ID   H5X118_9PSEU            Unreviewed;       333 AA.
AC   H5X118;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Zn-dependent alcohol dehydrogenase {ECO:0000313|EMBL:EHR53077.1};
GN   ORFNames=SacmaDRAFT_4904 {ECO:0000313|EMBL:EHR53077.1};
OS   Saccharomonospora marina XMU15.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR53077.1, ECO:0000313|Proteomes:UP000004926};
RN   [1] {ECO:0000313|EMBL:EHR53077.1, ECO:0000313|Proteomes:UP000004926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XMU15 {ECO:0000313|EMBL:EHR53077.1,
RC   ECO:0000313|Proteomes:UP000004926};
RX   PubMed=22768369; DOI=10.4056/sigs.2655905;
RA   Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA   Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA   Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA   Woyke T.;
RT   "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT   type strain (XMU15(T)).";
RL   Stand. Genomic Sci. 6:265-275(2012).
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}.
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DR   EMBL; CM001439; EHR53077.1; -; Genomic_DNA.
DR   RefSeq; WP_009156455.1; NZ_CM001439.1.
DR   AlphaFoldDB; H5X118; -.
DR   STRING; 882083.SacmaDRAFT_4904; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_0_11; -.
DR   OrthoDB; 9787435at2; -.
DR   Proteomes; UP000004926; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR43161; SORBITOL 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:UP000004926};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          4..322
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   333 AA;  35130 MW;  03214C6A7C798EC5 CRC64;
     MRAVVLTKPH HVEVVDNWPR PTLRADEVLV GMRSVGLCGS DLAVHEGHRE PPALPWVMGH
     EGGGEILAVG TGVTQRHVGQ RVVVEPNYSC FQCDACLAGT TSACTGRGIV GMNLPGLLAE
     QVAVPARFTW PVPDSVSDAT LACVEPLAVA RAAVRRAHVR PGEQCLVVGA GSQGLFLCQA
     LLAAGAAPRV VEPIPGRLEL AERIGAARAS DTGEDSFAIV FDTAGTPQTW DISLRSVARM
     GTIVMIGMGS EPVSVSPMEL ARRQLRIRGS LIYDHPADFS ETVASVVDGS IRPSEVLHER
     FLPSDAATAF ALARSAPGKS WIDLSGWQEG SDG
//