位置:首页 > 蛋白库 > MSHC1_CORU7
MSHC1_CORU7
ID   MSHC1_CORU7             Reviewed;         404 AA.
AC   B1VEQ2;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase 1 {ECO:0000255|HAMAP-Rule:MF_01697};
DE            Short=L-Cys:GlcN-Ins ligase 1 {ECO:0000255|HAMAP-Rule:MF_01697};
DE            EC=6.3.1.13 {ECO:0000255|HAMAP-Rule:MF_01697};
DE   AltName: Full=Mycothiol ligase 1 {ECO:0000255|HAMAP-Rule:MF_01697};
DE            Short=MSH ligase 1 {ECO:0000255|HAMAP-Rule:MF_01697};
GN   Name=mshC1 {ECO:0000255|HAMAP-Rule:MF_01697}; OrderedLocusNames=cu0281;
OS   Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=504474;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43042 / DSM 7109;
RX   PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA   Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA   Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA   Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA   Puehler A.;
RT   "The lifestyle of Corynebacterium urealyticum derived from its complete
RT   genome sequence established by pyrosequencing.";
RL   J. Biotechnol. 136:11-21(2008).
CC   -!- FUNCTION: Catalyzes the ATP-dependent condensation of GlcN-Ins and L-
CC       cysteine to form L-Cys-GlcN-Ins. {ECO:0000255|HAMAP-Rule:MF_01697}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + ATP
CC         + L-cysteine = 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-
CC         glucopyranoside + AMP + diphosphate + H(+); Xref=Rhea:RHEA:26176,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:58886, ChEBI:CHEBI:58887,
CC         ChEBI:CHEBI:456215; EC=6.3.1.13; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01697};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01697};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01697};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01697}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MshC subfamily. {ECO:0000255|HAMAP-Rule:MF_01697}.
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; AM942444; CAQ04241.1; -; Genomic_DNA.
DR   RefSeq; WP_012359542.1; NC_010545.1.
DR   AlphaFoldDB; B1VEQ2; -.
DR   SMR; B1VEQ2; -.
DR   STRING; 504474.cu0281; -.
DR   EnsemblBacteria; CAQ04241; CAQ04241; cu0281.
DR   GeneID; 60605086; -.
DR   KEGG; cur:cu0281; -.
DR   eggNOG; COG0215; Bacteria.
DR   HOGENOM; CLU_013528_0_0_11; -.
DR   OrthoDB; 952207at2; -.
DR   Proteomes; UP000001727; Chromosome.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0035446; F:cysteine-glucosaminylinositol ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010125; P:mycothiol biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   CDD; cd00672; CysRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01697; MshC; 1.
DR   InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR   InterPro; IPR017812; Mycothiol_ligase_MshC.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR10890; PTHR10890; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR03447; mycothiol_MshC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Zinc.
FT   CHAIN           1..404
FT                   /note="L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-
FT                   glucopyranoside ligase 1"
FT                   /id="PRO_0000400443"
FT   MOTIF           49..59
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   MOTIF           188..193
FT                   /note="'ERGGDP' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   MOTIF           290..294
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   BINDING         47..50
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   BINDING         62
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   BINDING         85..87
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   BINDING         228
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   BINDING         250..252
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   BINDING         257
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   BINDING         284
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
SQ   SEQUENCE   404 AA;  44141 MW;  49333AC7C2DD6BDA CRC64;
     MHAWPDPSVP AVAGTPVPLK LFDTADQRVK EVDTTPDANG EVGMYVCGIT PYDSTHLGHA
     ATYLTFDLAQ RQLLANGHKV HYVQNITDVD DPLFERAERD GVDWRELGTS QINLFRSDME
     ILSVIPPRDY IGAMESVDEV IAMVQQLLDA GAAYELDQGD IYASIDATEQ FGYESNLDRA
     TMEEYFAERG GDPDREGKRD PLDALVWRGH REGEPAWDSP FGPGRPGWHV ECSAIATNRL
     GSHFAIQGGG SDLAFPHHEF SAAHAEAALK VERMAGHYVH AGMIALDGVK MSKSLGNLVF
     VHKLSEAGHD PSAIRLAVFA GHYREDRDFS DAILAEAEER LTRWREQLAG EVSEAEATEV
     VDKLRAILAD DLNTPEALSL LDGAAGDCNQ IIATALDGLL GVRI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024