MSHD_KOCRD
ID MSHD_KOCRD Reviewed; 303 AA.
AC B2GI63;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=KRH_05710;
OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX NCBI_TaxID=378753;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201;
RX PubMed=18408034; DOI=10.1128/jb.01853-07;
RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL J. Bacteriol. 190:4139-4146(2008).
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; AP009152; BAG28918.1; -; Genomic_DNA.
DR RefSeq; WP_012397644.1; NC_010617.1.
DR AlphaFoldDB; B2GI63; -.
DR SMR; B2GI63; -.
DR STRING; 378753.KRH_05710; -.
DR EnsemblBacteria; BAG28918; BAG28918; KRH_05710.
DR KEGG; krh:KRH_05710; -.
DR eggNOG; COG0456; Bacteria.
DR eggNOG; COG1670; Bacteria.
DR HOGENOM; CLU_068014_0_0_11; -.
DR OMA; AEPWFDP; -.
DR OrthoDB; 1526822at2; -.
DR Proteomes; UP000008838; 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..303
FT /note="Mycothiol acetyltransferase"
FT /id="PRO_0000400262"
FT DOMAIN 3..152
FT /note="N-acetyltransferase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT DOMAIN 155..303
FT /note="N-acetyltransferase 2"
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 182
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 224
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 237
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 241..243
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT BINDING 248..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 275
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 303 AA; 32580 MW; 6661CA634921008B CRC64;
MSVTVTPYDS IPFPDELVAL AERSRAADGE PPFSDQTLVD IRSGRAGATC VAATDGDELV
GAAVVVPQQD AASTFTVELT VAPGHRDQGV ATAIAGQLRA MVDGTVEAWA HGDQPASRRL
AELYGLTAVR DLLQLKRTVS GAQDIPLEVS LPQGVRIRPF EVGRDEQAWL HVNSRAFAQH
PEQGRITLGD LQEREGQSWF DPRGFLLAVS EQDPDRVLGF HWTKVHPGSG DSPALGEVYA
VGVDPEQQGS GLGRALTAAG INHLAQEGLC EVMLYVDADN SAAMALYESL GFERWHVDVM
YRS
