MSHD_MYCS2
ID MSHD_MYCS2 Reviewed; 295 AA.
AC A4ZHT6; I7FL88;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Mycothiol acetyltransferase;
DE Short=MSH acetyltransferase;
DE EC=2.3.1.189;
DE AltName: Full=Mycothiol synthase;
GN Name=mshD; OrderedLocusNames=MSMEG_5783, MSMEI_5630; ORFNames=MSMEG5754;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION.
RX PubMed=12375100; DOI=10.1007/s00203-002-0462-y;
RA Koledin T., Newton G.L., Fahey R.C.;
RT "Identification of the mycothiol synthase gene (mshD) encoding the
RT acetyltransferase producing mycothiol in actinomycetes.";
RL Arch. Microbiol. 178:331-337(2002).
CC -!- FUNCTION: Catalyzes the transfer of acetyl from acetyl-CoA to
CC desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
CC {ECO:0000305|PubMed:12375100}.
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;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. MshD subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CP000480; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ866865; ABJ96326.1; -; Genomic_DNA.
DR EMBL; CP000480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP001663; AFP42065.1; -; Genomic_DNA.
DR RefSeq; WP_014878453.1; NZ_SIJM01000007.1.
DR AlphaFoldDB; A4ZHT6; -.
DR SMR; A4ZHT6; -.
DR STRING; 246196.MSMEI_5630; -.
DR EnsemblBacteria; AFP42065; AFP42065; MSMEI_5630.
DR GeneID; 66737074; -.
DR KEGG; msg:MSMEI_5630; -.
DR PATRIC; fig|246196.56.peg.5750; -.
DR eggNOG; COG0456; Bacteria.
DR OrthoDB; 1526822at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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..295
FT /note="Mycothiol acetyltransferase"
FT /id="PRO_0000399829"
FT DOMAIN 4..138
FT /note="N-acetyltransferase 1"
FT DOMAIN 149..295
FT /note="N-acetyltransferase 2"
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:0000250"
FT BINDING 77..79
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85..90
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000250"
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:0000250"
FT BINDING 225
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000250"
FT BINDING 229..231
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 236..242
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000250"
FT BINDING 271..276
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 295 AA; 31897 MW; 080B30FC97044B91 CRC64;
MTSTEWRTGL TGAQQAEIRA LIDAATTHDG VAPVGDQVLR ELGRDRTRHL LTTDDDRVVG
YLNLAPAEGD DPAMAELVVH PQARRRGIGA AMARTALAEG GPGARIWAHG NIAAAQAMAS
SLRLVVVREL LQMRRPLTDL PPVPDTPGVR IATYAGPGDD AEILRVNNAA FSWHPEQGGW
TEHEIDERRN EGWFDPEGLF QAFDEQTGSL LGFHWTKIHD ASLGEVYVVG VDPQAQGRGL
GYTLTLIGLH HLAEKLAGPE PTVLLYVEAD NSAAVNTYRK LGFEVFSVDA AYAAN
