ID   A0A0Q4L1D6_9SPHN        Unreviewed;       360 AA.
AC   A0A0Q4L1D6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KQN28407.1};
GN   ORFNames=ASF00_11210 {ECO:0000313|EMBL:KQN28407.1};
OS   Sphingomonas sp. Leaf34.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736216 {ECO:0000313|EMBL:KQN28407.1, ECO:0000313|Proteomes:UP000051932};
RN   [1] {ECO:0000313|EMBL:KQN28407.1, ECO:0000313|Proteomes:UP000051932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf34 {ECO:0000313|EMBL:KQN28407.1,
RC   ECO:0000313|Proteomes:UP000051932};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN28407.1, ECO:0000313|Proteomes:UP000051932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf34 {ECO:0000313|EMBL:KQN28407.1,
RC   ECO:0000313|Proteomes:UP000051932};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {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:KQN28407.1}.
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DR   EMBL; LMLC01000003; KQN28407.1; -; Genomic_DNA.
DR   RefSeq; WP_055878534.1; NZ_LMLC01000003.1.
DR   AlphaFoldDB; A0A0Q4L1D6; -.
DR   OrthoDB; 9770544at2; -.
DR   Proteomes; UP000051932; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08279; Zn_ADH_class_III; 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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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          10..357
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   360 AA;  37848 MW;  75DB0300732D6530 CRC64;
     MKAAVLFEAN TPLSIEDVTI SKPGPREVLI RTMAVGVCRS DLHFVDGAYP HAMPTIPGHE
     ACGVVEAIGD EVGMVKVGDH VVTCLSAFCG HCEFCVTGRM ALCVDSSVRR PKGAPPRLML
     GDRPIAQMLN LSAYAEMMLV HEHACVAIDR DMPMDRAALL GCAITTGAGA VFNTTDVTPG
     ETVCVVGCGG IGLAAVNAAK IAGAGKIIAL DPVPEKRAMA EKLGATHSID ALSDTAADEV
     VSLTKGGVHH AIEAVGRAQS AATAVKVLRR GGTATILGMM PLGEKVGLSA MDLLSGKRLQ
     GGFMGSNRFP VDIPRLVDFY MRGLLDLDTI IADRMPLERI NDAFDELRRG DTTRSVITFS
//