ID C9YTQ3_STRSW Unreviewed; 346 AA.
AC C9YTQ3;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Putative alchohol dehydrogenase {ECO:0000313|EMBL:CBG72202.1};
GN OrderedLocusNames=SCAB_51631 {ECO:0000313|EMBL:CBG72202.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG72202.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG72202.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG72202.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; FN554889; CBG72202.1; -; Genomic_DNA.
DR AlphaFoldDB; C9YTQ3; -.
DR STRING; 680198.SCAB_51631; -.
DR KEGG; scb:SCAB_51631; -.
DR eggNOG; COG1062; Bacteria.
DR HOGENOM; CLU_026673_11_2_11; -.
DR Proteomes; UP000001444; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 9..344
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 346 AA; 36035 MW; 44EC452BD49DE7D4 CRC64;
MVFDGKRAEV VDDLAVRDPG PGEVLVAVSA AGLCHSDLSV VDGTIPFPVP VVLGHEGAGV
VEAVGAGVRH VRPGDHVALS TLANCGACAD CDRGRPTMCR SAIGRPTRPF SRAGRDVFQF
AANSAFAERT VVKAVQAVRI PDDIPLTSAA LIGCGVLTGV GAVLNRARVD RGDAVVVIGV
GGIGLNVVQG ARIAGATRIV AVDANPEKEA AARLFGATHF LTSTAGVRDI LPTGADHAFE
CVGRVQLVRQ AIDLLDRHGQ AVLLGVPAAT AEASFLVSSL YLDKSILGCR YGSSRPQRDI
ALYADLYREG RLLLDELVTA TYPVEEFAKA AQDAEEGRVA RAVLTF
//
