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MSHD_CATAD
ID   MSHD_CATAD              Reviewed;         314 AA.
AC   C7QKH8;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-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=Caci_8254;
OS   Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS   B-24433 / ID139908).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908;
RX   PubMed=21304647; DOI=10.4056/sigs.17259;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(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; CP001700; ACU77077.1; -; Genomic_DNA.
DR   RefSeq; WP_015796802.1; NC_013131.1.
DR   AlphaFoldDB; C7QKH8; -.
DR   SMR; C7QKH8; -.
DR   STRING; 479433.Caci_8254; -.
DR   PRIDE; C7QKH8; -.
DR   EnsemblBacteria; ACU77077; ACU77077; Caci_8254.
DR   KEGG; cai:Caci_8254; -.
DR   eggNOG; COG0456; Bacteria.
DR   HOGENOM; CLU_068014_0_0_11; -.
DR   OMA; AEPWFDP; -.
DR   OrthoDB; 1526822at2; -.
DR   Proteomes; UP000000851; 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; 2.
PE   3: Inferred from homology;
KW   Acyltransferase; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..314
FT                   /note="Mycothiol acetyltransferase"
FT                   /id="PRO_0000400243"
FT   DOMAIN          18..156
FT                   /note="N-acetyltransferase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   DOMAIN          168..314
FT                   /note="N-acetyltransferase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         38
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         92..94
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         195
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         234
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         248
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         252..254
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         259..265
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         286
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   314 AA;  34116 MW;  BDEED7619459A0E0 CRC64;
     MTGISIGVVR RPNEADVATI RSLAEAAERA DGVAPLPEQV LLHLKRSGDA DADADTDAWH
     FVARRLSPQG SELTGYAFLD KSNAEEGPTA EVVVLPDARR QGVGGALLDA LRMKVRRGDK
     PIRVWSHGAL PAAAALAAKR GLEPVRELWV MSRPLADVPP APTPPDGIRI ATFRPGVDDE
     AWVEVNARAF AHHPEQGSMT VQDLRDRMAE PWFDPEGFFL AWRGAKLAGF HWTKVHDHSA
     YGDGPVGEVY VVGLDPAEQG HGLGRTLTEV GLRHLHDRGL GEVILYVEAD NTPAVAVYTK
     LGFTRRSADV MYQL
 
 
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