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
//