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MSHC_SEGRD
ID   MSHC_SEGRD              Reviewed;         420 AA.
AC   D6ZFG9;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 58.
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=Srot_1222;
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM
OS   44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae; Segniliparus.
OX   NCBI_TaxID=640132;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578;
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M., Schneider S.,
RA   Bruce D., Goodwin L., Pitluck S., Liolios K., Mikhailova N., Pati A.,
RA   Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chertkov O., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Detter J.C., Han C.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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; CP001958; ADG97693.1; -; Genomic_DNA.
DR   RefSeq; WP_013138149.1; NC_014168.1.
DR   AlphaFoldDB; D6ZFG9; -.
DR   SMR; D6ZFG9; -.
DR   STRING; 640132.Srot_1222; -.
DR   EnsemblBacteria; ADG97693; ADG97693; Srot_1222.
DR   KEGG; srt:Srot_1222; -.
DR   eggNOG; COG0215; Bacteria.
DR   HOGENOM; CLU_013528_0_0_11; -.
DR   OMA; HAWPASE; -.
DR   OrthoDB; 952207at2; -.
DR   Proteomes; UP000002247; 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..420
FT                   /note="L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-
FT                   glucopyranoside ligase"
FT                   /id="PRO_0000400484"
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           295..299
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         289
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01697"
SQ   SEQUENCE   420 AA;  45821 MW;  495F0F94948BE9FF CRC64;
     MRSWLAPSVP KLAGAGPRLR LWDSADRIIR PVTPGRTATM YVCGITPYDA THLGHAATYL
     AFDLVHRLWL DAGHQVAYAQ NITDVDDPLL ERADRDHRDW QELAAEQIEL FRTDMSALRV
     LPPHEYVGVT ESVGLVVAMV EKLLANQSAY VVAEGEYPDV YHRIAATEDF GYVSGYGREE
     MAQVFRERGG DPDRPGKADP LDALLWRAAR PGEPSWPSPF GPGRPGWHVE CSAIALDRIG
     FGFDVQGGGS DLVFPHHEFS AAHAQAQHGA GAADEHRRFA RNYVHAGMIG LDGEKMSKSL
     GNLVFVSALR ERGVDPSAIR LALFAGHYRA DRSWDQGLLR EAQERLARWR HAASLASGPA
     AHDVVARMRE HLANDLDTPK ALAALDSWSL EAAAHGGGDQ EAPALVARAA DALLGVQLTP
 
 
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