ID S5TJD7_9CORY Unreviewed; 410 AA.
AC S5TJD7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase {ECO:0000256|HAMAP-Rule:MF_01697};
DE Short=L-Cys:GlcN-Ins ligase {ECO:0000256|HAMAP-Rule:MF_01697};
DE EC=6.3.1.13 {ECO:0000256|HAMAP-Rule:MF_01697};
DE AltName: Full=Mycothiol ligase {ECO:0000256|HAMAP-Rule:MF_01697};
DE Short=MSH ligase {ECO:0000256|HAMAP-Rule:MF_01697};
GN Name=mshC {ECO:0000256|HAMAP-Rule:MF_01697};
GN ORFNames=B841_06875 {ECO:0000313|EMBL:AGS34848.1};
OS Corynebacterium maris DSM 45190.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS34848.1, ECO:0000313|Proteomes:UP000015388};
RN [1] {ECO:0000313|EMBL:AGS34848.1, ECO:0000313|Proteomes:UP000015388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT 45190).";
RL Submitted (NOV-2012) 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:0000256|ARBA:ARBA00003679,
CC ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000987, ECO:0000256|HAMAP-
CC Rule:MF_01697};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01697};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01697};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_01697}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MshC subfamily. {ECO:0000256|ARBA:ARBA00007723, ECO:0000256|HAMAP-
CC Rule:MF_01697}.
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DR EMBL; CP003924; AGS34848.1; -; Genomic_DNA.
DR RefSeq; WP_020934781.1; NC_021915.1.
DR AlphaFoldDB; S5TJD7; -.
DR STRING; 1224163.B841_06875; -.
DR KEGG; cmd:B841_06875; -.
DR PATRIC; fig|1224163.3.peg.1381; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_0_11; -.
DR OrthoDB; 9815130at2; -.
DR Proteomes; UP000015388; 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; 1.20.120.640; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR03447; mycothiol_MshC; 1.
DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR PANTHER; PTHR10890:SF33; L-CYSTEINE:1D-MYO-INOSITOL 2-AMINO-2-DEOXY-ALPHA-D-GLUCOPYRANOSIDE LIGASE; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01697};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01697};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01697};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01697}; Reference proteome {ECO:0000313|Proteomes:UP000015388};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01697}.
FT DOMAIN 36..334
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT MOTIF 184..189
FT /note="'ERGGDP' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT MOTIF 286..290
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 40..43
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 55
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 78..80
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 224
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 246..248
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 280
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
SQ SEQUENCE 410 AA; 45084 MW; 2AF67E304C3CAC9E CRC64;
MHSWPHPAVP DVGGVSVPLH LYDSADEVIK PVQGSGMYVC GITPYDSTHL GHAATYVTFD
VVYRVLKDNG HDVHYVQNIT DVDDPLFERA QRDGVDWREL GESQIELFRT DMEQLSVIPP
RDYIGAVESV DEVIDLVQRL LDVGAAYVVD DAEHPDVYAS IEATEQFGYQ SNYSRAQMEE
FFAERGGDPE RPGKRDPLDA LVWQARREGE PHWESPFGPG RPGWHVECSA IATNRLGSNF
AIQGGGSDLK FPHHEFSAAH AEAASGGERM AEHYVHAGMI GLEGTKMSKS LGNLVFVHKL
TEAGHDPAAI RLGIYASHYR SDRDWSDDIL AVAEKRLAVW REALQTPGSL ADAEAAVAKL
RERLSDDLDT AGAMEAIDEW AQADSLDDAA AAELMADSVE GLLGVRLREK
//
