(data stored in ACNUC7421 zone)

SWISSPROT: MSHC_RHOOB

ID   MSHC_RHOOB              Reviewed;         415 AA.
AC   C1ASS8;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 46.
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};
GN   OrderedLocusNames=ROP_06130;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent condensation of GlcN-Ins and
CC       L-cysteine to form L-Cys-GlcN-Ins. {ECO:0000255|HAMAP-
CC       Rule:MF_01697}.
CC   -!- CATALYTIC ACTIVITY: 1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-
CC       1D-myo-inositol + L-cysteine + ATP = 1-O-(2-(L-cysteinamido)-2-
CC       deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + AMP + diphosphate.
CC       {ECO:0000255|HAMAP-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-
CC       Rule:MF_01697};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01697}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. MshC subfamily. {ECO:0000255|HAMAP-Rule:MF_01697}.
DR   EMBL; AP011115; BAH48860.1; -; Genomic_DNA.
DR   RefSeq; WP_012687865.1; NC_012522.1.
DR   ProteinModelPortal; C1ASS8; -.
DR   SMR; C1ASS8; -.
DR   STRING; 632772.ROP_06130; -.
DR   EnsemblBacteria; BAH48860; BAH48860; ROP_06130.
DR   KEGG; rop:ROP_06130; -.
DR   PATRIC; fig|632772.20.peg.672; -.
DR   eggNOG; ENOG4105C8N; Bacteria.
DR   eggNOG; COG0215; LUCA.
DR   HOGENOM; HOG000245251; -.
DR   KO; K15526; -.
DR   OMA; IFPHHEM; -.
DR   OrthoDB; POG091H004K; -.
DR   Proteomes; UP000002212; 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   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   PANTHER; PTHR10890:SF19; PTHR10890:SF19; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   TIGRFAMs; TIGR03447; mycothiol_MshC; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1ASS8.
DR   SWISS-2DPAGE; C1ASS8.
KW   ATP-binding; Complete proteome; Ligase; Metal-binding;
KW   Nucleotide-binding; Zinc.
FT   CHAIN         1    415       L-cysteine:1D-myo-inositol 2-amino-2-
FT                                deoxy-alpha-D-glucopyranoside ligase.
FT                                /FTId=PRO_0000400476.
FT   REGION       43     46       Cysteinyl adenylate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01697}.
FT   REGION       81     83       Cysteinyl adenylate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01697}.
FT   REGION      249    251       Cysteinyl adenylate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01697}.
FT   MOTIF        45     55       "HIGH" region. {ECO:0000255|HAMAP-
FT                                Rule:MF_01697}.
FT   MOTIF       187    192       "ERGGDP" region. {ECO:0000255|HAMAP-
FT                                Rule:MF_01697}.
FT   MOTIF       289    293       "KMSKS" region. {ECO:0000255|HAMAP-
FT                                Rule:MF_01697}.
FT   METAL        43     43       Zinc. {ECO:0000255|HAMAP-Rule:MF_01697}.
FT   METAL       231    231       Zinc. {ECO:0000255|HAMAP-Rule:MF_01697}.
FT   METAL       256    256       Zinc. {ECO:0000255|HAMAP-Rule:MF_01697}.
FT   BINDING      58     58       Cysteinyl adenylate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01697}.
FT   BINDING     227    227       Cysteinyl adenylate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01697}.
FT   BINDING     283    283       Cysteinyl adenylate; via amide nitrogen
FT                                and carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01697}.
SQ   SEQUENCE   415 AA;  45710 MW;  99C2B1F764035985 CRC64;
     MQSWSETAVP SVPGQGPPLR LFDTADRQVR PVTPGRTATM YVCGITPYDA THLGHAATYL
     TFDLVNRIWR DAGHDVHYVQ NVTDVDDPLF ERANRDGEDW VVLGMRETAL FREDMEALRV
     LPPRDYIGAV ESIGEVIEMV EKFVASGAAY VVDDPEFPDV YFRADATEQF GYESGYDRAT
     MDTFFAERGG DPDRPGKQNP LDALVWRAAR PGEPSWPSPF GPGRPGWHIE CSAIALNRIG
     SGFDVQGGGS DLIFPHHEYS AAHAESATGD RRFARHYVHT GMIGLDGEKM SKSRGNLVFV
     SKLRGEGVDP AAIRLGLLSG HYRQDRPWTE QVLADAHTRL QLWKDAAALE SAQSATDTIA
     RLRQHLADDL DTPKALDALD GWARRALDNG GSDTNAPTEF AAAVDALLGV RLRRP
//

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