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Database: UniProt
Entry: A0A177HT20_9ACTN
LinkDB: A0A177HT20_9ACTN
Original site: A0A177HT20_9ACTN 
ID   A0A177HT20_9ACTN        Unreviewed;       353 AA.
AC   A0A177HT20;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
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:OAH13876.1};
GN   ORFNames=STSP_28540 {ECO:0000313|EMBL:OAH13876.1};
OS   Streptomyces jeddahensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH13876.1, ECO:0000313|Proteomes:UP000077381};
RN   [1] {ECO:0000313|EMBL:OAH13876.1, ECO:0000313|Proteomes:UP000077381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA   Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA   Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT   "Genome sequence of Streptomyces sp. G25.";
RL   Submitted (DEC-2015) 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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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:OAH13876.1}.
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DR   EMBL; LOHS01000072; OAH13876.1; -; Genomic_DNA.
DR   RefSeq; WP_067276855.1; NZ_LOHS01000072.1.
DR   AlphaFoldDB; A0A177HT20; -.
DR   STRING; 1716141.STSP_28540; -.
DR   PATRIC; fig|1716141.3.peg.3003; -.
DR   OrthoDB; 3567264at2; -.
DR   Proteomes; UP000077381; Unassembled WGS sequence.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) 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; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 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:OAH13876.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077381};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          20..348
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   353 AA;  37471 MW;  DBDD55318542DEDC CRC64;
     MTTPSAVSAV PAYAAPAPKA PLERTVIERR QVGEFDVLID IKFAGICHSD IHQAREGWGE
     AIFPMVPGHE IAGVVSEVGS GVTKYQVGDR VGVGCLVDSC RECENCKAGQ EQYCLNGSFG
     PTYNAIGRDG TPNYGGYSQK IVVDENYVVR IPDGLSLDVA APLLCAGITL YSPLKRWNAG
     PGKKVAILGL GGLGHMGVKI AHALGAEVTV LSQSLRKKDD GLKLGADHYY ATSDPKTFEE
     LRGTFDLIVS TVSAPLDFNA YLTLLKTEGA LVNVGAPEEP ISLNLFSVIG GGKTLAGSMI
     GGIGETQEML DFCAGHGFGA EIEMIRGDQI NEAYERVLAS DVRYRFVIDT ATI
//
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