MSHC_TSUPD
ID MSHC_TSUPD Reviewed; 414 AA.
AC D5UPJ5;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=Tpau_2140;
OS Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / CCUG 35730 / CIP
OS 100753 / JCM 10117 / KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040)
OS (Corynebacterium paurometabolum).
OC Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae;
OC Tsukamurella.
OX NCBI_TaxID=521096;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 / KCTC
RC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040;
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 Mikhailova N., Munk A.C., Brettin T., Detter J.C., Tapia R., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Jando M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; CP001966; ADG78751.1; -; Genomic_DNA.
DR RefSeq; WP_013126773.1; NC_014158.1.
DR AlphaFoldDB; D5UPJ5; -.
DR SMR; D5UPJ5; -.
DR STRING; 521096.Tpau_2140; -.
DR EnsemblBacteria; ADG78751; ADG78751; Tpau_2140.
DR KEGG; tpr:Tpau_2140; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_0_11; -.
DR OMA; HAWPASE; -.
DR OrthoDB; 952207at2; -.
DR Proteomes; UP000001213; 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_0000400493"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT MOTIF 187..192
FT /note="'ERGGDP' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT MOTIF 289..293
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 43..46
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 58
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 81..83
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 227
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 249..251
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 283
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
SQ SEQUENCE 414 AA; 45122 MW; 0DCDE9C701752815 CRC64;
MRSWPSPAVP TLSGPSVPLR LYDTSDQAVR SVNPGAVSGM YVCGITPYDA THLGHAATYL
TFDLINRVLR ANGHEVHYVQ NVTDVDDPLF ERAARDGIDW RDLGARETDL FCEDMQALRV
LAPQDYIGAV ESIDEVIALV GRLLENGAAY IVDDPEFPDV YYRTDATEQF GYESGYDRAT
MERFFAERGG DPDRPGKRDP LDALLWRAAR PGEPSWPSPQ GPGRPGWHIE CAAIAQNRLG
VGFDIQGGGS DLIFPHHEFS AAHVEADTGE RRFARHYVHA AMIGLDGEKM SKSRGNLVFV
STLRRAGVDP AAIRLGLFEG HYRTDRAWSD EVLARAQARL DLWRNAFAAA SSPDGAELVG
RLRRYLADDL DTPKALSALD AWAHRAVTSG GPDPDGPSTV ATAVDALLGV AVSA
