ID   A0A263DVY3_9PSEU        Unreviewed;       341 AA.
AC   A0A263DVY3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:OZM82840.1};
GN   ORFNames=CFP66_09210 {ECO:0000313|EMBL:OZM82840.1};
OS   Pseudonocardia sp. MH-G8.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1854588 {ECO:0000313|EMBL:OZM82840.1, ECO:0000313|Proteomes:UP000216936};
RN   [1] {ECO:0000313|EMBL:OZM82840.1, ECO:0000313|Proteomes:UP000216936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MH-G8 {ECO:0000313|EMBL:OZM82840.1,
RC   ECO:0000313|Proteomes:UP000216936};
RA   Wang J., Leiva S., Huang J., Huang Y.;
RT   "Non-contiguous finished genome sequence and description of Pseudonocardia
RT   marinum sp. nov., an obligate marine actinomycete from a macroalgal
RT   phycosphere.";
RL   Submitted (JUL-2017) 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}.
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:OZM82840.1}.
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DR   EMBL; NKYF01000002; OZM82840.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A263DVY3; -.
DR   OrthoDB; 334894at2; -.
DR   Proteomes; UP000216936; 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; cd05284; arabinose_DH_like; 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; 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:UP000216936};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..339
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   341 AA;  35689 MW;  51F8E7DB45B82D3B CRC64;
     MRAVQVIGYH RDLEMTEVPA PSAVDPHDVI VRIGGAGVCR TDIHILEGQW EQKSGVTLPY
     TIGHENAGWV HAVGSAVTNV AEGDKVIVHP LMTCGLCRAC RSGDDVHCAR SQFPGIDTHG
     GYAEYLRTTA RSVVKLDDSL EPADVAALAD AGLTAYHAAA NAARRLRPGD RCVVIGAGGL
     GHIGIQVLAA LTAAELVVVD RNPDAVDLGR SVGAHHGVVA DGTHVAQVAE LTGGEGAEVV
     LDFVGEGGST REGLAMTRRA GDYHVVGYGE NVDVPTIDLV SAEINIIGNL VGSYGDLCEL
     MVLAARGKVT LHTTKYPLAD FQKAIDDLDA GRVRGRAILI P
//