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Database: UniProt
Entry: A0A0P0N520_9CREN
LinkDB: A0A0P0N520_9CREN
Original site: A0A0P0N520_9CREN 
ID   A0A0P0N520_9CREN        Unreviewed;       284 AA.
AC   A0A0P0N520;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Putative lysine biosynthesis protein LysX {ECO:0000313|EMBL:ALL01880.1};
GN   ORFNames=Pyrde_1837 {ECO:0000313|EMBL:ALL01880.1};
OS   Pyrodictium delaneyi.
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Pyrodictium.
OX   NCBI_TaxID=1273541 {ECO:0000313|EMBL:ALL01880.1, ECO:0000313|Proteomes:UP000058613};
RN   [1] {ECO:0000313|EMBL:ALL01880.1, ECO:0000313|Proteomes:UP000058613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Su06 {ECO:0000313|EMBL:ALL01880.1,
RC   ECO:0000313|Proteomes:UP000058613};
RA   Jung J.-H., Lin J., Holden J.F., Park C.-S.;
RT   "Complete genome sequence of hyperthermophilic archaeon Pyrodictium
RT   delaneyi Su06.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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; CP013011; ALL01880.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P0N520; -.
DR   STRING; 1273541.Pyrde_1837; -.
DR   KEGG; pdl:Pyrde_1837; -.
DR   PATRIC; fig|1273541.4.peg.1952; -.
DR   Proteomes; UP000058613; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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:SF2; COENZYME GAMMA-F420-2:ALPHA-L-GLUTAMATE LIGASE; 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   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          95..279
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   284 AA;  30950 MW;  292EB5D636D89822 CRC64;
     MPRVGMAYMV ARWEEKAIAA AARRRGVELE LLHMPSFYAL IGDRRLGAKL PSVVLQRSIS
     HYVALSSTLL LESIGVRVVN RGQATAAAND KVWSLSLLAA AGIPTPVTGV AFGSEAASKL
     AEEIGYPVVV KPTNGSWGRM LALADDWEDL RVILEHREYM PQPEMKVHLI QEYVKKPDRD
     IRVTVVGGRP VAAIYRYSSH WITNTARGGK AEPAPTEGEL GELAVRAAEA VGLEVAGVDV
     FEDPERGYIV NEVNPVPEFK NTVAVTGVDV AAEILDYLVE LARR
//
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