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Entry: A0A0M3T4A2_9MICC
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Original site: A0A0M3T4A2_9MICC 
ID   A0A0M3T4A2_9MICC        Unreviewed;       428 AA.
AC   A0A0M3T4A2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=AL755_11770 {ECO:0000313|EMBL:ALE05991.1};
OS   Arthrobacter sp. ERGS1:01.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE05991.1, ECO:0000313|Proteomes:UP000060433};
RN   [1] {ECO:0000313|EMBL:ALE05991.1, ECO:0000313|Proteomes:UP000060433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE05991.1,
RC   ECO:0000313|Proteomes:UP000060433};
RX   PubMed=26415659; DOI=10.1016/j.jbiotec.2015.09.025;
RA   Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT   "Complete genome sequence of Arthrobacter sp. ERGS1:01, a putative novel
RT   bacterium with prospective cold active industrial enzymes, isolated from
RT   East Rathong glacier in India.";
RL   J. Biotechnol. 214:139-140(2015).
RN   [2] {ECO:0000313|Proteomes:UP000060433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS1:01 {ECO:0000313|Proteomes:UP000060433};
RA   Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT   "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
RL   Submitted (AUG-2015) 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; CP012479; ALE05991.1; -; Genomic_DNA.
DR   RefSeq; WP_054011168.1; NZ_CP012479.1.
DR   AlphaFoldDB; A0A0M3T4A2; -.
DR   STRING; 1704044.AL755_11770; -.
DR   KEGG; are:AL755_11770; -.
DR   PATRIC; fig|1704044.3.peg.1629; -.
DR   OrthoDB; 9815130at2; -.
DR   Proteomes; UP000060433; 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:UP000060433};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01697}.
FT   DOMAIN          37..351
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           201..206
FT                   /note="'ERGGDP' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   MOTIF           303..307
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         242
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   BINDING         264..266
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   BINDING         297
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
SQ   SEQUENCE   428 AA;  45717 MW;  ADED992D8AB57318 CRC64;
     MKTWKSRPVP ELPGEMPALF LHETTANRVT ALPAGDTASL YVCGITPYDA THMGHAATYV
     AFDLLNRTWR DAGRTVSYVQ NVTDVDDPLL ERATRDGVDW RELAAEQTAL FHEDMEALNV
     LAPDNYIGAV EAIEWIVPQI EALVAAGVAY TVPGSEGGPD GDVYFSVDAA SASSQDGIDG
     PWWLGQVSGL SPEEMLPIFA ERGGDPQRSG KRNPLDALLW RVARDGEPHW DGASLGEGRP
     GWHIECTVIA QRFLPEPFTV QGGGSDLIFP HHEMGAGHAF ALSHVPMAQH YAHTGMVGLD
     GEKMSKSLGN LVLVSKLRAE GVDPSAIRLA ILANHYRSDW FWTDALLENA QAQLAAWRAA
     LPQTPEGSAP ELMAELRAAL AADLDAPRAL AAVDAWAATA AAAPAADGCE RDAALVSDAI
     EALLGVAL
//
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