ID   K6VPH9_9MICO            Unreviewed;       347 AA.
AC   K6VPH9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Putative zinc-containing alcohol dehydrogenase {ECO:0000313|EMBL:GAB77280.1};
GN   ORFNames=AUCHE_05_01850 {ECO:0000313|EMBL:GAB77280.1};
OS   Austwickia chelonae NBRC 105200.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC   Austwickia.
OX   NCBI_TaxID=1184607 {ECO:0000313|EMBL:GAB77280.1, ECO:0000313|Proteomes:UP000008495};
RN   [1] {ECO:0000313|EMBL:GAB77280.1, ECO:0000313|Proteomes:UP000008495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 105200 {ECO:0000313|EMBL:GAB77280.1,
RC   ECO:0000313|Proteomes:UP000008495};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Ohji S.,
RA   Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Austwickia chelonae NBRC 105200.";
RL   Submitted (AUG-2012) 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:GAB77280.1}.
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DR   EMBL; BAGZ01000005; GAB77280.1; -; Genomic_DNA.
DR   RefSeq; WP_006502032.1; NZ_BAGZ01000005.1.
DR   AlphaFoldDB; K6VPH9; -.
DR   STRING; 100225.SAMN05421595_1100; -.
DR   eggNOG; COG1063; Bacteria.
DR   OrthoDB; 9797931at2; -.
DR   Proteomes; UP000008495; 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; cd08254; hydroxyacyl_CoA_DH; 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; L-THREONINE 3-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43401:SF2; 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:UP000008495};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          12..338
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   347 AA;  36916 MW;  C29EBD14D1E2CC69 CRC64;
     MVDSMLAARF HSAEKVTRLE EVPVPRPGPG EVLIEVAYCG ICHSDISLID GHFPALLPVV
     TQGHEASGTI VEVGSQVFGW AVGDRVIPAA GQACFRCRAC LRGALANCLD KRLMAFAYDG
     AWAKYHLAKA TGLTRIPEGV PMEQAALLAD AVSTPYAAVV RTAQVRLGES VGIWGLGGVG
     SHLVQLAKLA GGMPIIAVDI DDHALERALR LGADAALRSD DPQLGRQIAE LTSGRMLDVA
     FDAVGIPATL RQSVAWLDTE GRAVSVGMSD AEIEIGPILD FNLRRKQLLG HLGYQTQDVA
     SLAEMVSRGR LDLSESVSSI IALSDIHEGI SALRERRGNP IRILVQP
//