ID A0A0Q2RXH3_MYCGO Unreviewed; 361 AA.
AC A0A0Q2RXH3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=S-(Hydroxymethyl)mycothiol dehydrogenase {ECO:0000313|EMBL:KQH79899.1};
GN ORFNames=AO501_22275 {ECO:0000313|EMBL:KQH79899.1};
OS Mycobacterium gordonae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH79899.1, ECO:0000313|Proteomes:UP000051677};
RN [1] {ECO:0000313|EMBL:KQH79899.1, ECO:0000313|Proteomes:UP000051677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH79899.1,
RC ECO:0000313|Proteomes:UP000051677};
RA Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA Chernousova L.;
RT "Mycobacterium gordonae draft genome assembly.";
RL Submitted (OCT-2015) 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}.
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:KQH79899.1}.
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DR EMBL; LKTM01000057; KQH79899.1; -; Genomic_DNA.
DR RefSeq; WP_055577183.1; NZ_LKTM01000057.1.
DR AlphaFoldDB; A0A0Q2RXH3; -.
DR STRING; 1778.A9W97_16600; -.
DR OrthoDB; 334894at2; -.
DR Proteomes; UP000051677; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR017816; MycoS_dep_FDH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR03451; mycoS_dep_FDH; 1.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF19; RIBULOSE-5-PHOSPHATE REDUCTASE; 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:UP000051677};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..359
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 361 AA; 38164 MW; CA51BA26D130F99F CRC64;
MSQTVRGVIS RSKGQPVELV DIVIPDPGPG EAVVDITACG VCHTDLTYRE GGINDEYPFL
LGHEAAGTVE AVGPGVTHVE PGDFVILNWR AVCGQCRACR RGRPHLCFDT FNAEQKMTLT
DGTELTPALG IGAFADKTLV AAGQCTKVNP EADPAVAGLL GCGVMAGLGA AINTGGVTRD
DTVAVIGCGG VGDAAIAGAA LVGAKKIIAV DTDNAKLEWA RKFGATHTVN AREFDVVETI
QDLTDGFGVD VVVDAVGRPE TWKQAFYARD LAGTVVLVGV PTPDMRLDMP LVDFFSRGGS
LKSSWYGDCL PERDFPTLVD LYLQGRLPLE KFVSERIGLD GIEEAFHKMH DGKVLRSVVI
L
//
