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MSHD_MYCBP
ID   MSHD_MYCBP              Reviewed;         315 AA.
AC   A1KGV2;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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}; OrderedLocusNames=BCG_0871;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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; AM408590; CAL70857.1; -; Genomic_DNA.
DR   RefSeq; WP_003404307.1; NC_008769.1.
DR   AlphaFoldDB; A1KGV2; -.
DR   SMR; A1KGV2; -.
DR   KEGG; mbb:BCG_0871; -.
DR   HOGENOM; CLU_068014_0_0_11; -.
DR   OMA; AEPWFDP; -.
DR   Proteomes; UP000001472; 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; Repeat; Transferase.
FT   CHAIN           1..315
FT                   /note="Mycothiol acetyltransferase"
FT                   /id="PRO_0000400269"
FT   DOMAIN          4..141
FT                   /note="N-acetyltransferase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   DOMAIN          152..315
FT                   /note="N-acetyltransferase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         36
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         80..82
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         88..93
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         179
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         224
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         234
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         238..240
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         245..251
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         282
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         287..292
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
SQ   SEQUENCE   315 AA;  33599 MW;  E1728C0652CF2716 CRC64;
     MTALDWRSAL TADEQRSVRA LVTATTAVDG VAPVGEQVLR ELGQQRTEHL LVAGSRPGGP
     IIGYLNLSPP RGAGGAMAEL VVHPQSRRRG IGTAMARAAL AKTAGRNQFW AHGTLDPARA
     TASALGLVGV RELIQMRRPL RDIPEPTIPD GVVIRTYAGT SDDAELLRVN NAAFAGHPEQ
     GGWTAVQLAE RRGEAWFDPD GLILAFGDSP RERPGRLLGF HWTKVHPDHP GLGEVYVLGV
     DPAAQRRGLG QMLTSIGIVS LARRLGGRKT LDPAVEPAVL LYVESDNVAA VRTYQSLGFT
     TYSVDTAYAL AGTDN
 
 
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