MSHC_CORA7
ID MSHC_CORA7 Reviewed; 414 AA.
AC C3PG89;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase {ECO:0000255|HAMAP-Rule:MF_01697};
DE Short=L-Cys:GlcN-Ins ligase {ECO:0000255|HAMAP-Rule:MF_01697};
DE EC=6.3.1.13 {ECO:0000255|HAMAP-Rule:MF_01697};
DE AltName: Full=Mycothiol ligase {ECO:0000255|HAMAP-Rule:MF_01697};
DE Short=MSH ligase {ECO:0000255|HAMAP-Rule:MF_01697};
GN Name=mshC {ECO:0000255|HAMAP-Rule:MF_01697}; OrderedLocusNames=cauri_1250;
OS Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS CN-1) (Corynebacterium nigricans).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=548476;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1;
RX PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT vaginal swab of a woman with spontaneous abortion.";
RL BMC Genomics 11:91-91(2010).
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; CP001601; ACP32843.1; -; Genomic_DNA.
DR RefSeq; WP_010186666.1; NZ_ACLH01000003.1.
DR AlphaFoldDB; C3PG89; -.
DR SMR; C3PG89; -.
DR STRING; 548476.cauri_1250; -.
DR EnsemblBacteria; ACP32843; ACP32843; cauri_1250.
DR GeneID; 31923873; -.
DR KEGG; car:cauri_1250; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_0_11; -.
DR OMA; HAWPASE; -.
DR OrthoDB; 952207at2; -.
DR Proteomes; UP000002077; Chromosome.
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 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 PANTHER; PTHR10890; PTHR10890; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
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..414
FT /note="L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-
FT glucopyranoside ligase"
FT /id="PRO_0000400437"
FT MOTIF 46..56
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 44..47
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 59
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 82..84
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 414 AA; 45942 MW; CA66809E7C0AD4D8 CRC64;
MQSWPVPHID SVPGTPSPLH LYDSADGEVK RLNIKGETAT MYVCGITPYD STHLGHAATY
LTFDLIYRQL LDNGYKVNYA QNITDVDDPL FERAERDGVD WRELGTSQIN LFRSDMELLS
VFPPQHFVGA MEAIDEITEM VQALLDAGAA YVVDDPDYPD VYASIEATKN FGYESNYSRE
QMETFFAERG GDPERPGKRD PLDALIWRAH REGEPAWESP FGPGRPGWHI ECSAIATNRL
GSSFDIQGGG SDLKFPHHEF SAAHAEAALG VERMAQSYVH TGMIGLEGTK MSKSLGNLVF
VHKLVEAGVD PSAIRLGVFS GHYREDRDWS DEVLHTAQER LERWRAASRN PGTVEEIKEV
VHNVRLALAE DLDTQRAIAV LDQWAEQALG AAEASEEASD VLRTAVNSLL GVRL
