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Database: UniProt
Entry: A1RFM0
LinkDB: A1RFM0
Original site: A1RFM0 
ID   RIMK1_SHESW             Reviewed;         301 AA.
AC   A1RFM0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   13-FEB-2019, entry version 74.
DE   RecName: Full=Probable alpha-L-glutamate ligase 1 {ECO:0000255|HAMAP-Rule:MF_01552};
DE            EC=6.3.2.- {ECO:0000255|HAMAP-Rule:MF_01552};
GN   Name=rimK1 {ECO:0000255|HAMAP-Rule:MF_01552};
GN   OrderedLocusNames=Sputw3181_0614;
OS   Shewanella sp. (strain W3-18-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W3-18-1;
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.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella sp. W3-18-1.";
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}.
DR   EMBL; CP000503; ABM23465.1; -; Genomic_DNA.
DR   RefSeq; WP_011787996.1; NC_008750.1.
DR   SMR; A1RFM0; -.
DR   EnsemblBacteria; ABM23465; ABM23465; Sputw3181_0614.
DR   KEGG; shw:Sputw3181_0614; -.
DR   HOGENOM; HOG000293092; -.
DR   KO; K05844; -.
DR   OMA; NYLRCYM; -.
DR   BioCyc; SSP351745:G1G7O-645-MONOMER; -.
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:0006464; P:cellular protein modification process; IEA:InterPro.
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; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR   Pfam; PF08443; RimK; 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.
FT   CHAIN         1    301       Probable alpha-L-glutamate ligase 1.
FT                                /FTId=PRO_0000340566.
FT   DOMAIN      104    287       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01552}.
FT   NP_BIND     178    179       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   NP_BIND     211    213       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       248    248       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       260    260       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       260    260       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       262    262       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   BINDING     141    141       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   BINDING     187    187       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
SQ   SEQUENCE   301 AA;  32423 MW;  4CA3524ADE304856 CRC64;
     MKIGILSQFP QLYSTQRLVA ACESRGHEAV VINTLNCYMN INSIKPSIHY EGQELVGFDA
     IIPRIHASVT FYGCAVVRQF EMMGVFVAND SISIARSRDK LRALQLLSRK GIGMPITGFA
     NKPNDIPDLI NMVGGAPLVI KLLEGTQGIG VVLAETKTAA ESVIEAFLGL KANILVQEYI
     KESNGSDIRC FVVGDKVVAS MKRQGPEGDF RSNLHLGGCG ETVKITSVER KMAIAAVKAM
     GLVVAGVDIL RSNRGPLILE VNSAPGIEGI EQTTGISVTE PIVEYIEKMV AARKTNRPII
     A
//
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