAAGGDDVA VTYRSGEPPE GLLGVRCDIT DSAQVDAAFK
EVEEAQGPVE VLVANAGITK DQLLALMSEE DFSSVLDTNL TGSFRVTKRA VRGMMRKRSG
RVILISSVVG LLGSGGQANY AASKAGLVGF GRSLARELGS RNITVNVVSP GFVETDMTAA
LPEERQAEIR KNVPLGRIGA TEDIARTVAF LAGPGGSYIT GAVIPVDGGL GMGH
//
