ID A0A177YG48_9NOCA Unreviewed; 305 AA.
AC A0A177YG48;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ORFNames=A3K89_03990 {ECO:0000313|EMBL:OAK54526.1};
OS Rhodococcus kyotonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=398843 {ECO:0000313|EMBL:OAK54526.1, ECO:0000313|Proteomes:UP000077519};
RN [1] {ECO:0000313|EMBL:OAK54526.1, ECO:0000313|Proteomes:UP000077519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KB10 {ECO:0000313|EMBL:OAK54526.1,
RC ECO:0000313|Proteomes:UP000077519};
RA Jeong H., Hong C.E., Jo S.H., Park J.M.;
RT "Genome sequence of Rhodococcus kyotonensis KB10.";
RL Submitted (MAR-2016) 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:OAK54526.1}.
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DR EMBL; LVHI01000012; OAK54526.1; -; Genomic_DNA.
DR RefSeq; WP_068424868.1; NZ_LVHI01000012.1.
DR AlphaFoldDB; A0A177YG48; -.
DR Proteomes; UP000077519; 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; 2.
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; PTHR43617; L-AMINO ACID N-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43617:SF31; MYCOTHIOL ACETYLTRANSFERASE; 1.
DR Pfam; PF00583; Acetyltransf_1; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000077519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01698};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01698}.
FT DOMAIN 10..149
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 157..305
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 41
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 83..85
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 184
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 225
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 238
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 242..244
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 249..255
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 276
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 281..286
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
SQ SEQUENCE 305 AA; 32805 MW; 17D3ACE3A52BE078 CRC64;
MTVSFDIAKA EFASITEAMA EDILAIVSRA TVADGTAPIS EQAVKAVTAD GDSVHLVATD
GATVVGYAGV VPSNENAPAM AEVVVDPTFR GRGIGRMLVE RALTEGGDDA RVWAHGNLAP
ARAVASHLGL EVARELLQMR RPLAAPELPD VVVPEGVSLR TYRGHQDDAE LLRVNNAAFS
WHPEQGGWTD KDIAERRDES WFDPAGVFLA FEEGTDTLLG FHWTKVHPAE GDEAEIGEVY
VVGIDPAAQG RGLGRVLTLA GLHYLENRQL EDVLLYVEAD NAAAVHTYER LGFDRFHVDA
AYARG
//