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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//