ID   A0A1M6CKT1_9FLAO        Unreviewed;       346 AA.
AC   A0A1M6CKT1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:SHI61635.1};
GN   ORFNames=SAMN04488508_102165 {ECO:0000313|EMBL:SHI61635.1};
OS   Aquimarina spongiae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aquimarina.
OX   NCBI_TaxID=570521 {ECO:0000313|EMBL:SHI61635.1, ECO:0000313|Proteomes:UP000184432};
RN   [1] {ECO:0000313|Proteomes:UP000184432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22623 {ECO:0000313|Proteomes:UP000184432};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FQYP01000002; SHI61635.1; -; Genomic_DNA.
DR   RefSeq; WP_073314770.1; NZ_FQYP01000002.1.
DR   AlphaFoldDB; A0A1M6CKT1; -.
DR   STRING; 570521.SAMN04488508_102165; -.
DR   OrthoDB; 9787435at2; -.
DR   Proteomes; UP000184432; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd08260; Zn_ADH6; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic 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; PTHR43401:SF5; ALCOHOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 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:UP000184432};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          11..343
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   346 AA;  37318 MW;  B08A7B7CF4A4B66E CRC64;
     MKAIVFEEFK GPLTEQNVQD PTPNPHSVVI KVTATGLCRS DWHGWMGHDP DIRLPHVPGH
     ELAGVIEATG KFVKNFKIGD RVTVPFVAGC GHCGECISGN HQVCDHQSQP GFTHWGSFAE
     YVAIDYADTN LVRLPDSIDD ETAATLGCRF ITSFRAVVEQ GKVSAGQFIA IHGCGGVGLS
     AIMIAKAIGA QVIAIDINDQ TLQFAKELGA FATINAKDQK HIVDEIRSLT NGGVHVSLDA
     LGSAATCFNS VANLRKRGKH IQVGLMTGDH AHPKIPMDMV LANELEVIGS HGMQAYKYPE
     MLQMISAGTL KPQKLIQKTI SLEDAITALP QMNTFQNMGV QVINSF
//