ID A0A089WNY3_9PSED Unreviewed; 390 AA.
AC A0A089WNY3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:AIR91020.1};
GN ORFNames=LK03_17865 {ECO:0000313|EMBL:AIR91020.1};
OS Pseudomonas cremoricolorata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=157783 {ECO:0000313|EMBL:AIR91020.1, ECO:0000313|Proteomes:UP000029493};
RN [1] {ECO:0000313|EMBL:AIR91020.1, ECO:0000313|Proteomes:UP000029493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND07 {ECO:0000313|EMBL:AIR91020.1,
RC ECO:0000313|Proteomes:UP000029493};
RA Chan K.-G.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361277}.
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DR EMBL; CP009455; AIR91020.1; -; Genomic_DNA.
DR RefSeq; WP_038413692.1; NZ_CP009455.1.
DR AlphaFoldDB; A0A089WNY3; -.
DR STRING; 157783.LK03_17865; -.
DR KEGG; psw:LK03_17865; -.
DR eggNOG; COG1063; Bacteria.
DR OrthoDB; 9773078at2; -.
DR Proteomes; UP000029493; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08283; FDH_like_1; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029493};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..386
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 390 AA; 41676 MW; F6339964254F1661 CRC64;
MLALTYQGAG EVKVLSVPDP VIEQDDDVLV RVRLSGICGS DLHLYHDKIP SVRKGDILGH
EFMGTVVKVG SAVTAVAEGD RVVVPFIIAC GECFFCKQEQ YAACETTNPT SAVISGEHAT
RSGAALFGYG HLYGGVPGGQ AEYVRVPKGN INAFKVPDDI SDEAALLLSD TLPTAWQAIK
NAKVDKGSSV AIFGAGPVGL LAAEIAQMLG ATQIFLVDEY SYRLKFAAET YGVIPVNFYH
DNDPARTIVN ATVDQRGVDA VIDAVGFEAS GTTVEAVMNM FGFEGSSGKA LRQCIEAVRR
GGVVSVAGMY SGLMHSLQLG AAFDKGLSFH MGKTHVHAYL PELCKHLQAG SLRPERLITH
RLSLNEAVQG YEMYDEKRPG CCKVILTLDS
//