GenomeNet

Database: UniProt
Entry: A0A0Q8P231_9ACTN
LinkDB: A0A0Q8P231_9ACTN
Original site: A0A0Q8P231_9ACTN 
ID   A0A0Q8P231_9ACTN        Unreviewed;       307 AA.
AC   A0A0Q8P231;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=ASE03_01335 {ECO:0000313|EMBL:KRB67619.1};
OS   Kitasatospora sp. Root187.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB67619.1, ECO:0000313|Proteomes:UP000051829};
RN   [1] {ECO:0000313|EMBL:KRB67619.1, ECO:0000313|Proteomes:UP000051829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root187 {ECO:0000313|EMBL:KRB67619.1,
RC   ECO:0000313|Proteomes:UP000051829};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB67619.1, ECO:0000313|Proteomes:UP000051829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root187 {ECO:0000313|EMBL:KRB67619.1,
RC   ECO:0000313|Proteomes:UP000051829};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRB67619.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMHX01000023; KRB67619.1; -; Genomic_DNA.
DR   RefSeq; WP_057228094.1; NZ_LMHX01000023.1.
DR   AlphaFoldDB; A0A0Q8P231; -.
DR   STRING; 1736486.ASE03_01335; -.
DR   Proteomes; UP000051829; 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; 1.
DR   Pfam; PF13508; Acetyltransf_7; 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   Reference proteome {ECO:0000313|Proteomes:UP000051829};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01698};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01698}.
FT   DOMAIN          12..157
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          160..307
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         86..88
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT   BINDING         187
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         226
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         234
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..240
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT   BINDING         245..251
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
FT   BINDING         273
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         278..283
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01698"
SQ   SEQUENCE   307 AA;  33178 MW;  811803D53F838C82 CRC64;
     METTNPSQDG IRSTETLGAD DLAAARAVLA AASAVDGREA VSEAGRLRLR VDSARPGVTH
     LVQRQEGVPA GYAQLEAGEG RTTVELTVHP DHRRLGLGRQ LLDATLAEAD AGTVDFWAHG
     GHPGAARLAA EYGAELVREL RQMRRPAEPV PAEPVLPEGV TVRSFRPGQD DAAWLRLNAL
     AFAHHPEQGG WTEQDLAERL AEPWFDPAGL FLAFRGADLV GFHWTKVHPD GLGEVYVVAV
     DPAEQGSGLG RALTATGLRH LAEDRKVPAV LLYVDADNPA AVRVYERLGF TVYEVDLMYR
     VDTAVRR
//
DBGET integrated database retrieval system