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Database: UniProt
Entry: A0A177YG48_9NOCA
LinkDB: A0A177YG48_9NOCA
Original site: A0A177YG48_9NOCA 
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
//
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