ID A0A1H5N276_9ACTN Unreviewed; 309 AA.
AC A0A1H5N276;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=SAMN05216533_4583 {ECO:0000313|EMBL:SEE94758.1};
OS Streptomyces sp. Ag109_O5-10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855349 {ECO:0000313|EMBL:SEE94758.1, ECO:0000313|Proteomes:UP000198812};
RN [1] {ECO:0000313|EMBL:SEE94758.1, ECO:0000313|Proteomes:UP000198812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag109_O5-10 {ECO:0000313|EMBL:SEE94758.1,
RC ECO:0000313|Proteomes:UP000198812};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNTQ01000001; SEE94758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5N276; -.
DR STRING; 1855349.SAMN05216533_4583; -.
DR OrthoDB; 3208058at2; -.
DR Proteomes; UP000198812; Unassembled WGS sequence.
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; 2.
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:UP000198812};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01698};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01698}.
FT DOMAIN 17..153
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 166..309
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48
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 92..94
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 193
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 232
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 241
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 245..247
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 252..258
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 279
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 309 AA; 33181 MW; 40837A3853CF96BF CRC64;
MTSDDTARPP TYSRSIDTYS ALAPDQAEAV RELLTAAAQA DGQQPVSEQG RLQLSGGARE
GVSHLLLSVG DELVGYAQLE DTDPVEAPAA ELVVHPAHRG HGHGRALGSA LLTASGKRLR
VWAHGGHSAA RHLAQVLGLT LFRELRQMRR SLTDLDLPDP KLPEGVTVRA FVPGRDDAAW
LAVNAAAFAH HPEQGSLTQR DLDDRKAQPW FDPAGFFLAE RGGELLGFHW TKVHDAEGLG
EVYVLGVSPT AQGGGLGKSL TTIGLRHLAE RGLPTAMLYV DADNTAAVAV YERLGFVTHE
TDLMYRTET
//
