ID A0A263DKM4_9PSEU Unreviewed; 344 AA.
AC A0A263DKM4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=alcohol dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00024074};
DE EC=1.1.1.2 {ECO:0000256|ARBA:ARBA00024074};
GN ORFNames=CFP66_29760 {ECO:0000313|EMBL:OZM78518.1};
OS Pseudonocardia sp. MH-G8.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1854588 {ECO:0000313|EMBL:OZM78518.1, ECO:0000313|Proteomes:UP000216936};
RN [1] {ECO:0000313|EMBL:OZM78518.1, ECO:0000313|Proteomes:UP000216936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH-G8 {ECO:0000313|EMBL:OZM78518.1,
RC ECO:0000313|Proteomes:UP000216936};
RA Wang J., Leiva S., Huang J., Huang Y.;
RT "Non-contiguous finished genome sequence and description of Pseudonocardia
RT marinum sp. nov., an obligate marine actinomycete from a macroalgal
RT phycosphere.";
RL Submitted (JUL-2017) 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:OZM78518.1}.
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DR EMBL; NKYF01000017; OZM78518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263DKM4; -.
DR OrthoDB; 3567264at2; -.
DR Proteomes; UP000216936; 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; 3.90.180.10; 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; IPR029752; D-isomer_DH_CS1.
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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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:UP000216936};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 13..340
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 344 AA; 35436 MW; 0BAD33D53825B689 CRC64;
MHDITALAAT QPGGPLRPWT ATRRDPGRHD VAVRILYCGI CASDLSAIAH AQGDAPLVPG
HEIVGEVTAV GDDVSRFVPG DLVAIGNIVD SCRECPACLA GRENWCYSYP TLTYGGGADR
HGNPTYGGFS AEYVLDQHFV YTVPQGLDPA AVAPLLCAGV TTYAPLRRLG VGPGSTVGIV
GLGGLGHLAL KITRALGAET VQFTTSPGKA EAALALGAHD AVLSTDEKQM AAQAHRFDLV
LDTAGAPHAL APYLSTLAID GTLCLVGLQE GPLDVTPLDL VVGAKSIAGS GSGGTVETAE
MLEFCAEHAI SADIELVTTG GINEALARLA ASDVRYRFVV DMTS
//
