ID C6R8P9_9CORY Unreviewed; 350 AA.
AC C6R8P9;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=alcohol dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00024074};
DE EC=1.1.1.2 {ECO:0000256|ARBA:ARBA00024074};
GN ORFNames=CORTU0001_2009 {ECO:0000313|EMBL:EET77769.1};
OS Corynebacterium tuberculostearicum SK141.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=553206 {ECO:0000313|EMBL:EET77769.1, ECO:0000313|Proteomes:UP000004384};
RN [1] {ECO:0000313|EMBL:EET77769.1, ECO:0000313|Proteomes:UP000004384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK141 {ECO:0000313|EMBL:EET77769.1,
RC ECO:0000313|Proteomes:UP000004384};
RA Dodson R., Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B.,
RA Sutton G.G., Strausberg R.L., Nelson K.E.;
RL Submitted (JUN-2009) 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:EET77769.1}.
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DR EMBL; ACVP01000012; EET77769.1; -; Genomic_DNA.
DR RefSeq; WP_005327690.1; NZ_ACVP01000012.1.
DR AlphaFoldDB; C6R8P9; -.
DR Proteomes; UP000004384; 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 Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 15..343
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 350 AA; 37634 MW; 148836E5A0CAE44F CRC64;
MTIKSKVLQK ESPEAPFKVV EIERRDPRED DVVIDIKAAG ICHSDIHTIR NEWGQAHFPL
TVGHEIAGVV EAVGDKVTKF KVGDRVGVGC LVNSCGECEQ CRNGQEQNCL NGNVGTYNSE
DVDGTITQGG YAQKVVVNEN FVCTIPEGID FDVAAPLLCA GITTYSPLAR WQVKEGDKVA
VVGLGGLGHM GVQIAAAKGA EVTVISRSLR KEKEAYELGA KHILATGEEE DFFANHRGEF
DVILSTISAQ YSLDDYLQLL KPRGIMSVVG LPPEELGIHM SSLVGGGKVL TGNNIGGIAE
TQEMLDFCAE HGIGAVIEKI GVNDVDDAYE RVVAGDVKFR FVIDTATFDD
//
