ID A0A3L6ZVT1_9MICO Unreviewed; 295 AA.
AC A0A3L6ZVT1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Mycothiol acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01698};
DE Short=MSH acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01698};
DE EC=2.3.1.189 {ECO:0000256|HAMAP-Rule:MF_01698};
DE AltName: Full=Mycothiol synthase {ECO:0000256|HAMAP-Rule:MF_01698};
GN Name=mshD {ECO:0000256|HAMAP-Rule:MF_01698,
GN ECO:0000313|EMBL:RLP72106.1};
GN ORFNames=D9V29_06645 {ECO:0000313|EMBL:RLP72106.1};
OS Mycetocola manganoxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Mycetocola.
OX NCBI_TaxID=699879 {ECO:0000313|EMBL:RLP72106.1, ECO:0000313|Proteomes:UP000270299};
RN [1] {ECO:0000313|EMBL:RLP72106.1, ECO:0000313|Proteomes:UP000270299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB209002 {ECO:0000313|EMBL:RLP72106.1,
RC ECO:0000313|Proteomes:UP000270299};
RA Li J.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of acetyl from acetyl-CoA to
CC desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_01698};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01698}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. MshD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01698}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01698}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLP72106.1}.
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DR EMBL; RCUV01000006; RLP72106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6ZVT1; -.
DR OrthoDB; 3208058at2; -.
DR Proteomes; UP000270299; Unassembled WGS sequence.
DR GO; GO:0035447; F:mycothiol synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010125; P:mycothiol biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR HAMAP; MF_01698; MshD; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR017813; Mycothiol_AcTrfase.
DR NCBIfam; TIGR03448; mycothiol_MshD; 1.
DR PANTHER; PTHR43420; ACETYLTRANSFERASE; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR PIRSF; PIRSF021524; MSH_acetyltransferase; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01698,
KW ECO:0000313|EMBL:RLP72106.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000270299};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01698};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01698, ECO:0000313|EMBL:RLP72106.1}.
FT DOMAIN 6..149
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 153..295
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 40
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 82..84
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="1"
FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_01698"
FT BINDING 220
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 227
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 231..233
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 263
FT /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT alpha-D-glucopyranoside"
FT /ligand_id="ChEBI:CHEBI:58887"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
SQ SEQUENCE 295 AA; 31947 MW; 3D457BA50533AD1A CRC64;
MTVRTPVLRS RNLADAAPRA AFDRLVRRAV AGDGASPFND QALIDAGDGS RSLVFAVAPP
ESPSAAELLV GAVLIGQGEL ELVVDPEWRG TGVGTAMLTG ILLDAPGDLL AWAHGDHPAS
RALATRFGFE RVRTLLQLRM PLEPGDDIPP LPDGITTFRP DIDDAEWVEL NARVFADHPE
QGRITVDDVR ARRAEPWFDA GDFLLARDDA GRMIGYNWLK IDGESGEIYV IGVGEPGRGL
GRQLMVAGLD RLRERGVTTA SLYVEGDNER AVALYRSLGF TDHTVDIQYR RGATA
//
