MSHD_AMYMD
ID MSHD_AMYMD Reviewed; 301 AA.
AC Q5EDG0;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 59.
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}; Synonyms=LH3;
OS Amycolatopsis mediterranei (Nocardia mediterranei).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=33910;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17151777; DOI=10.1111/j.1745-7270.2006.00238.x;
RA Yu H., Peng W.T., Liu Y., Wu T., Yao Y.F., Cui M.X., Jiang W.H., Zhao G.P.;
RT "Identification and characterization of glnA promoter and its corresponding
RT trans-regulatory protein GlnR in the rifamycin SV producing actinomycete,
RT Amycolatopsis mediterranei U32.";
RL Acta Biochim. Biophys. Sin. 38:831-843(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yu H., Jiang W., Zhao G.;
RT "Cloning and preliminary characterization of the glnR operon in
RT Amycolatopsis mediterranei U32.";
RL Submitted (MAR-2006) 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; DQ432066; AAW82910.1; -; Genomic_DNA.
DR RefSeq; WP_013230716.1; NZ_JPRA01000085.1.
DR AlphaFoldDB; Q5EDG0; -.
DR SMR; Q5EDG0; -.
DR PATRIC; fig|33910.4.peg.920; -.
DR OMA; AEPWFDP; -.
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..301
FT /note="Mycothiol acetyltransferase"
FT /id="PRO_0000400237"
FT DOMAIN 6..151
FT /note="N-acetyltransferase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT DOMAIN 153..301
FT /note="N-acetyltransferase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 79..81
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 180
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 219
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 235
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 239..241
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 246..252
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 273
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 301 AA; 33223 MW; 96FA2E4F131D0430 CRC64;
MSGDGEWRQE LDEQQLEDVR RLLLAVREAD GRPEVEPAGA LPGEFDGGEH LVACVEGEVV
GYAHLNTTGN SFGHQVAELF VHPAHRNRGY GAKLLQALDE RAAVGFRVWA HGDHPAARKL
ALKTGLERKR ELLILHVDVE GADWPEPILR DGVSLRTFVP GQDEDAVVRV NARAFDWHPE
QGALTVEDVR ADERRAWFDE DGFFLAEERG EVIGFHWTKV HEPTPGRFGG ERVGEVYVVG
VDPAAQGGGL GRALTLAGLR YLASRGLRQI ILYVEGDNAA ALAVYTKLGF TRHETDVQYG
R
