ID A0A023Y3J3_9GAMM Unreviewed; 387 AA.
AC A0A023Y3J3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:AHY59227.1};
GN ORFNames=DX03_11140 {ECO:0000313|EMBL:AHY59227.1};
OS Stenotrophomonas rhizophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=216778 {ECO:0000313|EMBL:AHY59227.1, ECO:0000313|Proteomes:UP000025222};
RN [1] {ECO:0000313|EMBL:AHY59227.1, ECO:0000313|Proteomes:UP000025222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14405 {ECO:0000313|Proteomes:UP000025222};
RA Alavi P., Starcher M.R., Thallinger G., Zachow C., Mueller H., Berg G.;
RT "Is there a border between beneficial and pathogenic bacteria?";
RL Submitted (APR-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; CP007597; AHY59227.1; -; Genomic_DNA.
DR RefSeq; WP_038688679.1; NZ_CP007597.1.
DR AlphaFoldDB; A0A023Y3J3; -.
DR STRING; 216778.DX03_11140; -.
DR GeneID; 61476477; -.
DR HOGENOM; CLU_026673_11_3_6; -.
DR Proteomes; UP000025222; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..384
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 387 AA; 41044 MW; E0EC72FBEFB32221 CRC64;
MRALTYHGSK DVRVDTVPDP VLAAPDDLIL RVTATAICGS DLHLYRGKIP DLHSGDVLGH
EFMGIVEEVG SGVSDLRPGD RVVIPFVIAC GSCFHCRLAE FAACETTNSG KGAATNQKGI
RPPAALFGYS HLYGGVSGGQ AEFVRVPKAN VGPLRIPDGL SDEQVLFLSD ILPTGYQAAI
NAGVKPGSSV AIFGAGPVGL MSAACCRLLG AETIFMVDHL AYRLDFAQRT YGVTPIDFTR
VDDPAEYIVT QTNGRGVDAT IEAVGFEAEG SALESALTTL KVEGSSGVAI RQCIAATRRG
GTVSIPGVYA GFVHGFLLGD AFDKGLTFKM GQTHVQKLMP ELLDHIAEGN LDPGVIVTHR
MPLEEAAKGY EIFDRKQEDC RKVILTP
//
