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MSHD_FRASN
ID   MSHD_FRASN              Reviewed;         322 AA.
AC   A8LDL3;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Mycothiol acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01698};
DE            Short=MSH acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01698};
DE            EC=2.3.1.189 {ECO:0000255|HAMAP-Rule:MF_01698};
DE   AltName: Full=Mycothiol synthase {ECO:0000255|HAMAP-Rule:MF_01698};
GN   Name=mshD {ECO:0000255|HAMAP-Rule:MF_01698};
GN   OrderedLocusNames=Franean1_6177;
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia;
OC   unclassified Frankia.
OX   NCBI_TaxID=298653;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- FUNCTION: Catalyzes the transfer of acetyl from acetyl-CoA to
CC       desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_01698};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01698}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. MshD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01698}.
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DR   EMBL; CP000820; ABW15521.1; -; Genomic_DNA.
DR   RefSeq; WP_020463599.1; NC_009921.1.
DR   AlphaFoldDB; A8LDL3; -.
DR   SMR; A8LDL3; -.
DR   STRING; 298653.Franean1_6177; -.
DR   EnsemblBacteria; ABW15521; ABW15521; Franean1_6177.
DR   KEGG; fre:Franean1_6177; -.
DR   eggNOG; COG0456; Bacteria.
DR   HOGENOM; CLU_068014_0_0_11; -.
DR   OMA; AEPWFDP; -.
DR   OrthoDB; 1526822at2; -.
DR   GO; GO:0035447; F:mycothiol synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0010125; P:mycothiol biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01698; MshD; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR017813; Mycothiol_AcTrfase.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF13508; Acetyltransf_7; 1.
DR   PIRSF; PIRSF021524; MSH_acetyltransferase; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR03448; mycothiol_MshD; 1.
DR   PROSITE; PS51186; GNAT; 2.
PE   3: Inferred from homology;
KW   Acyltransferase; Repeat; Transferase.
FT   CHAIN           1..322
FT                   /note="Mycothiol acetyltransferase"
FT                   /id="PRO_0000400257"
FT   DOMAIN          5..150
FT                   /note="N-acetyltransferase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   DOMAIN          160..322
FT                   /note="N-acetyltransferase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         36
FT                   /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT                   alpha-D-glucopyranoside"
FT                   /ligand_id="ChEBI:CHEBI:58887"
FT                   /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         87..92
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         252
FT                   /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT                   alpha-D-glucopyranoside"
FT                   /ligand_id="ChEBI:CHEBI:58887"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         256..258
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         290
FT                   /ligand="1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-
FT                   alpha-D-glucopyranoside"
FT                   /ligand_id="ChEBI:CHEBI:58887"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         295..300
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
SQ   SEQUENCE   322 AA;  34273 MW;  635BF719B4B28A52 CRC64;
     MTSLSWLRAL DVADIAAITD LLAAAERADG NGGVSEDVRL TLRPGPVGGG VEHLVARAGS
     AVVGYAALGG TATERQAELV VHPDHRRRGV GTALVHALFA TTSPVSLNIW AHGDTPAAAA
     LATRNGFDRE RVLLQLRRPL ASVRPGDPDD LPRPIIPADV TIRAFEVGVD EEAWLAVNAE
     AFADHPEQGR WTLDDLRARE GEPWFDPAGF FLAERNGALL GFHWTKVHPQ DPVPEHPAAT
     DQPAGQPGPI GEVYVVGVAS AAAGTGLGAA LTIVGLRHLR DIGLASVMLY VDEDNARAVR
     LYTRLGFRRH AADVSYRRPA RG
 
 
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