ID Q0SCU9_RHOJR Unreviewed; 371 AA.
AC Q0SCU9;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN OrderedLocusNames=RHA1_ro02832 {ECO:0000313|EMBL:ABG94637.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG94637.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={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; CP000431; ABG94637.1; -; Genomic_DNA.
DR RefSeq; WP_011595525.1; NC_008268.1.
DR AlphaFoldDB; Q0SCU9; -.
DR KEGG; rha:RHA1_ro02832; -.
DR PATRIC; fig|101510.16.peg.2865; -.
DR eggNOG; COG1062; Bacteria.
DR HOGENOM; CLU_026673_14_1_11; -.
DR OrthoDB; 334894at2; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08279; Zn_ADH_class_III; 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; IPR023921; ADH_Zn_actinomycetes.
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 NCBIfam; TIGR03989; Rxyl_3153; 1.
DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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:ABG94637.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 12..368
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 371 AA; 39399 MW; BE4D94660F512E4B CRC64;
MKTQAAVLWE PGQPWQIEEL ELDPPKHGEV LLQLAASGMC HSDEHVRDGS LPLEYYPFIG
GHEGAGVVLE VGPGVTSVEK GDHVALGFIP ACGRCRQCAT GQSSICDLGA HLLEGWQISD
GTARHHVRGK DAAIQCLIGT FSPYTVVNEA SCVKITKDIP LDKAALVGCG VTTGWGSSVY
AAGVQAGETV VVIGMGGVGC GAVQGAALAG ARHVVVVDPA EFKREQAKIF GATHTAASID
EALPLLQDLT WGQLADKVLI TVANASGRII APAMSLVAKG GTCVHVSVGD VTQNDVDLNL
FDLTAMRKTL KGAWFGNANI RFDIPHLLRL YMEGQLKLDE MITRTYTLDQ INDGYEAMRK
AENVRGVIMY S
//
