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Database: UniProt
Entry: A0A248YN85_9ACTN
LinkDB: A0A248YN85_9ACTN
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ID   A0A248YN85_9ACTN        Unreviewed;       412 AA.
AC   A0A248YN85;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=CIK06_13890 {ECO:0000313|EMBL:ASW55039.1};
OS   Plantactinospora sp. KBS50.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Plantactinospora.
OX   NCBI_TaxID=2024580 {ECO:0000313|EMBL:ASW55039.1, ECO:0000313|Proteomes:UP000216795};
RN   [1] {ECO:0000313|EMBL:ASW55039.1, ECO:0000313|Proteomes:UP000216795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBS50 {ECO:0000313|EMBL:ASW55039.1,
RC   ECO:0000313|Proteomes:UP000216795};
RA   Juboi H., Hwang S.S., Yeo T.C., Nissom P.M.;
RT   "Genome sequencing and analysis of secondary metabolite biosynthetic
RT   capabilities of Plantactinospora sp. KBS50.";
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}.
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DR   EMBL; CP022961; ASW55039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A248YN85; -.
DR   KEGG; plk:CIK06_13890; -.
DR   OrthoDB; 9815130at2; -.
DR   Proteomes; UP000216795; 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; 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:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 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:UP000216795};
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           186..191
FT                   /note="'ERGGDP' 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   412 AA;  44439 MW;  FD7A6B1292C06D81 CRC64;
     MESWAGHELP RLPGAGRPLA LYDSARRGVH PTRPPGAATL YVCGITPYDA THLGHAATMI
     AFDLVQRMWR DAGLPVTYVQ NVTDIDDPLL ERAQRDHEDW VVLAMRETAL FREDMEALRI
     IPPTHYVGAV ESIPDIADKV LLLLKDGAAY RLEDGTGDVY FDVAAAPRWG AESNLDRAQM
     LELFAERGGD PDRAGKRDRL DPLLWRGARP DEPSWPGGEL GPGRPGWHIE CATIALNLLG
     ATIDVQGGGN DLIFPHHECS AAHAERLTGA LPFARHYAHA GMIGLDGEKM SKSRGNLVFV
     SRLRADRVDP MAIRLGLLAG HYRDDRAWTD EVLATAQGRL TRWRSAAAAP AGPSAGELLA
     GVRERLADDL DTPAVLALVD AWAAAAVAGE GTDADAPALM AATVDALLGV RL
//
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