ID A0A2A3HYU6_9ACTN Unreviewed; 409 AA.
AC A0A2A3HYU6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ORFNames=BX265_1226 {ECO:0000313|EMBL:PBC76509.1};
OS Streptomyces sp. TLI_235.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938860 {ECO:0000313|EMBL:PBC76509.1, ECO:0000313|Proteomes:UP000218662};
RN [1] {ECO:0000313|EMBL:PBC76509.1, ECO:0000313|Proteomes:UP000218662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TLI_235 {ECO:0000313|EMBL:PBC76509.1,
RC ECO:0000313|Proteomes:UP000218662};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2017) 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: 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:PBC76509.1}.
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DR EMBL; NSGV01000001; PBC76509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3HYU6; -.
DR OrthoDB; 9815130at2; -.
DR Proteomes; UP000218662; 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; 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|HAMAP-Rule:MF_01697};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01697}; Reference proteome {ECO:0000313|Proteomes:UP000218662};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01697}.
FT DOMAIN 39..334
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT MOTIF 184..189
FT /note="'ERGGDP' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT MOTIF 286..290
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 44..47
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 59
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 82..84
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 224
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 246..248
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT BINDING 280
FT /ligand="L-cysteinyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:144924"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
SQ SEQUENCE 409 AA; 44070 MW; A5FE975892F59513 CRC64;
MHAWPASEVP ALPGQGLPLR VFDTATSSVR VVVPDGPTAR LYVCGITPYD ATHLGHAATY
NTFDLVQRVW KDAGHDVLYV QNVTDVDDPL LERAVATGQD WTELAARETA LFREDMTALR
MLPPAHYVGA VESIPWIVPL VKQLLASGAA YELDGDIYFS VDADPRFGEV SGLDRDAMLP
VFAERGGDPQ RPGKKHPLDA LLWLAARPGE PAWDTELGHG RPGWHIECVA IALQYLGMSF
DIQGGGTDLS FPHHEMGAAH AQVATGENPY AKAYVHAGMV ALDGHKMSKS RGNLVFVSAL
RREGVDPAAI RLALLAHHYR SDWEWTEQDL ARAKERLARW RAAVSRPDGP SAEGMLAEVR
AALAEDLDAP AALAAVDRWA AAQTADGGED IGAPGLVSRT VDALLGVAL
//
