ID F5YUX0_MYCSD Unreviewed; 363 AA.
AC F5YUX0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN Name=adhD_1 {ECO:0000313|EMBL:AEF36351.1};
GN OrderedLocusNames=JDM601_2351 {ECO:0000313|EMBL:AEF36351.1};
OS Mycolicibacter sinensis (strain JDM601) (Mycobacterium sinense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF36351.1, ECO:0000313|Proteomes:UP000009224};
RN [1] {ECO:0000313|EMBL:AEF36351.1, ECO:0000313|Proteomes:UP000009224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDM601 {ECO:0000313|EMBL:AEF36351.1,
RC ECO:0000313|Proteomes:UP000009224};
RX PubMed=21685274; DOI=10.1128/JB.05291-11;
RA Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., Song Y.Z.,
RA Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.;
RT "Complete genome sequence of a novel clinical isolate, the nontuberculous
RT Mycobacterium strain JDM601.";
RL J. Bacteriol. 193:4300-4301(2011).
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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; CP002329; AEF36351.1; -; Genomic_DNA.
DR AlphaFoldDB; F5YUX0; -.
DR STRING; 875328.JDM601_2351; -.
DR KEGG; mjd:JDM601_2351; -.
DR eggNOG; COG1062; Bacteria.
DR HOGENOM; CLU_026673_14_1_11; -.
DR OMA; VCEMSGH; -.
DR Proteomes; UP000009224; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000009224};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 4..360
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 363 AA; 38164 MW; BE701A0978D8B974 CRC64;
MAHAPNQPFE IMELDLDGPG PGEVLIKFTA AGLCHSDLHL ADGDWPARFP IVGGHEGSGI
IEDVGPGVTK VAPGDHVVCC FIPSCGTCRY CSTGRQNLCD MGATILEGCM PDGTFRFHSG
GTDYGGFCML GTFAERATVS QHSVVKVDDW LPLQTAVLVG CGVPTGWASA NYDGGVRAGD
TVVVYGVGGV GINAVQGAAH AGAKYVVAVD PVEFKRETAL KLGATHAFAT AEEAMVTVAE
LTWGQMADQA LITVGDLDEA VTTAAFNTIG KGGTVVIAAL AKLESLDVHI SGSQLALFGK
TIKGTLFGGA NPQYDIVRLL RLYDAGKLKL DELVTRRYTL EQVNEGYQDL RDGKNIRGVI
VHR
//