ID A0A0D5ACV0_9NOCA Unreviewed; 301 AA.
AC A0A0D5ACV0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=NY08_2607 {ECO:0000313|EMBL:AJW40623.1};
OS Rhodococcus sp. B7740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW40623.1, ECO:0000313|Proteomes:UP000032410};
RN [1] {ECO:0000313|EMBL:AJW40623.1, ECO:0000313|Proteomes:UP000032410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7740 {ECO:0000313|EMBL:AJW40623.1};
RX PubMed=25931596;
RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT Bacterium Isolated from the Arctic Sea.";
RL Genome Announc. 3:0-0(2015).
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}.
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DR EMBL; CP010797; AJW40623.1; -; Genomic_DNA.
DR RefSeq; WP_045196639.1; NZ_CP010797.1.
DR AlphaFoldDB; A0A0D5ACV0; -.
DR STRING; 1564114.NY08_2607; -.
DR KEGG; rhb:NY08_2607; -.
DR PATRIC; fig|1564114.4.peg.2565; -.
DR HOGENOM; CLU_068014_0_0_11; -.
DR Proteomes; UP000032410; Chromosome.
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); 2.
DR PROSITE; PS51186; GNAT; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01698};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01698};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01698, ECO:0000313|EMBL:AJW40623.1}.
FT DOMAIN 17..155
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 152..301
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 43
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 79..81
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 179
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 233
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 237..239
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 244..250
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT BINDING 271
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 276..281
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
SQ SEQUENCE 301 AA; 32754 MW; 3366D59F2C35C3BD CRC64;
MSSDPAFDVH SIDGGAPSSR VSYEIHRILS RATEADGTAP LSEQAVKTVD DGDEVVRFVA
TEGDRVVGYV GIADGMAEAV VDPSFRGHGV GRELVSRALD VGSDTRIWAH GNLPAARSVA
AALGLQVVRE LLQMRRSSGH PDLPDVVVPE GISLRTYRGH QDDAELLRVN NAAFSWHPEQ
GGWTDRDIDA RREESWFDPA GLFLAFEEGS DRLLGFHWTK VHRAEGAEPA IGEVYVVGID
PQSQGRGLGR VLTLAGLHYL RSRELGQIML YVEADNTAAV HTYTKLGFEN YHVDAAYARS
A
//