ID Q9CBN2_MYCLE Unreviewed; 361 AA.
AC Q9CBN2;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 133.
DE SubName: Full=Alcohol dehydrogenase (Zn dependent) {ECO:0000313|EMBL:CAC30737.1};
GN Name=adhE2 {ECO:0000313|EMBL:CAC30737.1};
GN OrderedLocusNames=ML1784 {ECO:0000313|EMBL:CAC30737.1};
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631 {ECO:0000313|EMBL:CAC30737.1, ECO:0000313|Proteomes:UP000000806};
RN [1] {ECO:0000313|EMBL:CAC30737.1, ECO:0000313|Proteomes:UP000000806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN {ECO:0000313|EMBL:CAC30737.1,
RC ECO:0000313|Proteomes:UP000000806};
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; AL583923; CAC30737.1; -; Genomic_DNA.
DR PIR; A87132; A87132.
DR RefSeq; NP_302213.1; NC_002677.1.
DR RefSeq; WP_010908534.1; NC_002677.1.
DR AlphaFoldDB; Q9CBN2; -.
DR SMR; Q9CBN2; -.
DR STRING; 272631.gene:17575631; -.
DR KEGG; mle:ML1784; -.
DR PATRIC; fig|272631.5.peg.3388; -.
DR Leproma; ML1784; -.
DR eggNOG; COG1062; Bacteria.
DR HOGENOM; CLU_026673_14_1_11; -.
DR OMA; CLSQKTN; -.
DR OrthoDB; 334894at2; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR017816; MycoS_dep_FDH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR03451; mycoS_dep_FDH; 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:UP000000806};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 13..359
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 361 AA; 38110 MW; 464713FFB2919F82 CRC64;
MSQTVRGVIS RKKDEPVELV DIVIPDPGPG EAVVDVTACG VCHTDLTYRE GGINDRYPFL
LGHEAAGTVE VVGPGVTAVE PGDFVILNWR AVCGQCRACK RGRPSYCFDT FNAQQKMTLI
DGTELTPALG IGAFADKTLV HSGQCTKVDP AADPAVAGLL GCGVMAGLGA AINTAAVSRD
DTVAVIGCGG VGDAAISGAA LVGANRIIAV DIDDTKLEWA RTFGATHTVN ALELEVVKTI
QDLTSGFGVD VVIDTVGRPE TWKQAFYARD LAGTVVLVGV PTPDMRLDMP LLDFFSHGGS
LKSSWYGDCL PERDFPTLVD LYLQGRLPLG KFVSERIGLG DVEEAFHKIH GGKVLRSVVM
L
//