ID A0A1G7NXK9_9PSEU Unreviewed; 513 AA.
AC A0A1G7NXK9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=alcohol dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00024074};
DE EC=1.1.1.2 {ECO:0000256|ARBA:ARBA00024074};
GN ORFNames=SAMN05216553_103287 {ECO:0000313|EMBL:SDF78762.1};
OS Lentzea fradiae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=200378 {ECO:0000313|EMBL:SDF78762.1, ECO:0000313|Proteomes:UP000199623};
RN [1] {ECO:0000313|Proteomes:UP000199623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3506 {ECO:0000313|Proteomes:UP000199623};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNCC01000003; SDF78762.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7NXK9; -.
DR STRING; 200378.SAMN05216553_103287; -.
DR OrthoDB; 3567264at2; -.
DR Proteomes; UP000199623; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 1.
DR Gene3D; 3.30.530.20; -; 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 InterPro; IPR019587; Polyketide_cyclase/dehydratase.
DR InterPro; IPR023393; START-like_dom_sf.
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 Pfam; PF10604; Polyketide_cyc2; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF55961; Bet v1-like; 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 Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 180..508
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 151..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 54592 MW; 2C3F245DBCD25243 CRC64;
MKEHSIALST PADADEVFDL LLNPSRFSCA DIESVEPSEE GDRYALRFRG GLARWTQRTE
ADRAARVLRF EQVSGDFVDF GGSWEVTPDG AGSRVVHRVS FRTSVPHLAG AVDPMIARVL
LRAAAGVVDG LAGPAVIVEG TLHDEIAVPS QQDPPVEKAH DRTASPGPTL AAAYAAPSPG
APLEPATITR RPLRPTDVAI AIHYCGICHS DVHQVHGDWG GGTFPMVPGH EITGIVTAIG
ADVTRHAVGD RVGVGVIIGS CRDCAECEEG LEQYCSHSVE VYAAVDPHDG EPTRGGYSTH
IVADEHFVLR IPDALPLDQA APLLCAGITT YSPLKHWAAG PGKKVAVLGL GGLGHLAVKI
ANAMGAEVTV LSRSSRKEAD GLNLGADHFH ATDDPATFER LAGTFDLIVC TVACRLDVDT
YLSLLANGGT MVYLGITEEP LDVSVFSLLR SRTSLAGSRI GGMDETQEML DFCAEHGIRA
EIEVIDAAQV NEAFDRVRHG DVRYRFVIDA KTI
//
