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 29-MAY-2013, entry version 26.
DE RecName: Full=L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase;
DE Short=L-Cys:GlcN-Ins ligase;
DE EC=6.3.1.13;
DE AltName: Full=Mycothiol ligase;
DE Short=MSH ligase;
GN Name=mshC; OrderedLocusNames=ROP_06130;
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Nocardiaceae; 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 (By similarity).
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 -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family. MshC subfamily.
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DR EMBL; AP011115; BAH48860.1; -; Genomic_DNA.
DR RefSeq; YP_002777805.1; NC_012522.1.
DR ProteinModelPortal; C1ASS8; -.
DR STRING; 632772.ROP_06130; -.
DR EnsemblBacteria; BAH48860; BAH48860; ROP_06130.
DR GeneID; 7747768; -.
DR KEGG; rop:ROP_06130; -.
DR PATRIC; 23218379; VBIRhoOpa21106_0608.
DR eggNOG; COG0215; -.
DR HOGENOM; HOG000245251; -.
DR KO; K15526; -.
DR OMA; DVHYVQN; -.
DR ProtClustDB; PRK12418; -.
DR BioCyc; ROPA632772:GH0Q-612-MONOMER; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035446; F:cysteine-glucosaminylinositol ligase activity; IEA:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR GO; GO:0010125; P:mycothiol biosynthetic process; IEA:HAMAP.
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 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; 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 (By
FT similarity).
FT REGION 81 83 Cysteinyl adenylate binding (By
FT similarity).
FT REGION 249 251 Cysteinyl adenylate binding (By
FT similarity).
FT MOTIF 45 55 "HIGH" region (By similarity).
FT MOTIF 187 192 "ERGGDP" region (By similarity).
FT MOTIF 289 293 "KMSKS" region (By similarity).
FT METAL 43 43 Zinc (By similarity).
FT METAL 231 231 Zinc (By similarity).
FT METAL 256 256 Zinc (By similarity).
FT BINDING 58 58 Cysteinyl adenylate (By similarity).
FT BINDING 227 227 Cysteinyl adenylate (By similarity).
FT BINDING 283 283 Cysteinyl adenylate; via amide nitrogen
FT and carbonyl oxygen (By similarity).
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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