位置:首页 > 蛋白库 > MSHD_GEOOG
MSHD_GEOOG
ID   MSHD_GEOOG              Reviewed;         308 AA.
AC   D2S4P5;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 61.
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}; OrderedLocusNames=Gobs_4647;
OS   Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC
OS   A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20).
OC   Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae;
OC   Geodermatophilus.
OX   NCBI_TaxID=526225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 / NBRC
RC   13315 / NRRL B-3577 / G-20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M.,
RA   Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Geodermatophilus obscurus DSM 43160.";
RL   Submitted (JAN-2010) 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: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}.
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; CP001867; ADB77195.1; -; Genomic_DNA.
DR   RefSeq; WP_012950619.1; NC_013757.1.
DR   AlphaFoldDB; D2S4P5; -.
DR   SMR; D2S4P5; -.
DR   STRING; 526225.Gobs_4647; -.
DR   EnsemblBacteria; ADB77195; ADB77195; Gobs_4647.
DR   KEGG; gob:Gobs_4647; -.
DR   eggNOG; COG0456; Bacteria.
DR   HOGENOM; CLU_068014_0_0_11; -.
DR   OMA; AEPWFDP; -.
DR   OrthoDB; 1526822at2; -.
DR   Proteomes; UP000001382; Chromosome.
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; 2.
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; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..308
FT                   /note="Mycothiol acetyltransferase"
FT                   /id="PRO_0000400258"
FT   DOMAIN          8..155
FT                   /note="N-acetyltransferase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   DOMAIN          160..308
FT                   /note="N-acetyltransferase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         39
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         84..86
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         240
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         244..246
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         251..257
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01698"
FT   BINDING         278
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"
SQ   SEQUENCE   308 AA;  33398 MW;  8D117115974356A6 CRC64;
     MSAAPLVRDV DRLDPAGVAA VLALLRAATA ADGVRPLSEE AELRLQHGGP AGGRDVLATA
     ADGALTGYAR FEGGEGTGDA EAELVVAPGS RRRGVGRALL TRLEELAGDR PLRVWAHGDL
     PGSAELAQRH GYERARVLLQ MRRELAGVDP EPRLRLPEGV QVRTFRSGTD EQAWLRTNAR
     AFASHPEQGS WTAEDLRLRE AEPWFDPAGF FLAWDGDRLL GSHWTKVHPP GDEGPEAVGE
     VYVLGIDPDA QGLGLGRALT DVGLAHLRRL GLRQVLLYVE EDNTAAVTLY ERSGFTRHAV
     DVSWRRAR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024