MSHD_MYCLB
ID MSHD_MYCLB Reviewed; 311 AA.
AC B8ZSU0;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=MLBr02193;
OS Mycobacterium leprae (strain Br4923).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=561304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Br4923;
RX PubMed=19881526; DOI=10.1038/ng.477;
RA Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA Rougemont J., Brennan P.J., Cole S.T.;
RT "Comparative genomic and phylogeographic analysis of Mycobacterium
RT leprae.";
RL Nat. Genet. 41:1282-1289(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FM211192; CAR72290.1; -; Genomic_DNA.
DR RefSeq; WP_010908756.1; NC_011896.1.
DR AlphaFoldDB; B8ZSU0; -.
DR SMR; B8ZSU0; -.
DR EnsemblBacteria; CAR72290; CAR72290; MLBr02193.
DR KEGG; mlb:MLBr02193; -.
DR HOGENOM; CLU_068014_0_0_11; -.
DR OMA; AEPWFDP; -.
DR OrthoDB; 1526822at2; -.
DR Proteomes; UP000006900; 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; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Repeat; Transferase.
FT CHAIN 1..311
FT /note="Mycothiol acetyltransferase"
FT /id="PRO_0000400273"
FT DOMAIN 155..311
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 35
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 79..81
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 180
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 225
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
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 239..241
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 246..252
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 278
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 283..288
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
SQ SEQUENCE 311 AA; 33819 MW; 8764CE7504C689A5 CRC64;
MVLNWRFALS ADEQRLVREI ISAATEFDEV SPVGEQVLRE LGYDRTEHLL VTDSRPYAPI
IGYLNLSSPR DAGVAMAELV VHPRERRRGV GAAMVRAALA KTGGRNRFWA HGTLASARAT
ASVLGLVPVR ELVQMQRSLR TIPDPMVPDQ LGVWVRTYVG TVDDAELLRV NNAAFAGHPE
QGGWTATQLA ERRSEPWFDP AGLFLAFGDS SSNQPGKLLG FHWTKVHAAH PGLGEVYVLG
VDPSAQGRGL GQMLTSIGIA SLAQRLVGPS AEPTVMLYVE SDNVAAARTY ERLGFTTYSV
DTAYALARID D
