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MSHC_SALAI
ID   MSHC_SALAI              Reviewed;         412 AA.
AC   A8M264;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Sare_2322;
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=391037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-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; CP000850; ABV98180.1; -; Genomic_DNA.
DR   RefSeq; WP_012182481.1; NC_009953.1.
DR   AlphaFoldDB; A8M264; -.
DR   SMR; A8M264; -.
DR   STRING; 391037.Sare_2322; -.
DR   EnsemblBacteria; ABV98180; ABV98180; Sare_2322.
DR   GeneID; 5704246; -.
DR   KEGG; saq:Sare_2322; -.
DR   PATRIC; fig|391037.6.peg.2355; -.
DR   eggNOG; COG0215; Bacteria.
DR   HOGENOM; CLU_013528_0_0_11; -.
DR   OMA; HAWPASE; -.
DR   OrthoDB; 952207at2; -.
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   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..412
FT                   /note="L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-
FT                   glucopyranoside ligase"
FT                   /id="PRO_0000400481"
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   MOTIF           186..191
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   412 AA;  44789 MW;  69C66C12BE965EED CRC64;
     MDSWAGHEVP RLPGRGGPLM LFDSARQGVA ASTPTGTGTM YVCGITPYDA THLGHAATMI
     TFDLVQRVWR DAGLDVTYVQ NVTDIDDPLL ERAARDGEDW KVLAMRETAL FREDMVALRI
     IPPAHYVGAV ESIPDIAERV LTLVKEEAAY RIDDGTGDVY FDISAAPRFG YESNLGREQM
     LKIFPERGGD PDRAGKRDPL DPLLWRSARA DEPSWPGGGL GPGRPGWHIE CAVIALNLLG
     HRIDVQGGGN DLIFPHHECS AAHAELLTGQ SPFAQHYVHA GMIGLAGEKM SKSRGNLVFV
     SRLRADRVDP MAVRLALMSG HYRSDRSWND DLLVTAQKRL DRWRRAAAAP SGPSARTFLA
     AFRERLADDL DSPGALTLAD SWADAALVGT GDDQAAPALF ARAVDALLGV RL
 
 
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