ARGX_SULAC
ID ARGX_SULAC Reviewed; 282 AA.
AC Q4J8E7;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Glutamate--LysW ligase ArgX {ECO:0000305};
DE EC=6.3.2.- {ECO:0000269|PubMed:23434852};
GN Name=argX {ECO:0000303|PubMed:23434852}; OrderedLocusNames=Saci_1621;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
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:0000269|PubMed:23434852}.
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:0000269|PubMed:23434852};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q970U6};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000250|UniProtKB:Q970U6};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000269|PubMed:23434852}.
CC -!- SUBUNIT: Homotetramer. Interacts with LysW.
CC {ECO:0000250|UniProtKB:Q970U6}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene require arginine for
CC growth. {ECO:0000269|PubMed:23434852}.
CC -!- SIMILARITY: Belongs to the RimK family. LysX subfamily. {ECO:0000305}.
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DR EMBL; CP000077; AAY80933.1; -; Genomic_DNA.
DR RefSeq; WP_011278435.1; NC_007181.1.
DR AlphaFoldDB; Q4J8E7; -.
DR SMR; Q4J8E7; -.
DR STRING; 330779.Saci_1621; -.
DR EnsemblBacteria; AAY80933; AAY80933; Saci_1621.
DR GeneID; 3474177; -.
DR KEGG; sai:Saci_1621; -.
DR PATRIC; fig|330779.12.peg.1560; -.
DR eggNOG; arCOG01589; Archaea.
DR HOGENOM; CLU_054353_2_1_2; -.
DR OMA; VDKSMTS; -.
DR BioCyc; MetaCyc:MON-18311; -.
DR BRENDA; 6.3.2.60; 6160.
DR BRENDA; 6.3.2.B19; 6160.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..282
FT /note="Glutamate--LysW ligase ArgX"
FT /id="PRO_0000422991"
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:0000250|UniProtKB:Q970U6"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q970U6"
FT BINDING 131..137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 167..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q970U6"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q970U6"
FT BINDING 203..204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q970U6"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q970U6"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q970U6"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q970U6"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q970U6"
FT BINDING 256..260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q970U6"
SQ SEQUENCE 282 AA; 31715 MW; 329F02E95A6F7997 CRC64;
MRVALVVDIV RQEEKLIAKA LEKFQLQYDV INVAQEPLPF NKALGRYDVA IIRPISMYRA
LYASAVLESA GVHTINSSDT ISLCGDKILT YSKLYREGIP IPDSIIAMSS DAALKAYEQK
GFPLIDKPPI GSWGRLVSLI RDIFEGKTII EHRELMGNSA LKVHIVQEYI NYKSRDIRCI
VIGSELLGCY ARNIPSNEWR ANIALGGYPS QIEVDHKLKE TVLKATSIIG GEFVSIDVME
HQSKNYVINE FNDVPEFKGF MLATNIDVAE ELVSYVKNNY LR
