ID Q18E33_HALWD Unreviewed; 299 AA.
AC Q18E33;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Putative glutamate--argW ligase {ECO:0000313|EMBL:CAJ53800.1};
DE EC=6.3.2.- {ECO:0000313|EMBL:CAJ53800.1};
GN Name=argX {ECO:0000313|EMBL:CAJ53800.1};
GN OrderedLocusNames=HQ_3714A {ECO:0000313|EMBL:CAJ53800.1};
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ53800.1, ECO:0000313|Proteomes:UP000001975};
RN [1] {ECO:0000313|EMBL:CAJ53800.1, ECO:0000313|Proteomes:UP000001975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001 {ECO:0000313|Proteomes:UP000001975};
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H.H., Palm P.P., Wende A.W., Falb M.M., Rampp M.M.,
RA Rodriguez-Valera F.F., Pfeiffer F.F., Oesterhelt D.D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the RimK family. LysX subfamily.
CC {ECO:0000256|ARBA:ARBA00006239}.
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DR EMBL; AM180088; CAJ53800.1; -; Genomic_DNA.
DR RefSeq; WP_011572882.1; NC_008212.1.
DR AlphaFoldDB; Q18E33; -.
DR STRING; 362976.HQ_3714A; -.
DR GeneID; 4193717; -.
DR KEGG; hwa:HQ_3714A; -.
DR eggNOG; arCOG01589; Archaea.
DR HOGENOM; CLU_054353_2_1_2; -.
DR Proteomes; UP000001975; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0009085; P:lysine biosynthetic process; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR02144; LysX_arch; 1.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:CAJ53800.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000001975}.
FT DOMAIN 94..278
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 299 AA; 32636 MW; 8264ADEAE7F54997 CRC64;
MNVGLLYSRI RQDEKLLLSE LRSRGHTITK IDIRDEQFDI ANPPAAFTQV DVVLDRCLAT
SRSYYITQFL EAYGIPIIND ATTADVCADK VKNSLALQSA EVPTPRTEVA FTTDSAMESI
ERFGYPCILK PVVGSWGRLM AKIDSASAAE AILEHKSTLG HYEHKVFYIQ EFVSKPGRDI
RVLAADGEPI AAMTRTADHW LTNAAKGAET APFSLDDRAR ELVADASKAV GGGLLGIDLM
ETGGGDYTVH EINHTVEFKA LNDAVSTDVP GEVIDWLEMA IDALSDNNSN EIITDAETT
//
