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Database: UniProt
Entry: O87969_STRGR
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Original site: O87969_STRGR 
ID   O87969_STRGR            Unreviewed;       346 AA.
AC   O87969;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 115.
DE   RecName: Full=alcohol dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00024074};
DE            EC=1.1.1.2 {ECO:0000256|ARBA:ARBA00024074};
GN   Name=adhC2 {ECO:0000313|EMBL:SQA25361.1};
GN   ORFNames=NCTC13033_05112 {ECO:0000313|EMBL:SQA25361.1};
OS   Streptomyces griseus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1911 {ECO:0000313|EMBL:BAA32135.1};
RN   [1] {ECO:0000313|EMBL:BAA32135.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Umeyama T.;
RT   "Open reading frame encoded around afsA gene.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SQA25361.1, ECO:0000313|Proteomes:UP000251334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13033 {ECO:0000313|EMBL:SQA25361.1,
RC   ECO:0000313|Proteomes:UP000251334};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH;
CC         Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00023978};
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; AB011413; BAA32135.1; -; Genomic_DNA.
DR   EMBL; UAVD01000033; SQA25361.1; -; Genomic_DNA.
DR   RefSeq; WP_012382295.1; NZ_UAVD01000033.1.
DR   AlphaFoldDB; O87969; -.
DR   GeneID; 6215122; -.
DR   OMA; YRFSIDM; -.
DR   OrthoDB; 3567264at2; -.
DR   Proteomes; UP000251334; Unassembled WGS sequence.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046029; F:mannitol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF85; DEATH RESISTOR ADH DOMAIN CONTAINING TARGET, ISOFORM C; 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   ECO:0000313|EMBL:SQA25361.1}; Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          14..341
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   346 AA;  36549 MW;  24050592F0514A4E CRC64;
     MTTVAAYAAP RAKAPLERTT IERRPVGEFD ILIDIKFAGI CHSDIHQARD GWGEGIFPMV
     PGHEIAGIVA ETGPGVTRFK VGDRVGVGCM VDSCGTCDAC LMGREQHCAE GNTQTYNALD
     RNGEPTYGGY STHLVVTEKF ALSIPEGIAL DEAAPLLCAG ITTYSPLRRW GAGPGKKVAV
     VGLGGLGHMA VKIAHALGAE VTVLSQSLRK KDDGLKLGAD HYYATGDPRT FEELAGTFDV
     ILSTVSAPLD FGAYLALLRT EGTLVNVGAP EEPVSLNLFS LILGNRSIAG SAIGGIEETQ
     EMLDFCAVHG LGAEIEVIGA GQVNEAYERV LASDVRYRFV IDTATI
//
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