ID F5YWD2_MYCSD Unreviewed; 341 AA.
AC F5YWD2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:AEF34033.1};
GN OrderedLocusNames=JDM601_0033 {ECO:0000313|EMBL:AEF34033.1};
OS Mycolicibacter sinensis (strain JDM601) (Mycobacterium sinense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF34033.1, ECO:0000313|Proteomes:UP000009224};
RN [1] {ECO:0000313|EMBL:AEF34033.1, ECO:0000313|Proteomes:UP000009224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDM601 {ECO:0000313|EMBL:AEF34033.1,
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|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; CP002329; AEF34033.1; -; Genomic_DNA.
DR RefSeq; WP_013826977.1; NC_015576.1.
DR AlphaFoldDB; F5YWD2; -.
DR STRING; 875328.JDM601_0033; -.
DR KEGG; mjd:JDM601_0033; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_11; -.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000009224; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:UP000009224};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 7..339
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 34170 MW; 4A1DB04DC8AFB700 CRC64;
MRSVVIDAPG SVRVDTRPDP GLPGPDGAVV AVSATAICGS DLHFYEGDYP IVDPVPLGHE
AIGTVVEAGP EVTSVKAGDR VMVSSVAGCG RCAGCATRDP IRCHAGPLIF GSGALGGAQS
ELLAVPGADF QLAPIPDGLC DEEALLLTDN LATGWAAALR ADIPVGGTVA VIGLGAVGLC
AAQSALFLGA ATVLGIDPVP QRRDRAAAMG ATPAPPSATV AAMEHTGGRG VDAVIDAVGS
DTTMADALTA VRAGGTVSVV GVHDLQPFPF PALAALVRSI TLRMTTAPVQ QTWPQLVPLL
QSGRLSVAGI FTTEMPLDAA ADAYRAVAAR SGDVVKVLLT P
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