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Database: UniProt
Entry: Q5SL93_THET8
LinkDB: Q5SL93_THET8
Original site: Q5SL93_THET8 
ID   Q5SL93_THET8            Unreviewed;       344 AA.
AC   Q5SL93;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=Zinc-binding dehydrogenase {ECO:0000313|EMBL:BAD70223.1};
GN   OrderedLocusNames=TTHA0400 {ECO:0000313|EMBL:BAD70223.1};
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852 {ECO:0000313|EMBL:BAD70223.1, ECO:0000313|Proteomes:UP000000532};
RN   [1] {ECO:0000313|EMBL:BAD70223.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HB8 {ECO:0000313|EMBL:BAD70223.1};
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) 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}.
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DR   EMBL; AP008226; BAD70223.1; -; Genomic_DNA.
DR   RefSeq; WP_011172490.1; NC_006461.1.
DR   RefSeq; YP_143666.1; NC_006461.1.
DR   AlphaFoldDB; Q5SL93; -.
DR   EnsemblBacteria; BAD70223; BAD70223; BAD70223.
DR   GeneID; 3168639; -.
DR   KEGG; ttj:TTHA0400; -.
DR   PATRIC; fig|300852.9.peg.400; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_3_0; -.
DR   PhylomeDB; Q5SL93; -.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08284; FDH_like_2; 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; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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:UP000000532};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..342
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   344 AA;  36236 MW;  7376690DA2232167 CRC64;
     MRAVVYKGPF QVAVEEVPEP RLEADTDALL EVELSAICGS DLHIYHGKIA GVLPGTVLGH
     EFVGRIVEKG PLVPFPVGER VVGSFQVACG ECPACRKGQF FACSRGGVFG FGLALGNLPG
     AQAERVRVPF ARHTLFPIGD LPAEEAILAG DILTTAYGGV RPFLTPGMSV AVVGSGPVGL
     MAQMVAHALG AGQVYAIDPE EARLEKAKAL GSLPIHPKAE DPVARVRRET EGLGADLVVE
     AVGGDGEALK LALRLAGPGG VVSSLGVPTA ERLDYPWLPA FSRGITLRSA LANVPRWIGE
     VLALQKAGRL KGSFVFSHRL PLEEAPEGYR LFHERKATKV ALVP
//
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