MSHD_ROTMD
ID MSHD_ROTMD Reviewed; 354 AA.
AC D2NRH2;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Mycothiol acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01698};
DE Short=MSH acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01698};
DE EC=2.3.1.189 {ECO:0000255|HAMAP-Rule:MF_01698};
DE AltName: Full=Mycothiol synthase {ECO:0000255|HAMAP-Rule:MF_01698};
GN Name=mshD {ECO:0000255|HAMAP-Rule:MF_01698};
GN OrderedLocusNames=RMDY18_04160;
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Rothia.
OX NCBI_TaxID=680646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18;
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) 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:0000255|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:0000255|HAMAP-Rule:MF_01698};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01698}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. MshD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01698}.
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DR EMBL; AP011540; BAI64248.1; -; Genomic_DNA.
DR RefSeq; WP_012903004.1; NC_013715.1.
DR AlphaFoldDB; D2NRH2; -.
DR SMR; D2NRH2; -.
DR STRING; 680646.RMDY18_04160; -.
DR EnsemblBacteria; BAI64248; BAI64248; RMDY18_04160.
DR KEGG; rmu:RMDY18_04160; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_068014_0_0_11; -.
DR OMA; AEPWFDP; -.
DR OrthoDB; 1526822at2; -.
DR Proteomes; UP000001883; Chromosome.
DR GO; GO:0035447; F:mycothiol synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0010125; P:mycothiol biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01698; MshD; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR017813; Mycothiol_AcTrfase.
DR Pfam; PF00583; Acetyltransf_1; 2.
DR PIRSF; PIRSF021524; MSH_acetyltransferase; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR03448; mycothiol_MshD; 1.
DR PROSITE; PS51186; GNAT; 2.
PE 3: Inferred from homology;
KW Acyltransferase; Reference proteome; Repeat; Transferase.
FT CHAIN 1..354
FT /note="Mycothiol acetyltransferase"
FT /id="PRO_0000400293"
FT DOMAIN 21..176
FT /note="N-acetyltransferase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT DOMAIN 191..354
FT /note="N-acetyltransferase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 101..103
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 217
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 259
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 274
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 278..280
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 285..291
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 318
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
SQ SEQUENCE 354 AA; 38639 MW; DF9ACCCFE44AC1F0 CRC64;
MMVDNQTPDS STLSTASTPV YAEPQLTEEL LERFDSFAQK VARHDGVSAF SEQTRIELSK
ALRESTLTPP RFFVAEDNGT LAAVFVALTP ANDEDTGVIE AAVAPEYRGQ GVGSAFFDHA
VRQLGDDATR YRLWVHGSAT DTGIESPAHA FATLHGFEPV RVLYKMVLPL DAQTREELVE
RSDARTLPEN LRMRTFTGAD EFPWLRVNAA AFAHHPEQGK LTLADLRERT GSPWFRPEGF
FIASEVEDDS AIAAFTWTKI PTGQEQSELS PSGEIYVVGV NPQAQGGGLG RTLTLRALAY
LACAEDENGE PLRAIDLYVD ADNTAAYSLY TSLGFGVATV DRMYAPAQQD EPAA
