ARGX_SULTO
ID ARGX_SULTO Reviewed; 282 AA.
AC Q970U6;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glutamate--LysW ligase ArgX {ECO:0000305};
DE EC=6.3.2.- {ECO:0000250|UniProtKB:Q4J8E7};
GN Name=argX {ECO:0000303|PubMed:23434852}; Synonyms=argE;
GN OrderedLocusNames=STK_15050;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH LYSW; ADP AND
RP MAGNESIUM, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION
RP WITH LYSW.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=23434852; DOI=10.1038/nchembio.1200;
RA Ouchi T., Tomita T., Horie A., Yoshida A., Takahashi K., Nishida H.,
RA Lassak K., Taka H., Mineki R., Fujimura T., Kosono S., Nishiyama C.,
RA Masui R., Kuramitsu S., Albers S.V., Kuzuyama T., Nishiyama M.;
RT "Lysine and arginine biosyntheses mediated by a common carrier protein in
RT Sulfolobus.";
RL Nat. Chem. Biol. 9:277-283(2013).
CC -!- FUNCTION: Catalyzes the ATP-dependent formation of a covalent bond
CC between the amino group of glutamate and the gamma-carboxyl group of
CC the C-terminal glutamate residue in LysW.
CC {ECO:0000250|UniProtKB:Q4J8E7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[amino-group carrier protein]-C-terminal-L-glutamate + ATP +
CC L-glutamate = [amino-group carrier protein]-C-terminal-gamma-(L-
CC glutamyl)-L-glutamate + ADP + H(+) + phosphate; Xref=Rhea:RHEA:52624,
CC Rhea:RHEA-COMP:9693, Rhea:RHEA-COMP:13311, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:78525, ChEBI:CHEBI:136714, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q4J8E7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23434852};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000269|PubMed:23434852};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000250|UniProtKB:Q4J8E7}.
CC -!- SUBUNIT: Homotetramer. Interacts with LysW.
CC {ECO:0000269|PubMed:23434852}.
CC -!- INTERACTION:
CC Q970U6; Q970U6: argX; NbExp=3; IntAct=EBI-16037902, EBI-16037902;
CC -!- SIMILARITY: Belongs to the RimK family. LysX subfamily. {ECO:0000305}.
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DR EMBL; BA000023; BAB66577.1; -; Genomic_DNA.
DR RefSeq; WP_010979555.1; NC_003106.2.
DR PDB; 3VPB; X-ray; 1.80 A; A/B/C/D=1-282.
DR PDB; 3VPC; X-ray; 1.87 A; A/B/C/D=1-282.
DR PDBsum; 3VPB; -.
DR PDBsum; 3VPC; -.
DR AlphaFoldDB; Q970U6; -.
DR SMR; Q970U6; -.
DR DIP; DIP-61747N; -.
DR IntAct; Q970U6; 1.
DR STRING; 273063.STK_15050; -.
DR EnsemblBacteria; BAB66577; BAB66577; STK_15050.
DR GeneID; 1459541; -.
DR KEGG; sto:STK_15050; -.
DR PATRIC; fig|273063.9.peg.1713; -.
DR eggNOG; arCOG01589; Archaea.
DR OMA; VDKSMTS; -.
DR OrthoDB; 42812at2157; -.
DR BRENDA; 6.3.2.B19; 15396.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009085; P:lysine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011870; LysX_arch.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR02144; LysX_arch; 1.
DR TIGRFAMs; TIGR00768; rimK_fam; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..282
FT /note="Glutamate--LysW ligase ArgX"
FT /id="PRO_0000422990"
FT DOMAIN 91..277
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT MOTIF 259..260
FT /note="GF motif that is essential for ArgX substrate
FT specificity"
FT /evidence="ECO:0000305|PubMed:23434852"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:23434852"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:23434852"
FT BINDING 131..137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:23434852"
FT BINDING 167..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:23434852"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:23434852"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:23434852"
FT BINDING 203..204
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:23434852"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23434852"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23434852"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23434852"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23434852"
FT BINDING 256..260
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:23434852"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:3VPB"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:3VPB"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3VPB"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:3VPB"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3VPB"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:3VPB"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3VPB"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:3VPB"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3VPB"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:3VPB"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 172..182
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:3VPB"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3VPB"
FT HELIX 216..229
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:3VPB"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:3VPB"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:3VPB"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:3VPB"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:3VPB"
SQ SEQUENCE 282 AA; 31534 MW; B1690D7F15D6E75F CRC64;
MRVVLIVDIV RQEEKLIAKA LEENKVQYDI INVAQEPLPF NKALGRYDVA IIRPVSMYRA
LYSSAVLEAA GVHTINSSDV INVCGDKILT YSKLYREGIP IPDSIIALSA EAALKAYEQR
GFPLIDKPPI GSWGRLVSLI RDVFEGKTII EHRELMGNSA LKAHIVQEYI QYKGRDIRCI
AIGEELLGCY ARNIPPNEWR ANVALGGTPS NIEVDEKLKE TVVKAVSIVH GEFVSIDILE
HPNKGYVVNE LNDVPEFKGF MVATNINVAQ KLVEYIKENY SK
