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Database: UniProt
Entry: Q743J0_MYCPA
LinkDB: Q743J0_MYCPA
Original site: Q743J0_MYCPA 
ID   Q743J0_MYCPA            Unreviewed;       375 AA.
AC   Q743J0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   Name=adhB {ECO:0000313|EMBL:AAS02912.1};
GN   OrderedLocusNames=MAP_0595c {ECO:0000313|EMBL:AAS02912.1};
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS02912.1, ECO:0000313|Proteomes:UP000000580};
RN   [1] {ECO:0000313|EMBL:AAS02912.1, ECO:0000313|Proteomes:UP000000580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580};
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS02912.1; -; Genomic_DNA.
DR   RefSeq; WP_003875756.1; NZ_CP106873.1.
DR   AlphaFoldDB; Q743J0; -.
DR   STRING; 262316.MAP_0595c; -.
DR   GeneID; 75268542; -.
DR   KEGG; mpa:MAP_0595c; -.
DR   eggNOG; COG1062; Bacteria.
DR   HOGENOM; CLU_026673_14_0_11; -.
DR   Proteomes; UP000000580; 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:UP000000580};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          15..368
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   375 AA;  39802 MW;  65C7E43CAEEBF93E CRC64;
     MKTKGALIWE FNQPWSIEEI EIGDPQAHEV KIQMEAAGMC HSDHHLVTGG IPMAGFPVLG
     GHEGAGIVTE VGPGVEDIAP GDHVVLSFIP SCGSCPTCQA GMRNLCDLGA GLLGGEAVSD
     GTFRIQARGQ NVYPMTLLGT FSPYMVVHRS SVVKIDPSIP FEVAALVGCG VTTGYGSAVR
     TADIRPGQDV AIVGVGGVGM AALQGAVNAG ARYIFAIDPV EWKRDQALKF GATHVYPDIM
     AAMAGMAEVT YGLMAHKVVV TVGELQGADV DNYLNITQKG GTCVLTAIGS LLDTNVTLNL
     AMLTLMQKNL QGTIFGGGNP QYDIPQLLSM YKAGKLNLDD MITRQYRLEQ INDGYQDMLD
     GKNIRGVIRY TDADR
//
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