ID A0A344U7U4_9ACTN Unreviewed; 310 AA.
AC A0A344U7U4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Mycothiol acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01698};
DE Short=MSH acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01698};
DE EC=2.3.1.189 {ECO:0000256|HAMAP-Rule:MF_01698};
DE AltName: Full=Mycothiol synthase {ECO:0000256|HAMAP-Rule:MF_01698};
GN Name=mshD {ECO:0000256|HAMAP-Rule:MF_01698,
GN ECO:0000313|EMBL:AXE26965.1};
GN ORFNames=C0216_29225 {ECO:0000313|EMBL:AXE26965.1};
OS Streptomyces globosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68209 {ECO:0000313|EMBL:AXE26965.1, ECO:0000313|Proteomes:UP000252004};
RN [1] {ECO:0000313|EMBL:AXE26965.1, ECO:0000313|Proteomes:UP000252004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LZH-48 {ECO:0000313|EMBL:AXE26965.1,
RC ECO:0000313|Proteomes:UP000252004};
RA Ran K., Li Z., Wei S., Dong R.;
RT "Draft genome Sequence of streptomyces globosus LZH-48.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of acetyl from acetyl-CoA to
CC desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
CC {ECO:0000256|HAMAP-Rule:MF_01698}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-
CC glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol;
CC Xref=Rhea:RHEA:26172, ChEBI:CHEBI:15378, ChEBI:CHEBI:16768,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58887;
CC EC=2.3.1.189; Evidence={ECO:0000256|HAMAP-Rule:MF_01698};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01698}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. MshD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01698}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01698}.
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DR EMBL; CP030862; AXE26965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A344U7U4; -.
DR KEGG; sgz:C0216_29225; -.
DR OrthoDB; 3208058at2; -.
DR Proteomes; UP000252004; Chromosome.
DR GO; GO:0035447; F:mycothiol synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010125; P:mycothiol biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04301; NAT_SF; 2.
DR Gene3D; 3.40.630.30; -; 1.
DR HAMAP; MF_01698; MshD; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR017813; Mycothiol_AcTrfase.
DR NCBIfam; TIGR03448; mycothiol_MshD; 1.
DR PANTHER; PTHR43617; L-AMINO ACID N-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43617:SF31; MYCOTHIOL ACETYLTRANSFERASE; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF13508; Acetyltransf_7; 1.
DR PIRSF; PIRSF021524; MSH_acetyltransferase; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01698}; Reference proteome {ECO:0000313|Proteomes:UP000252004};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01698};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01698, ECO:0000313|EMBL:AXE26965.1}.
FT DOMAIN 16..152
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 167..310
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 47
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 91..93
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 194
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 233
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 242
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 246..248
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 253..259
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 280
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
SQ SEQUENCE 310 AA; 32705 MW; BF8DCB2A861CF2D3 CRC64;
MTDDAAAALE PGRRIETLDE LTAEQADAVV GLIEDAALTD GTTAVSEQGR LQLRGGPREG
VRHFLLTEKG RLAGYGQLED TDPVEAPAAE LVVHPALRGR GHGRALGQAL LAASGKRIRV
WAHGGKSAAR HLAQVLGLTL FRELRQLRRP LGAGAPPLPD PVLPPGVAVR TFVPGKDDAA
WLAANAAAFA HHPEQGSLTQ RDLDDRIAQP WFDPKGFFLA EREGEIVGFH WTKVHAAEGL
GEVYVVGVLP GAQGGGLGKA LTAVGLHHLA AAGLPTAMLY VDADNPAALA VYEGLGFSTH
EVDLMYRTES
//
