RIMK_HYDCU
ID RIMK_HYDCU Reviewed; 301 AA.
AC Q31DX2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=Tcr_2061;
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA Tinkham L.E., Zeruth G.T.;
RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT XCL-2.";
RL PLoS Biol. 4:1-17(2006).
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; CP000109; ABB42651.1; -; Genomic_DNA.
DR RefSeq; WP_011371478.1; NC_007520.2.
DR AlphaFoldDB; Q31DX2; -.
DR SMR; Q31DX2; -.
DR STRING; 317025.Tcr_2061; -.
DR PRIDE; Q31DX2; -.
DR EnsemblBacteria; ABB42651; ABB42651; Tcr_2061.
DR KEGG; tcx:Tcr_2061; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_054353_0_1_6; -.
DR OMA; CYMNIAS; -.
DR OrthoDB; 937913at2; -.
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.
FT CHAIN 1..301
FT /note="Probable alpha-L-glutamate ligase"
FT /id="PRO_1000068861"
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; 32549 MW; 43EEE7C48A092385 CRC64;
MKIAILSRNA KLYSTRRLIE AAEERGHEVR VIDALRCYMN ISSNHPQVHY KGEVLDGFDA
IIPRIGASIT FYGTAVLRQF EMMGVYPLNE SVAISRSRDK LRSLQLLSRR GVGLPVTGFA
HSPDDVNDLL ETVGGAPVVI KLLEGTQGVG VVLADTHSAA ESVIQAFNGL KANILVQEFI
KEARGADLRC FVIGGKVVAS MKRQAKDGEF RSNLHQGGSA SLVRITPEER ATAVRAAKIM
GLNVCGVDLL RSNHGPVVME VNSSPGIEGI ETATQKDIAS QIIAFIEKNA KPHNTKTRGK
G
