ID I0RQP0_MYCXE Unreviewed; 385 AA.
AC I0RQP0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=MXEN_10531 {ECO:0000313|EMBL:EID13443.1};
OS Mycobacterium xenopi RIVM700367.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID13443.1, ECO:0000313|Proteomes:UP000003584};
RN [1] {ECO:0000313|EMBL:EID13443.1, ECO:0000313|Proteomes:UP000003584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIVM700367 {ECO:0000313|EMBL:EID13443.1,
RC ECO:0000313|Proteomes:UP000003584};
RX PubMed=22628510; DOI=10.1128/JB.00482-12;
RA Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S.,
RA van Soolingen D., Bitter W., Pain A.;
RT "Complete Genome Sequence of Mycobacterium xenopi Type Strain RIVM700367.";
RL J. Bacteriol. 194:3282-3283(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EID13443.1}.
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DR EMBL; AJFI01000060; EID13443.1; -; Genomic_DNA.
DR RefSeq; WP_003920941.1; NZ_AJFI01000060.1.
DR AlphaFoldDB; I0RQP0; -.
DR PATRIC; fig|1150591.3.peg.2113; -.
DR OrthoDB; 334894at2; -.
DR Proteomes; UP000003584; Unassembled WGS sequence.
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:UP000003584};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 13..380
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 385 AA; 40224 MW; 0E40896E38C20379 CRC64;
MKSRAAILHD VGGPWSVEEF QLDPPRAGEV LVEMAAAGLC HSDDHILKGD LSAPNEVLRS
LGLPTMFPTI GGHEGSGIVR EVGDGVTDFM PGDHVVMSFV AVCGQCRWCA SGMEYICDAG
IGTLTPGMPT DGTFRHHTTD GKPLGHLSKI GAFAEHTVVS ANSLVKIEPD LPLLPSALLS
CAIPTGYGSA ANRAGVRGGD TVVVVGAGGI GTGAIQGARI NGAAQIVAVD PVEFKQKSAC
QFGATHAVAT TADALDLVRG LTYGVMADAV VVSPSLITPN DVRDALELTR KGGTCVLTGM
TSQLTRSVNL NLQDFILMNK TLAGTVFGSC NPKADIARLA KLYQTGQLQL DEMITKRYRL
DDINDAYADL LNGEIIRGVI DFGIG
//