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MSHD_ACTMD
ID   MSHD_ACTMD              Reviewed;         297 AA.
AC   C6WPR7;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=Amir_6822;
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS   / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 / NRRL
RC   B-12336 / IMRU 3971 / 101;
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA   Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA   Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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; CP001630; ACU40618.1; -; Genomic_DNA.
DR   RefSeq; WP_015805495.1; NC_013093.1.
DR   AlphaFoldDB; C6WPR7; -.
DR   SMR; C6WPR7; -.
DR   STRING; 446462.Amir_6822; -.
DR   EnsemblBacteria; ACU40618; ACU40618; Amir_6822.
DR   KEGG; ami:Amir_6822; -.
DR   eggNOG; COG0456; Bacteria.
DR   HOGENOM; CLU_068014_0_0_11; -.
DR   OMA; AEPWFDP; -.
DR   OrthoDB; 1526822at2; -.
DR   Proteomes; UP000002213; 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..297
FT                   /note="Mycothiol acetyltransferase"
FT                   /id="PRO_0000400236"
FT   DOMAIN          8..153
FT                   /note="N-acetyltransferase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   DOMAIN          156..297
FT                   /note="N-acetyltransferase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
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:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         80..82
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         183
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         223
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
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..237
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         242..248
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         269
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         274..279
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
SQ   SEQUENCE   297 AA;  31910 MW;  5BA3D1419C6F2DF5 CRC64;
     MADLTWHDAL DPEQAEEITR LLAEAEEVDG VAPVGEAVHL RLRPGASGSA HLLARADGVL
     AGYAHLDLLG DSDGNLVAEL AVRPGSRRAG VGSELAGALL GAAADRGKPV RFWAHGDREG
     ASGLAARLGA RRVRELWVMR RELAGLPEVP PLPEGVALRS FEPGRDEDAV VRVNARAFSW
     HPEQGAMTAD DVRLKEAEDW FDADGFLLAV DGADRLLGFH WTKRHDESMG EVYVVGVDPD
     AQGGGLGKAL TLAGLVHLKS TGLRDVHLYV ESDNSPAVRV YTRLGFSRWK ADVQYAL
 
 
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