MSHD_MYCTO
ID MSHD_MYCTO Reviewed; 315 AA.
AC P9WJM6; L0T7T7; O53831; Q7D982;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Mycothiol acetyltransferase;
DE Short=MSH acetyltransferase;
DE EC=2.3.1.189;
DE AltName: Full=Mycothiol synthase;
GN Name=mshD; OrderedLocusNames=MT0841;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the transfer of acetyl from acetyl-CoA to
CC desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol. {ECO:0000250}.
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}.
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DR EMBL; AE000516; AAK45083.1; -; Genomic_DNA.
DR PIR; C70810; C70810.
DR RefSeq; WP_003404307.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WJM6; -.
DR SMR; P9WJM6; -.
DR EnsemblBacteria; AAK45083; AAK45083; MT0841.
DR KEGG; mtc:MT0841; -.
DR PATRIC; fig|83331.31.peg.900; -.
DR HOGENOM; CLU_068014_0_0_11; -.
DR Proteomes; UP000001020; 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_0000427803"
FT DOMAIN 4..141
FT /note="N-acetyltransferase 1"
FT DOMAIN 152..315
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 80..82
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88..93
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
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:0000250"
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:0000250"
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:0000250"
FT BINDING 238..240
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 245..251
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
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:0000250"
FT BINDING 287..292
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
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
