ID   A6W9T5_KINRD            Unreviewed;       385 AA.
AC   A6W9T5;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Alcohol dehydrogenase zinc-binding domain protein {ECO:0000313|EMBL:ABS03574.1};
GN   OrderedLocusNames=Krad_2089 {ECO:0000313|EMBL:ABS03574.1};
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC   Kineococcus.
OX   NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS03574.1, ECO:0000313|Proteomes:UP000001116};
RN   [1] {ECO:0000313|Proteomes:UP000001116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC   {ECO:0000313|Proteomes:UP000001116};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J.,
RA   Fliermans C., Richardson P.;
RT   "Complete sequence of chromosome of Kineococcus radiotolerans SRS30216.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; CP000750; ABS03574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6W9T5; -.
DR   STRING; 266940.Krad_2089; -.
DR   KEGG; kra:Krad_2089; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_0_11; -.
DR   Proteomes; UP000001116; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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; 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.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001116};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          40..383
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   385 AA;  41763 MW;  D139A2AE66A68770 CRC64;
     MSAPHTLFCA GRRPDRAAKE QSMAETQTTG KTMQAVIVHG PHDYRLEEVP VPVAGPGEAL
     LKVEAVGICA SDLKCYHGAA KFWGDENRPA WAETDTVPGH EFTGRIAEID EEASERWGVV
     VGDRIVAEQI VPCWNCRYCN RGDYHMCQPH DMFGFKRRTP GAMAEYLVLP KEALVHKAPD
     DLPPWQVAYA EPLSCALHAV ERADIRFGDT VVVAGCGPIG LGMIAGAAAK FPQRIIALDA
     LPQKLELARK CGADVTLNIT EVDVVEEVKK LTGGYGADVY IEGTGHPSAV AQGLNLLRKL
     GTFVEYSVFK DPVTVDWSII SDDKELNVLG AHLGQNTWPA ALRLIASGRL PLDEICSHQL
     PLARFQEGLD LVADSANSVK VSLIP
//