ID C4KJ26_SULIK Unreviewed; 283 AA.
AC C4KJ26;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Lysine biosynthesis enzyme LysX {ECO:0000313|EMBL:ACR42590.1};
GN OrderedLocusNames=M164_1986 {ECO:0000313|EMBL:ACR42590.1};
OS Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR42590.1, ECO:0000313|Proteomes:UP000001479};
RN [1] {ECO:0000313|EMBL:ACR42590.1, ECO:0000313|Proteomes:UP000001479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001402; ACR42590.1; -; Genomic_DNA.
DR RefSeq; WP_012714114.1; NC_012726.1.
DR AlphaFoldDB; C4KJ26; -.
DR GeneID; 8762088; -.
DR KEGG; sid:M164_1986; -.
DR HOGENOM; CLU_054353_2_1_2; -.
DR Proteomes; UP000001479; 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 93..278
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 283 AA; 33092 MW; 8C1581AFE79786AA CRC64;
MKIGILYDMP RWEEKNLIEE GKKLGYQVTT IYSKDFVLFS NEFNIENDVN LFIQRNISHN
RALITSFLVE QLGYPVINDH MTLIRCENKI FTTYILAKHN IPTPKTFIAF DKTNAMEYSK
KLGYPVVIKP VEGSWGRMVA KADNLDVLYS YLEYQEFSTQ KYKDIYYIQE FVNKPNRDIR
IFVIGDETPV GIYRVNENNW RTNTALGAKA YPLKIDEELK ELALKVKDII GGFFLGIDIF
EDKDRGYLVD EVNGVPEYKN TVRVNNFNIS KFLLEKAVEW VKK
//