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}.
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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