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Database: UniProt
Entry: F0QTM9_VULM7
LinkDB: F0QTM9_VULM7
Original site: F0QTM9_VULM7 
ID   F0QTM9_VULM7            Unreviewed;       285 AA.
AC   F0QTM9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Lysine biosynthesis enzyme LysX {ECO:0000313|EMBL:ADY01742.1};
GN   OrderedLocusNames=VMUT_1538 {ECO:0000313|EMBL:ADY01742.1};
OS   Vulcanisaeta moutnovskia (strain 768-28).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Vulcanisaeta.
OX   NCBI_TaxID=985053 {ECO:0000313|EMBL:ADY01742.1, ECO:0000313|Proteomes:UP000007485};
RN   [1] {ECO:0000313|EMBL:ADY01742.1, ECO:0000313|Proteomes:UP000007485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=768-28 {ECO:0000313|EMBL:ADY01742.1,
RC   ECO:0000313|Proteomes:UP000007485};
RX   PubMed=21398550; DOI=10.1128/JB.00237-11;
RA   Gumerov V.M., Mardanov A.V., Beletsky A.V., Prokofeva M.I.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "Complete genome sequence of 'Vulcanisaeta moutnovskia' strain 768-28, a
RT   novel member of the hyperthermophilic crenarchaeal genus vulcanisaeta.";
RL   J. Bacteriol. 193:2355-2356(2011).
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; CP002529; ADY01742.1; -; Genomic_DNA.
DR   RefSeq; WP_013604904.1; NC_015151.1.
DR   AlphaFoldDB; F0QTM9; -.
DR   STRING; 985053.VMUT_1538; -.
DR   GeneID; 10289190; -.
DR   KEGG; vmo:VMUT_1538; -.
DR   eggNOG; arCOG01589; Archaea.
DR   HOGENOM; CLU_054353_2_1_2; -.
DR   OrthoDB; 33241at2157; -.
DR   Proteomes; UP000007485; 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          94..279
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   285 AA;  31662 MW;  1C571AF1962AA21A CRC64;
     MVLIEVVHFL YDVIRLDEKL LIREFDNLRM NYRLINAEKL TFEFPNSNDM GIAFIRTVSQ
     HRTQMLSQLY EAIGGKSINP AMSILIGNNK AVTLAILSRL GVPIPNSVVA LSSKVVIRSL
     DRVGVPAIVK PVHGSWGRLV SLVGSSDDMD LLIRHRDSME NPQYGTYLLQ EFVKKPGRDI
     RVTVVGDRAV AAIYRYAVGD DWRTNTARGG KAEAVRIDPE LEDISVRATK AIGAYYAGVD
     VVESDGGYKV LEVNTVPEFK NVQRVTGVNV ARHIAELVLD MARRG
//
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