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MSHC_MYCSJ
ID   MSHC_MYCSJ              Reviewed;         415 AA.
AC   A3Q1B7;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Mjls_3165;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-2007) 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; CP000580; ABN98944.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3Q1B7; -.
DR   SMR; A3Q1B7; -.
DR   STRING; 164757.Mjls_3165; -.
DR   KEGG; mjl:Mjls_3165; -.
DR   HOGENOM; CLU_013528_0_0_11; -.
DR   OMA; HAWPASE; -.
DR   BioCyc; MSP164757:G1G8C-3190-MON; -.
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; Zinc.
FT   CHAIN           1..415
FT                   /note="L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-
FT                   glucopyranoside ligase"
FT                   /id="PRO_0000400463"
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   415 AA;  45517 MW;  C99447E17632E85F CRC64;
     MESWSAPEVP ALPGRGPQLR LYDSADRQVR PVSAGDTATM YVCGITPYDA THLGHAATYL
     AFDLVHRLWL DAGHRVHYVQ NITDVDDPLF ERAARDGIDW RDLGAREIQL FREDMAALRV
     LPPHDYVAAT DAIAEVIELV EKMLASGAAY VVDDPEFPDV YYRADATVQF GYESNYDHET
     MLTLFAERGG DPDRAGKADE LDALLWRAER PGEPSWPSPF GPGRPGWHVE CAAIALSRIG
     TGLDIQGGGS DLIFPHHEFS AAHAESVTGE RRFARHYVHA GMIGWDGHKM SKSRGNLVLV
     SRLRAEGVDP SAIRLGLLAG HYREDRFWSD DVLSDAQTRL QRWRRATSLP TGPDATDVLA
     RVRTYLADDL DTPKALIALD AWCTEALDGG GSDVTAPKTV ATAVDALLGV ALPVE
 
 
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