MSHC_ARTS2
ID MSHC_ARTS2 Reviewed; 426 AA.
AC A0JWX8;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Arth_2168;
OS Arthrobacter sp. (strain FB24).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=290399;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB24;
RX PubMed=24501649; DOI=10.4056/sigs.4438185;
RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL Stand. Genomic Sci. 9:106-116(2013).
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; CP000454; ABK03548.1; -; Genomic_DNA.
DR RefSeq; WP_011692014.1; NC_008541.1.
DR AlphaFoldDB; A0JWX8; -.
DR SMR; A0JWX8; -.
DR STRING; 290399.Arth_2168; -.
DR EnsemblBacteria; ABK03548; ABK03548; Arth_2168.
DR KEGG; art:Arth_2168; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_0_11; -.
DR OMA; HAWPASE; -.
DR OrthoDB; 952207at2; -.
DR Proteomes; UP000000754; 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 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..426
FT /note="L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-
FT glucopyranoside ligase"
FT /id="PRO_0000400430"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT MOTIF 200..205
FT /note="'ERGGDP' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT MOTIF 302..306
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 241
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 263..265
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 296
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
SQ SEQUENCE 426 AA; 45580 MW; 5D1A68C5CF28BF49 CRC64;
MKSWISRPVP QLPGRMPAVR IFDTAVGAYS TLDATGEQSL YVCGITPYDA THMGHAASYV
AFDLLNRAWR DGGQRVAYVQ NVTDVDDPLL ERATATGVDW RDLAASQIEL FQTDMAALNV
LAPDHYVGAV ESIPEIVPAI ERLLHLGLAY RVTGTPGEPD GDVYYDVEAA SKHSAEAKDA
WTLGSVSGLS ETEMLELFAE RGGDPGRRGK RQALDPLLWR VARDGEPSWA GGELGSGRPG
WHIECTVIAQ KYLPAPFTVQ GGGSDLIFPH HEMGAGHAYS LTGVPLARHF AHAGMVGLDG
EKMSKSKGNL VLVSKLRAAG EEPAAIRLAI LAHHYRTDWS WTEAGFAQAK TRLAEWRDAL
TMAPGESAAT LIAEMRSELA NDLNAPGALA AVDRWAVAAK QQAGAGSPMD QALVSDAVNA
LLGVEL
