ID A0A438B040_9NOCA Unreviewed; 413 AA.
AC A0A438B040;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase {ECO:0000256|HAMAP-Rule:MF_01697};
DE Short=L-Cys:GlcN-Ins ligase {ECO:0000256|HAMAP-Rule:MF_01697};
DE EC=6.3.1.13 {ECO:0000256|HAMAP-Rule:MF_01697};
DE AltName: Full=Mycothiol ligase {ECO:0000256|HAMAP-Rule:MF_01697};
DE Short=MSH ligase {ECO:0000256|HAMAP-Rule:MF_01697};
GN Name=mshC {ECO:0000256|HAMAP-Rule:MF_01697,
GN ECO:0000313|EMBL:RVW04350.1};
GN ORFNames=EGT50_06730 {ECO:0000313|EMBL:RVW04350.1};
OS Rhodococcus xishaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2487364 {ECO:0000313|EMBL:RVW04350.1, ECO:0000313|Proteomes:UP000283479};
RN [1] {ECO:0000313|EMBL:RVW04350.1, ECO:0000313|Proteomes:UP000283479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW51113 {ECO:0000313|EMBL:RVW04350.1,
RC ECO:0000313|Proteomes:UP000283479};
RA Li L., Lin H.W.;
RT "Rhodococcus spongicola sp. nov. and Rhodococcus xishaensis sp. nov. from
RT marine sponges.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent condensation of GlcN-Ins and L-
CC cysteine to form L-Cys-GlcN-Ins. {ECO:0000256|ARBA:ARBA00003679,
CC ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000987, ECO:0000256|HAMAP-
CC Rule:MF_01697};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01697};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01697};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_01697}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MshC subfamily. {ECO:0000256|ARBA:ARBA00007723, ECO:0000256|HAMAP-
CC Rule:MF_01697}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01697}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RVW04350.1}.
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DR EMBL; RKLO01000002; RVW04350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A438B040; -.
DR OrthoDB; 9815130at2; -.
DR Proteomes; UP000283479; Unassembled WGS sequence.
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; cd07955; Anticodon_Ia_Cys_like; 1.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 1.20.120.640; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR03447; mycothiol_MshC; 1.
DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR PANTHER; PTHR10890:SF33; L-CYSTEINE:1D-MYO-INOSITOL 2-AMINO-2-DEOXY-ALPHA-D-GLUCOPYRANOSIDE LIGASE; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01697};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01697};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01697};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01697}; Reference proteome {ECO:0000313|Proteomes:UP000283479};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01697}.
FT DOMAIN 36..337
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT MOTIF 289..293
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 43..46
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 58
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 81..83
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 227
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 249..251
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 283
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
SQ SEQUENCE 413 AA; 45191 MW; 299EF825A514EE6F CRC64;
MQSWSEIAVP SVPGQGPALR LYDTADRQVR PVTPGQTARM YVCGITPYDA THLGHAATYL
TFDLVNRIWL DAGHDVHYVQ NVTDIDDPLF ERAERDGEDW VVLGMRETAL FREDMEALRV
LPPRDYIGAV ESVKEVVELV EKFVASGAAY IVDDPEYPDV YFRADATTQF GYESGYDRAT
MDHLFALRGG DPDRPGKKDP LDALVWRAER AGEPSWPSPF GPGRPGWHVE CAAIALNRIG
SGFDIQGGGS DLIFPHHEYS AAHAESATGT RRFARHYVHA GMIGLDGEKM SKSRGNLVFV
SKLRGEGVDP AAIRLGLLAG HYRTDRPWTD ELLATAQERL SLWRKAAGLG SGPSADDTIA
RLRQHLADDL DTPKALDAVD GWVRRALDHG GPDASAPSAL ATAVDALLGI DLR
//
