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RIMK2_SHEAM
ID   RIMK2_SHEAM             Reviewed;         301 AA.
AC   A1SAF6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Probable alpha-L-glutamate ligase 2 {ECO:0000255|HAMAP-Rule:MF_01552};
DE            EC=6.3.2.- {ECO:0000255|HAMAP-Rule:MF_01552};
GN   Name=rimK2 {ECO:0000255|HAMAP-Rule:MF_01552}; OrderedLocusNames=Sama_3160;
OS   Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=326297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1098 / SB2B;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella amazonensis SB2B.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01552};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01552};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01552};
CC   -!- SIMILARITY: Belongs to the RimK family. {ECO:0000255|HAMAP-
CC       Rule:MF_01552}.
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DR   EMBL; CP000507; ABM01363.1; -; Genomic_DNA.
DR   RefSeq; WP_011761267.1; NC_008700.1.
DR   AlphaFoldDB; A1SAF6; -.
DR   SMR; A1SAF6; -.
DR   STRING; 326297.Sama_3160; -.
DR   EnsemblBacteria; ABM01363; ABM01363; Sama_3160.
DR   KEGG; saz:Sama_3160; -.
DR   eggNOG; COG0189; Bacteria.
DR   HOGENOM; CLU_054353_0_1_6; -.
DR   OMA; CYMNIAS; -.
DR   OrthoDB; 937913at2; -.
DR   Proteomes; UP000009175; Chromosome.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01552; RimK; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR023533; RimK.
DR   InterPro; IPR041107; Rimk_N.
DR   InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR   Pfam; PF08443; RimK; 1.
DR   Pfam; PF18030; Rimk_N; 1.
DR   TIGRFAMs; TIGR00768; rimK_fam; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..301
FT                   /note="Probable alpha-L-glutamate ligase 2"
FT                   /id="PRO_0000340547"
FT   DOMAIN          104..287
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         178..179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         211..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         248
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         260
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         260
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         260
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         260
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         262
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         262
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
SQ   SEQUENCE   301 AA;  32435 MW;  6BE8A149212A5CB5 CRC64;
     MKIGVLSQFP ELYSTRRLVE ACESRGHEAW VINPINCYMN INSVKPSIHL EGEEVPMFDA
     IIPRIHASVT FYGCAVVRQF EMMGVFAAND SISIARSRDK LRALQLLSRK GIGMPVTGFA
     NKPNNIPDLI NMVGGAPLVI KLLEGTQGIG VVLAETRKAA ESVIEAFLGL KANIMVQEYI
     KEANGSDIRC FVVGDKVVAA MRRQGPEGDF RSNLHLGGSA EPVKITPQER KSAVAAAKAM
     GLVVAGVDIL RSARGPLVLE VNSAPGIEGI EQATGIKVAE PIVEYIEKVV AARRANHQVI
     A
 
 
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