ID A0A164JZ51_9NOCA Unreviewed; 350 AA.
AC A0A164JZ51;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-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 ORFNames=AWN90_40805 {ECO:0000313|EMBL:KZM70872.1};
OS Nocardia terpenica.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=455432 {ECO:0000313|EMBL:KZM70872.1, ECO:0000313|Proteomes:UP000076512};
RN [1] {ECO:0000313|EMBL:KZM70872.1, ECO:0000313|Proteomes:UP000076512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 0406 {ECO:0000313|EMBL:KZM70872.1,
RC ECO:0000313|Proteomes:UP000076512};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-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}.
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:KZM70872.1}.
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DR EMBL; LWGR01000013; KZM70872.1; -; Genomic_DNA.
DR RefSeq; WP_067594631.1; NZ_KV411304.1.
DR AlphaFoldDB; A0A164JZ51; -.
DR STRING; 455432.AWN90_40805; -.
DR OrthoDB; 3567264at2; -.
DR Proteomes; UP000076512; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000076512};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..345
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 350 AA; 37481 MW; 29A349329CE2FBCB CRC64;
MSTAAAYSVS AADGRFEKVT IERRELGAHD VLIDIKYAGI CHSDIHTARN EWHGTTYPCV
PGHEIAGIVA AVGSAVTRHK VGDRVGVGCM VDSCGECAAC VAGEQSYCLR GATMTYNTPV
PEAFQPGGHT LGGYSTQVVV TENFVLSIPE GIALDQAAPL LCAGITLYSP LRHWNTGPGK
RVAIIGMGGL GHVGVKLARA MGAEVTVLSQ SLRKKDDGLR LGAQHYYATS DEQTFRELRG
RFDLIINTVS ANLPIEDYMR LLNLDGTLVI LGLPDRPLAV QPFTLAAYRR SLAGSMIGGI
PQTQEMLNFC AEHGIGAEVE VISADRIDEA YDRAVASDVR YRFVIDAATM
//
