ID MSHD_NOCSJ Reviewed; 295 AA. AC A1SPL0; DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-NOV-2024, entry version 84. 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=Noca_4248; OS Nocardioides sp. (strain ATCC BAA-499 / JS614). OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales; OC Nocardioidaceae; Nocardioides. OX NCBI_TaxID=196162; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-499 / JS614; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J., RA Richardson P.; RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614."; RL Submitted (DEC-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 = mycothiol + CoA + H(+); 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}. 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; CP000509; ABL83745.1; -; Genomic_DNA. DR RefSeq; WP_011757674.1; NC_008699.1. DR AlphaFoldDB; A1SPL0; -. DR SMR; A1SPL0; -. DR STRING; 196162.Noca_4248; -. DR KEGG; nca:Noca_4248; -. DR eggNOG; COG0454; Bacteria. DR eggNOG; COG0456; Bacteria. DR HOGENOM; CLU_068014_0_0_11; -. DR OrthoDB; 3208058at2; -. DR Proteomes; UP000000640; Chromosome. DR GO; GO:0035447; F:mycothiol synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008999; F:peptide-alanine-alpha-N-acetyltransferase activity; IEA:TreeGrafter. DR GO; GO:0010125; P:mycothiol biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0017189; P:N-terminal peptidyl-alanine acetylation; IEA:TreeGrafter. 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; IPR050276; MshD_Acetyltransferase. 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 PIRSF; PIRSF021524; MSH_acetyltransferase; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR PROSITE; PS51186; GNAT; 1. PE 3: Inferred from homology; KW Acyltransferase; Reference proteome; Repeat; Transferase. FT CHAIN 1..295 FT /note="Mycothiol acetyltransferase" FT /id="PRO_0000400286" FT DOMAIN 137..295 FT /note="N-acetyltransferase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698" FT BINDING 30 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 62..64 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698" FT BINDING 165 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 209 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 227 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 231..233 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698" FT BINDING 238..244 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698" FT BINDING 265 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 295 AA; 30832 MW; 66A164AED8AB7224 CRC64; MDDHAADLLA AVAEVARAAE AADGAAPLDE ATWLALRHHP ERVRSWVRAG GFALVIGADL SLVVHPQARG RGLGAGLLSS ALAGLSAGMP LEAWSHGDHP AAAALARSHG FERARELWVM RRQMASALPQ LRAPDGVTVR AFRADSGDAE EVLRVNAAAF AHHPEQGSMD ATNLAERMAE PWFDPDGLLL ATSAAADGGE QVLGFHWTKV HPGDAGAGAG PGVEVGEVYV VGIDPAAQGR GLGKVLTLAG LHHLAGRGVP EVLLYVESDN RPAIAVYAGL GFTHADDDTH VQYRR //