RIMK_ALKEH
ID RIMK_ALKEH Reviewed; 301 AA.
AC Q0A6C9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Probable alpha-L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01552};
DE EC=6.3.2.- {ECO:0000255|HAMAP-Rule:MF_01552};
GN Name=rimK {ECO:0000255|HAMAP-Rule:MF_01552}; OrderedLocusNames=Mlg_2266;
OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Alkalilimnicola.
OX NCBI_TaxID=187272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1;
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 Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL Submitted (AUG-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI57608.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000453; ABI57608.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041718046.1; NC_008340.1.
DR AlphaFoldDB; Q0A6C9; -.
DR SMR; Q0A6C9; -.
DR PRIDE; Q0A6C9; -.
DR EnsemblBacteria; ABI57608; ABI57608; Mlg_2266.
DR KEGG; aeh:Mlg_2266; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_054353_0_1_6; -.
DR OrthoDB; 937913at2; -.
DR Proteomes; UP000001962; 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"
FT /id="PRO_0000340538"
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; 33064 MW; CF08CD3B95D6AB77 CRC64;
MNILILSRNS RLYSTRRLVE AGRERGHQVR VVDPLRCYMN ISPHKPEIHY KGETLENFDG
VIPRIGASIT FYGTAVLRQF EIMGTFPLNE SVAISRSRDK LRSTQLLARK GIGLPMTTFG
YSPDDTEDLI NLVGGPPMVI KLLEGTQGKG VVLAETQQAA ESLIDAFRGL NVHFLAQEYI
KEAGGSDIRC FVVGERVVAS MRRQAKEGEF RSNIHRGGQA STVRITPEER SMAVRAARIM
GLNVAGVDLI RSAHGSLVLE VNSSPGLEGI EKATGKDIAG TIYAFLEKNA RQGKTRTRGR
G
