ID A1UDI7_MYCSK Unreviewed; 343 AA.
AC A1UDI7;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE SubName: Full=Alcohol dehydrogenase, zinc-binding domain protein {ECO:0000313|EMBL:ABL90895.1};
GN OrderedLocusNames=Mkms_1692 {ECO:0000313|EMBL:ABL90895.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL90895.1};
RN [1] {ECO:0000313|EMBL:ABL90895.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL90895.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000518; ABL90895.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UDI7; -.
DR STRING; 189918.Mkms_1692; -.
DR KEGG; mkm:Mkms_1692; -.
DR HOGENOM; CLU_026673_11_0_11; -.
DR OMA; LFCGHCA; -.
DR OrthoDB; 9797931at2; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08233; butanediol_DH_like; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..339
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 343 AA; 35623 MW; 7684343819297B73 CRC64;
MRAAIYHGRE DVRIEELPDP SPRAGEVVIE VARAGICGTD LHEYIAGPMH AAPGVVIGHE
YSGTVVGVGS GVREFTEGDR VCGVGVFGCG ECGFCKQGAE ALCGAVGFIG FAVNGALARY
ASLPTKALFR IPDEISLAEA AVVEPIASAY HAVRRSGLAA GGTVFIAGAG PIGLALVQFS
LAQGATQVIV SEVSATRRVA AHRVGATRVI DPLAEDAVEV VRTLTNGNGV DISFDAAGVQ
PALDAALGVL RPRGRLMVVA IWEAPAGIDI NRSVMREANI GFSFCYEAQR QVPAILDLLA
TGAINLGELI TDEIPLDAVV SQGLEELRVN RDAHVKILID PSA
//