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Database: UniProt
Entry: Q970U6
LinkDB: Q970U6
Original site: Q970U6 
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   16-JAN-2019, entry version 91.
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 /
OS   7) (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.,
RA   Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S.,
RA   Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y.,
RA   Yoshizawa T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T.,
RA   Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic
RT   Crenarchaeon, 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
RP   INTERACTION 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
RT   in 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
CC       of the C-terminal glutamate residue in LysW.
CC       {ECO:0000250|UniProtKB:Q4J8E7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[2-aminoadipate-carrier protein]-C-terminal-L-glutamate +
CC         ATP + L-glutamate = [2-aminoadipate-carrier protein]-C-terminal-
CC         gamma-(L-glutamyl)-L-glutamate + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:52624, Rhea:RHEA-COMP:9693, Rhea:RHEA-COMP:13311,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:78525, ChEBI:CHEBI:136714,
CC         ChEBI:CHEBI:456216; 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.
CC       {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       Self; NbExp=3; IntAct=EBI-16037902, EBI-16037902;
CC   -!- SIMILARITY: Belongs to the RimK family. LysX subfamily.
CC       {ECO:0000305}.
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   ProteinModelPortal; Q970U6; -.
DR   SMR; Q970U6; -.
DR   DIP; DIP-61747N; -.
DR   IntAct; Q970U6; 1.
DR   STRING; 273063.ST1505; -.
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   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000228553; -.
DR   KO; K19412; -.
DR   OMA; VDKSMTS; -.
DR   OrthoDB; 42812at2157; -.
DR   BioCyc; STOK273063:G1G3D-1734-MONOMER; -.
DR   BRENDA; 6.3.2.B19; 6166.
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:0006464; P:cellular protein modification process; IEA:InterPro.
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;
KW   ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    282       Glutamate--LysW ligase ArgX.
FT                                /FTId=PRO_0000422990.
FT   DOMAIN       91    277       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     131    137       ATP. {ECO:0000305|PubMed:23434852}.
FT   NP_BIND     167    178       ATP. {ECO:0000305|PubMed:23434852}.
FT   REGION      203    204       Substrate binding.
FT                                {ECO:0000305|PubMed:23434852}.
FT   REGION      256    260       Substrate binding.
FT                                {ECO:0000305|PubMed:23434852}.
FT   MOTIF       259    260       GF motif that is essential for ArgX
FT                                substrate specificity.
FT                                {ECO:0000305|PubMed:23434852}.
FT   METAL       237    237       Magnesium 1.
FT                                {ECO:0000269|PubMed:23434852}.
FT   METAL       250    250       Magnesium 1.
FT                                {ECO:0000269|PubMed:23434852}.
FT   METAL       250    250       Magnesium 2.
FT                                {ECO:0000269|PubMed:23434852}.
FT   METAL       252    252       Magnesium 2.
FT                                {ECO:0000269|PubMed:23434852}.
FT   BINDING      87     87       ATP. {ECO:0000305|PubMed:23434852}.
FT   BINDING     127    127       ATP. {ECO:0000305|PubMed:23434852}.
FT   BINDING     192    192       Substrate. {ECO:0000305|PubMed:23434852}.
FT   BINDING     202    202       ATP. {ECO:0000305|PubMed:23434852}.
FT   STRAND        2      9       {ECO:0000244|PDB:3VPB}.
FT   HELIX        12     23       {ECO:0000244|PDB:3VPB}.
FT   STRAND       27     32       {ECO:0000244|PDB:3VPB}.
FT   TURN         33     35       {ECO:0000244|PDB:3VPB}.
FT   STRAND       38     41       {ECO:0000244|PDB:3VPB}.
FT   HELIX        42     46       {ECO:0000244|PDB:3VPB}.
FT   STRAND       48     52       {ECO:0000244|PDB:3VPB}.
FT   HELIX        57     69       {ECO:0000244|PDB:3VPB}.
FT   STRAND       73     76       {ECO:0000244|PDB:3VPB}.
FT   HELIX        78     84       {ECO:0000244|PDB:3VPB}.
FT   HELIX        87     96       {ECO:0000244|PDB:3VPB}.
FT   STRAND      104    107       {ECO:0000244|PDB:3VPB}.
FT   HELIX       110    120       {ECO:0000244|PDB:3VPB}.
FT   STRAND      122    127       {ECO:0000244|PDB:3VPB}.
FT   TURN        133    136       {ECO:0000244|PDB:3VPB}.
FT   STRAND      138    140       {ECO:0000244|PDB:3VPB}.
FT   HELIX       143    153       {ECO:0000244|PDB:3VPB}.
FT   HELIX       159    162       {ECO:0000244|PDB:3VPB}.
FT   STRAND      164    168       {ECO:0000244|PDB:3VPB}.
FT   STRAND      172    182       {ECO:0000244|PDB:3VPB}.
FT   STRAND      185    193       {ECO:0000244|PDB:3VPB}.
FT   HELIX       203    205       {ECO:0000244|PDB:3VPB}.
FT   STRAND      208    210       {ECO:0000244|PDB:3VPB}.
FT   HELIX       216    229       {ECO:0000244|PDB:3VPB}.
FT   STRAND      232    241       {ECO:0000244|PDB:3VPB}.
FT   TURN        242    244       {ECO:0000244|PDB:3VPB}.
FT   STRAND      245    254       {ECO:0000244|PDB:3VPB}.
FT   HELIX       258    264       {ECO:0000244|PDB:3VPB}.
FT   HELIX       268    280       {ECO:0000244|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
//
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