ID A0A0F6QYD0_9CORY Unreviewed; 375 AA.
AC A0A0F6QYD0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase {ECO:0000256|ARBA:ARBA00020068};
DE EC=6.3.1.13 {ECO:0000256|ARBA:ARBA00012088};
DE AltName: Full=Mycothiol ligase {ECO:0000256|ARBA:ARBA00033376};
GN Name=mshC {ECO:0000313|EMBL:AKE39178.1};
GN ORFNames=UL81_06070 {ECO:0000313|EMBL:AKE39178.1};
OS Corynebacterium camporealensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=161896 {ECO:0000313|EMBL:AKE39178.1, ECO:0000313|Proteomes:UP000033566};
RN [1] {ECO:0000313|EMBL:AKE39178.1, ECO:0000313|Proteomes:UP000033566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44610 {ECO:0000313|EMBL:AKE39178.1,
RC ECO:0000313|Proteomes:UP000033566};
RX PubMed=26021938;
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete Genome Sequence of Corynebacterium camporealensis DSM 44610,
RT Isolated from the Milk of a Manchega Sheep with Subclinical Mastitis.";
RL Genome Announc. 3:e00572-15(2015).
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 -!- 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};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MshC subfamily. {ECO:0000256|ARBA:ARBA00007723}.
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DR EMBL; CP011311; AKE39178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F6QYD0; -.
DR KEGG; ccj:UL81_06070; -.
DR PATRIC; fig|161896.4.peg.1191; -.
DR HOGENOM; CLU_013528_0_0_11; -.
DR Proteomes; UP000033566; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035446; F:cysteine-glucosaminylinositol ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010125; P:mycothiol biosynthetic process; IEA:InterPro.
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 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:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AKE39178.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000033566}.
FT DOMAIN 1..298
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
SQ SEQUENCE 375 AA; 41413 MW; 89DCB26AB23D3CA9 CRC64;
MYVCGITPYD STHLGHAATY LTFDLIYRQL LDQGKQVHYV QNITDVDDPL FERAERDGVD
WRELGDSQID LFRSDMELLS VFPPQDYIGA MESVDEVIEM VGKLLDNGAA YVVDDEEYPD
VYASVDATQQ FGYESNYNDE QMAEFFAERG GDPDRKGKRN PLDALIWKAE RPGEPSWDSP
FGPGRPGWHV ECSAIATNRL GKSFDIQGGG SDLKFPHHEF SAAHAEAALG VERMANFYVH
TGMIGLDGTK MSKSLGNLVF VHKLVEQGED PSAIRLGIFA GHYRAERDWS DEVLDKAKQQ
LAAWTEAVEN PGDMAHAEQV VDKLRASLAN DVDTPAALAA VDEWAAGDRG ENDPQAGELV
ALALDSLLGV QVSRK
//