MSHC_JONDD
ID MSHC_JONDD Reviewed; 423 AA.
AC C7R3Z4;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=Jden_1195;
OS Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / BCRC 15368 / CIP
OS 55.134 / JCM 11481 / NBRC 15587 / NCTC 10816 / Prevot 55134) (Listeria
OS denitrificans).
OC Bacteria; Actinobacteria; Micrococcales; Jonesiaceae; Jonesia.
OX NCBI_TaxID=471856;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14870 / DSM 20603 / BCRC 15368 / CIP 55.134 / JCM 11481 / NBRC
RC 15587 / NCTC 10816 / Prevot 55134;
RX PubMed=21304666; DOI=10.4056/sigs.41646;
RA Pukall R., Gehrich-Schroter G., Lapidus A., Nolan M., Glavina Del Rio T.,
RA Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., Copeland A.,
RA Saunders E., Brettin T., Detter J.C., Bruce D., Goodwin L., Pati A.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Goker M.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Han C.;
RT "Complete genome sequence of Jonesia denitrificans type strain (Prevot
RT 55134).";
RL Stand. Genomic Sci. 1:262-269(2009).
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; CP001706; ACV08851.1; -; Genomic_DNA.
DR RefSeq; WP_015771479.1; NC_013174.1.
DR AlphaFoldDB; C7R3Z4; -.
DR SMR; C7R3Z4; -.
DR STRING; 471856.Jden_1195; -.
DR EnsemblBacteria; ACV08851; ACV08851; Jden_1195.
DR KEGG; jde:Jden_1195; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_0_11; -.
DR OMA; HAWPASE; -.
DR OrthoDB; 952207at2; -.
DR Proteomes; UP000000628; 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..423
FT /note="L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-
FT glucopyranoside ligase"
FT /id="PRO_0000400450"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT MOTIF 197..202
FT /note="'ERGGDP' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT MOTIF 300..304
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 45..48
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 60
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 83..85
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 238
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 260..262
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT BINDING 294
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
SQ SEQUENCE 423 AA; 45605 MW; 591C68FAE6E8BB54 CRC64;
MITWPAPQVP SIPGALTSVR VMDTSSGQLV ETVRPGVGES SMYVCGITPY DATHIGHAAT
YIAFDLLYRA WLDAGQRVVY TSNVTDVDDP LLERATATGV DWTELATSQI TLFFDDMSAL
GVLPPHTYLS AVESVPMVIS ATRHLLESGR AYRVPVPAQE RPVHSPAYDI YADVTSDPDF
GSISGYTSEE RVRLFTDRGG DPATPGKKNP IDPIMWKAQR EGEPGWDGDD LGWGRPGWHI
ECTTIAHCGI GRSCTVQGGG SDLIFPHHEM SSAHARALFG QDAGASVHAH AGLIAYQGEK
MSKSKGNLVF VSRLRQEGVD PMAIRLAILA NHYRDEWEWT SDVLDAGIKR HQLWLQAMST
NGGPHPGATL AAMREALSND LDAPRALDAV DAWAYATLAG NDEDPGAPGV VSRAVNALLG
IRL
