MSHD_NOCSJ
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 03-AUG-2022, entry version 73.
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; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC 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 = 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; 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 EnsemblBacteria; ABL83745; ABL83745; Noca_4248.
DR KEGG; nca:Noca_4248; -.
DR eggNOG; COG0454; Bacteria.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_068014_0_0_11; -.
DR OMA; AEPWFDP; -.
DR OrthoDB; 1526822at2; -.
DR Proteomes; UP000000640; 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; 1.
DR PIRSF; PIRSF021524; MSH_acetyltransferase; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR03448; mycothiol_MshD; 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
