AC   MF_01697;
DC   Protein; auto
TR   HAMAP; MF_01697; -; 1; level=0
XX
Names: MshC
XX
ID   MSHC
DE   RecName: Full=L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase;
DE            Short=L-Cys:GlcN-Ins ligase;
DE            EC=6.3.1.13;
DE   AltName: Full=Mycothiol ligase;
DE            Short=MSH ligase;
GN   Name=mshC;
XX
CC   -!- FUNCTION: Catalyzes the ATP-dependent condensation of GlcN-Ins and L-
CC       cysteine to form L-Cys-GlcN-Ins.
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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MshC subfamily.
XX
DR   Pfam; PF01406; tRNA-synt_1e; 1; trigger=no
DR   PRINTS; PR00983; TRNASYNTHCYS; 1; trigger=no
DR   NCBIfam; TIGR03447; Mycothiol_MshC; 1; trigger=no
XX
KW   ATP-binding
KW   Ligase
KW   Metal-binding
KW   Nucleotide-binding
KW   Zinc
XX
GO   GO:0008270; F:zinc ion binding
GO   GO:0035446; F:cysteine-glucosaminylinositol ligase activity
GO   GO:0010125; P:mycothiol biosynthetic process
XX
FT   From: MSHC_MYCS2 (A0QZY0)
FT   BINDING         43..46
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT   Condition: C-G-I-T
FT   BINDING         81..83
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT   Condition: N-x-T
FT   BINDING         249..251
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT   Condition: G-x-D
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT   Condition: I-T-P-Y-D-[AS]-[AT]-H-[ILM]-G-H
FT   MOTIF           187..192
FT                   /note="'ERGGDP' region"
FT   Condition: [EDQ]-[HR]-G-G-D-P
FT   MOTIF           289..293
FT                   /note="'KMSKS' region"
FT   Condition: K-M-S-K-S
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: C
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: C
FT   BINDING         256
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: H
FT   BINDING         58
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT   Condition: [ST]
FT   BINDING         227
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT   Condition: W
FT   BINDING         283
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT   Condition: [LIV]
XX
Size: 384-520;
Related: None;
Template: A0QZY0; P9WJM9;
Scope:
 Bacteria; Actinomycetota
Fusion:
 Nter: None
 Cter: None
Duplicate: in CORJK, CORU7
Plasmid: in CORST
Comments: None
XX
# Revision 1.14 2023/06/01
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