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Database: UniProt
Entry: A0A1R1LZU7_9MICC
LinkDB: A0A1R1LZU7_9MICC
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ID   A0A1R1LZU7_9MICC        Unreviewed;       458 AA.
AC   A0A1R1LZU7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=BGP79_05515 {ECO:0000313|EMBL:OMH33021.1};
OS   Tersicoccus sp. Bi-70.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Tersicoccus.
OX   NCBI_TaxID=1897634 {ECO:0000313|EMBL:OMH33021.1, ECO:0000313|Proteomes:UP000187343};
RN   [1] {ECO:0000313|EMBL:OMH33021.1, ECO:0000313|Proteomes:UP000187343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bi-70 {ECO:0000313|EMBL:OMH33021.1,
RC   ECO:0000313|Proteomes:UP000187343};
RA   Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT   "Draft genome of Tersicoccus sp. strain Bi-70.";
RL   Submitted (AUG-2016) 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:OMH33021.1}.
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DR   EMBL; MIEU01000012; OMH33021.1; -; Genomic_DNA.
DR   RefSeq; WP_076694927.1; NZ_MIEU01000012.1.
DR   AlphaFoldDB; A0A1R1LZU7; -.
DR   STRING; 1897634.BGP79_05515; -.
DR   OrthoDB; 9815130at2; -.
DR   Proteomes; UP000187343; 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   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}; Zinc {ECO:0000256|HAMAP-Rule:MF_01697}.
FT   DOMAIN          43..349
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   REGION          419..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           50..60
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   MOTIF           199..204
FT                   /note="'ERGGDP' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   MOTIF           301..305
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   BINDING         48..51
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   BINDING         48
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   BINDING         63
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   BINDING         86..88
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   BINDING         240
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   BINDING         244
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   BINDING         262..264
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
FT   BINDING         295
FT                   /ligand="L-cysteinyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144924"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01697"
SQ   SEQUENCE   458 AA;  48839 MW;  A884D7FBA172313F CRC64;
     MQSWPTPGLT PLEPMPGSVH LYDTAARAVV PVELAEESGR AVAGLYVCGI TPYDATHLGH
     AATYLAFDLL IRQWRDTGAA VTYVQNVTDV DDPLLERAEA TGVDWQDLAV EQTDLFRTDM
     TALRVLPPDH YIGAVEAVPW IVPAVEALVT AGIAYRVPGT GGEPDGDVYF DVEAARSTGW
     RIGALGGYDP DQLLAFFGER GGDPDRPGKR NPLDALLWRV AREGEPQWPG GVLGAGRPGW
     HIECSVIAER FLATPFTVQG GGNDLIFPHH DMSAGHAQAL TGRPLAHHFA HTGMVGFEGH
     KMSKSRGNLV LVSRLREAGV DPAAIRIAVL GQHYRSAWEY TDALLTVAQD RLARWRAAAA
     VADAATGPLR GDVDDADTRL VERLRDRLRD DLDTPGALAA VDAWAATVLG ARDDAAIDGD
     IDHGSDTATD TGTAGEPSLG RRAVDALLGV DLAPETAS
//
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