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
//