ID A0A1Q4WBM9_9ACTN Unreviewed; 409 AA.
AC A0A1Q4WBM9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-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=AMK13_12835 {ECO:0000313|EMBL:OKI07480.1};
OS Streptomyces sp. CB02056.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703924 {ECO:0000313|EMBL:OKI07480.1, ECO:0000313|Proteomes:UP000186379};
RN [1] {ECO:0000313|EMBL:OKI07480.1, ECO:0000313|Proteomes:UP000186379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02056 {ECO:0000313|EMBL:OKI07480.1,
RC ECO:0000313|Proteomes:UP000186379};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI07480.1}.
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; LIPD01000004; OKI07480.1; -; Genomic_DNA.
DR RefSeq; WP_074002316.1; NZ_LIPD01000004.1.
DR AlphaFoldDB; A0A1Q4WBM9; -.
DR OrthoDB; 9815130at2; -.
DR Proteomes; UP000186379; 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:UP000186379};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01697}.
FT DOMAIN 36..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; 44326 MW; 49C5944D1DFDD79E CRC64;
MHAWPASEVP ALPGQGLPLR IHDTAAGTVR EVVPQDGTAR IYVCGITPYD ATHMGHAATY
NAFDLVQRVW RDAGHDVLYI QNVTDVDDPL LARAVETGQD WTALAERETA LFREDMTALR
MLPPAHYIGA VESIPWIVPI VQKLLASGAA YHVDGDIYFS VDADPRFGEV SGLTREAMRP
VFAERGGDPD RPGKRNPLDA LLWLAARPGE PAWDTELGHG RPGWHIECVA IALRYLGMSF
DIQGGGSDLS FPHHEMGAAH AQVATGAHPY AQAYVHAGMV ALDGHKMSKS RGNLVFVSAL
RREGVDPAAI RLALLSHHYR ADWEWTKSTL DEAVERLARW RAAVSRPDGP SAEQLLAEVR
EALANDLDAP AALAAVDRWA DRQEAEGGTD IGAPGLVTRT VDALLGVAL
//
