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Database: UniProt
Entry: A0A1D7VLS0_9ACTN
LinkDB: A0A1D7VLS0_9ACTN
Original site: A0A1D7VLS0_9ACTN 
ID   A0A1D7VLS0_9ACTN        Unreviewed;       377 AA.
AC   A0A1D7VLS0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:AOP47706.1};
GN   ORFNames=SL103_16900 {ECO:0000313|EMBL:AOP47706.1};
OS   Streptomyces lydicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=47763 {ECO:0000313|EMBL:AOP47706.1, ECO:0000313|Proteomes:UP000094094};
RN   [1] {ECO:0000313|EMBL:AOP47706.1, ECO:0000313|Proteomes:UP000094094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=103 {ECO:0000313|EMBL:AOP47706.1,
RC   ECO:0000313|Proteomes:UP000094094};
RA   Jia N., Ding M.-Z., Gao F., Yuan Y.-J.;
RT   "Complete genome sequencing of Streptomyces lydicus 103 and metabolic
RT   pathways analysis of antibiotic biosynthesis.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         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; CP017157; AOP47706.1; -; Genomic_DNA.
DR   RefSeq; WP_069569850.1; NZ_CP017157.1.
DR   AlphaFoldDB; A0A1D7VLS0; -.
DR   KEGG; slc:SL103_16900; -.
DR   OrthoDB; 241504at2; -.
DR   Proteomes; UP000094094; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08282; PFDH_like; 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; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42813:SF3; GLUTATHIONE-INDEPENDENT FORMALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 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:UP000094094};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          25..137
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          185..255
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   377 AA;  40338 MW;  4566A4B16A03CBE6 CRC64;
     MKAVVYKGPF TVAVENVEKP NIQHPNEALV RITSTAICGS DLHMYEGRTA AEPGIVFGHE
     NMGVIEEVGQ GVTSLKEGDR VVMPFNVACG FCTNCVEGFT GFCLTVNPGF AGGAYGYVAM
     GPWVGGQAEY LRVPYADFNC LKLPPGNEHE TDFILLADIF PTGYHGCELA QVRPGESVAV
     YGGGPVGLMA AYSAMLRGAS KVFVVDRVAE RLEKAREIGA VPINFAEGNP VQQIKDQTDG
     AGTDKGVDAV GYQAMAHGEA REEPATVLNS LVETVRPTGA LGVPGLYVPA DPGGPDEEAK
     RGMLLVSIGK LFEKGLRMGT GQCNVKRYNR QLRDMIVAGR AKPSFVVSHE LPLDQAPSAY
     EKFDKRIEGY TKVVLHP
//
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