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MSHC_SACVD
ID   MSHC_SACVD              Reviewed;         415 AA.
AC   C7MWX8;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=Svir_22240;
OS   Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC
OS   12207 / P101).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharomonospora.
OX   NCBI_TaxID=471857;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101;
RX   PubMed=21304650; DOI=10.4056/sigs.20263;
RA   Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA   Goodwin L., Chain P., D'haeseleer P., Chen A., Palaniappan K., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Rohde M., Tindall B.J., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Saccharomonospora viridis type strain
RT   (P101).";
RL   Stand. Genomic Sci. 1:141-149(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; CP001683; ACU97232.1; -; Genomic_DNA.
DR   RefSeq; WP_015786545.1; NC_013159.1.
DR   AlphaFoldDB; C7MWX8; -.
DR   SMR; C7MWX8; -.
DR   STRING; 471857.Svir_22240; -.
DR   EnsemblBacteria; ACU97232; ACU97232; Svir_22240.
DR   KEGG; svi:Svir_22240; -.
DR   eggNOG; COG0215; Bacteria.
DR   HOGENOM; CLU_013528_0_0_11; -.
DR   OMA; HAWPASE; -.
DR   OrthoDB; 952207at2; -.
DR   Proteomes; UP000000841; 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; 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..415
FT                   /note="L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-
FT                   glucopyranoside ligase"
FT                   /id="PRO_0000400479"
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   MOTIF           187..192
FT                   /note="'ERGGDP' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   MOTIF           289..293
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         227
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   BINDING         249..251
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   BINDING         256
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
FT   BINDING         283
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
SQ   SEQUENCE   415 AA;  46005 MW;  F68C433B0F43C1D1 CRC64;
     MQTWSSVAVP RVPGTSRPLR LYDTATGQIR PTAPGRVAKM YVCGITPYDA THLGHAATYL
     AFDLVHRLWL DAGHEVHYVQ NVTDIDDPLL ERAERDSEDW VVLGLRETAL FREDMEALRV
     LPPRDFVGAV ESIPEVVEMI EKLLASGAAY RVDDPEYPDV YFDRSFTGRF GYESNYDDET
     MRAIFPERGG DPDRPGKRDP LDALLWRVER PGEPAWDSSL GRGRPGWHIE CSAIALKHLG
     IGFDVQGGGS DLVFPHHEFS AAHAEAMTGE HPFARHYVHA GMIGLDGEKM SKSKGNLVFV
     SRLRADDVDP SAIRLALFAG HYRDDREWTD ELLKQANSRL ARWREAVSLP SGPDAEATVD
     RLRDHLADDL DTPKALAAVD AWVDEALRHR SGTVGSESAP ALVRAAVDSL LGVVL
 
 
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