ID A0A097ICZ1_9CORY Unreviewed; 348 AA.
AC A0A097ICZ1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=alcohol dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00024074};
DE EC=1.1.1.2 {ECO:0000256|ARBA:ARBA00024074};
GN ORFNames=CDOO_00675 {ECO:0000313|EMBL:AIT59995.1};
OS Corynebacterium doosanense CAU 212 = DSM 45436.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=558173 {ECO:0000313|EMBL:AIT59995.1, ECO:0000313|Proteomes:UP000029914};
RN [1] {ECO:0000313|EMBL:AIT59995.1, ECO:0000313|Proteomes:UP000029914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAU 212 {ECO:0000313|EMBL:AIT59995.1,
RC ECO:0000313|Proteomes:UP000029914};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium doosanense CAU 212(T) (=DSM
RT 45436(T)), isolated from activated sludge.";
RL Submitted (SEP-2013) 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; CP006764; AIT59995.1; -; Genomic_DNA.
DR RefSeq; WP_018022899.1; NZ_CP006764.1.
DR AlphaFoldDB; A0A097ICZ1; -.
DR STRING; 558173.CDOO_00675; -.
DR KEGG; cdo:CDOO_00675; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_2_11; -.
DR OrthoDB; 3567264at2; -.
DR Proteomes; UP000029914; Chromosome.
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:UP000029914};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..348
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 348 AA; 37249 MW; 06217DA1DC448636 CRC64;
MTTSTRAIGA HGPGRPLEPL EITRRELRND DIQIAIQFAG VCHSDIHTMN GDWGERQWPL
APGHEIVGIV SAVGSSVTAF TVGDRVGVGC FVNSCGECDP CSQGEISYCE RGAVGTYGDV
DRFSDGEYTQ GGYSRSIVVR ESFVLRIPDG LDPAGAAPLL CAGITTYSPL RHWNVGPGSR
VAVVGMGGLG HVGVKIALAM GAEVTVFSHS DRKRDDALAY GAKDLIATRD GLPRELRKHF
DFILNTVSAD IDINAYLGLL RFDGTLVQLG LPGEPMKIRA GSVVNRRGSL AGSLVGGIRE
TQEMLDFCGE HGITADIELI SADRINEAYE RTVAADVRYR FVIDASTI
//
