ID A1T2V7_MYCVP Unreviewed; 337 AA.
AC A1T2V7;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Alcohol dehydrogenase GroES domain protein {ECO:0000313|EMBL:ABM11507.1};
GN OrderedLocusNames=Mvan_0669 {ECO:0000313|EMBL:ABM11507.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM11507.1, ECO:0000313|Proteomes:UP000009159};
RN [1] {ECO:0000313|EMBL:ABM11507.1, ECO:0000313|Proteomes:UP000009159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1 {ECO:0000313|Proteomes:UP000009159};
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 Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; CP000511; ABM11507.1; -; Genomic_DNA.
DR RefSeq; WP_011777944.1; NZ_JACKSD010000046.1.
DR AlphaFoldDB; A1T2V7; -.
DR STRING; 350058.Mvan_0669; -.
DR KEGG; mva:Mvan_0669; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_1_11; -.
DR Proteomes; UP000009159; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF7; ALCOHOL DEHYDROGENASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 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|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009159};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 11..335
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 337 AA; 34971 MW; 16660180DB8AFB0C CRC64;
MPTHKAVQVP SANEALTHVE VDTLPPPAGH VRIDVAACGV CGTDREFRAG HFPGLQWPIT
LGHEIAGTVA ELGDGVEEFA VGDRVAVGWF GGNCNRCVPC RRGFFMQCER MQVPSWQYPG
GYAESVTAPA TALARIPDGL SFVEAAPMGC AGVTTFNGLR RTRAKAGDLV AVLGVGGLGH
LGVQWARAMG FETVAIGRGT GKAEEATQFG AHHYIDSTGQ DVAAELTKLG GASVVLATAN
NAAAMAAAVG GLGPAGELVV VGVTAENLPI SPLDLINAGR SVTGHPSGTS RDVEETMHFA
LLSGVRAKVE EVPLARAAEA YESMDSGRAR YRMVLTM
//
