ID S0ETW4_CHTCT Unreviewed; 335 AA.
AC S0ETW4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=CCALI_01155 {ECO:0000313|EMBL:CCW34974.1};
OS Chthonomonas calidirosea (strain DSM 23976 / ICMP 18418 / T49).
OC Bacteria; Armatimonadota; Chthonomonadetes; Chthonomonadales;
OC Chthonomonadaceae; Chthonomonas.
OX NCBI_TaxID=1303518 {ECO:0000313|EMBL:CCW34974.1, ECO:0000313|Proteomes:UP000014227};
RN [1] {ECO:0000313|Proteomes:UP000014227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23976 / ICMP 18418 / T49
RC {ECO:0000313|Proteomes:UP000014227};
RA Lee K.C.Y., Morgan X.C., Dunfield P.F., Tamas I., Houghton K.M.,
RA Vyssotski M., Ryan J.L.J., Lagutin K., McDonald I.R., Stott M.B.;
RT "Genome sequence of Chthonomonas calidirosea, the first sequenced genome
RT from the Armatimonadetes phylum (formally candidate division OP10).";
RL Submitted (MAR-2013) 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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; HF951689; CCW34974.1; -; Genomic_DNA.
DR RefSeq; WP_016482519.1; NC_021487.1.
DR AlphaFoldDB; S0ETW4; -.
DR STRING; 454171.CP488_00003; -.
DR KEGG; ccz:CCALI_01155; -.
DR PATRIC; fig|1303518.3.peg.1178; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_7_0; -.
DR InParanoid; S0ETW4; -.
DR OrthoDB; 9806940at2; -.
DR Proteomes; UP000014227; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08298; CAD2; 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; IPR014187; ADH_Zn_typ-2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR02822; adh_fam_2; 1.
DR PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 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|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CCW34974.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014227};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..330
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 335 AA; 36676 MW; 7A84452C10160F47 CRC64;
MRAMVLTKPG PVEDLPLQLQ ELPKPKPHSG EVVIRVEVCG VCRTDLHVVE GELPPHKLPI
IPGHEVIGTI EYRGPEATRF PIGARVGVAW LHASCGKCTY CKRGDENLCD SPTFTGYDAD
GGYAEYVVAP EAFIYPIPPG VSSREAAPFL CAGIIGYRAL RRSNLRPGEP LGLYGFGASA
HIVIQIARYW DCPVYVCTRD EKHRELARQL GAVWVGSTEE RPPVKLRSSI LFAPAGELVP
IALSALDKGG TLALAGIYMT RIPSMDYEKH LFYERNLRSV TANTRQDGKE LLHLAETVPL
HTHTQEFPLE AANEALQALK QDRINGAAVL RVASS
//
