ID U5VVA7_9ACTN Unreviewed; 350 AA.
AC U5VVA7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Alcohol dehydrogenase superfamily protein {ECO:0000313|EMBL:AGZ40809.1};
GN ORFNames=AFR_12615 {ECO:0000313|EMBL:AGZ40809.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ40809.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ40809.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ40809.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
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DR EMBL; CP006272; AGZ40809.1; -; Genomic_DNA.
DR AlphaFoldDB; U5VVA7; -.
DR STRING; 1246995.AFR_12615; -.
DR KEGG; afs:AFR_12615; -.
DR PATRIC; fig|1246995.3.peg.2562; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_026673_3_4_11; -.
DR Proteomes; UP000017746; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd08276; MDR7; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR45033; -; 1.
DR PANTHER; PTHR45033:SF2; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C1773.06C; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000017746}.
FT DOMAIN 18..343
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 350 AA; 35702 MW; AC794EF1BA33E1C8 CRC64;
MGSSTMNRWT LTPGAGGGHE LTLQTAPVPE PGPGQIRVKV HAAAMNYRDA LVRDGHYGST
AASELVPLSD GAGVVDAVGA GVETWTAGDR VISVYFQGWA DGAPGPGKGL GLGSGTENGM
LAEYAILSAD RVTAAPATLS LTEAATLPCA GLTAWTALLG NRPYNARQLD ADDTVLVLGT
GGVSLFAVQL ARAFGAQVWA TTSDAGKRER LSGLGVAGVV DYTDVPSWGE HVFAATGGAQ
IVVNSAGGRS MDQSIAAVAF GGEIAYMGLF DFADVSPDLL TLMSKTASIR GVAVGSVAAQ
NDLVAAVDQW GVRPVIDEVV PFVDAPSAYE RHLSKDSFGK VVIQVDAAGS
//
