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Database: UniProt
Entry: A0A0D5ACV0_9NOCA
LinkDB: A0A0D5ACV0_9NOCA
Original site: A0A0D5ACV0_9NOCA 
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
//
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