LYSX_SULTO
ID LYSX_SULTO Reviewed; 285 AA.
AC Q976J9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Alpha-aminoadipate--LysW ligase LysX;
DE Short=AAA--LysW ligase LysX;
DE EC=6.3.2.43;
GN Name=lysX; OrderedLocusNames=STK_01920;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
CC -!- FUNCTION: Catalyzes the ATP-dependent formation of a covalent bond
CC between the amino group of alpha-aminoadipate (AAA) and the gamma-
CC carboxyl group of the C-terminal glutamate residue in LysW.
CC {ECO:0000250|UniProtKB:Q4JAP9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[amino-group carrier protein]-C-terminal-L-glutamate + ATP +
CC L-2-aminoadipate = [amino-group carrier protein]-C-terminal-N-(1,4-
CC dicarboxybutan-1-yl)-L-glutamine + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:41940, Rhea:RHEA-COMP:9693, Rhea:RHEA-COMP:9694,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58672, ChEBI:CHEBI:78503, ChEBI:CHEBI:78525,
CC ChEBI:CHEBI:456216; EC=6.3.2.43;
CC Evidence={ECO:0000250|UniProtKB:Q4JAP9};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 1/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RimK family. LysX subfamily. {ECO:0000305}.
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DR EMBL; BA000023; BAB65148.1; -; Genomic_DNA.
DR RefSeq; WP_010978130.1; NC_003106.2.
DR AlphaFoldDB; Q976J9; -.
DR SMR; Q976J9; -.
DR STRING; 273063.STK_01920; -.
DR EnsemblBacteria; BAB65148; BAB65148; STK_01920.
DR GeneID; 1458076; -.
DR KEGG; sto:STK_01920; -.
DR PATRIC; fig|273063.9.peg.235; -.
DR eggNOG; arCOG01589; Archaea.
DR OMA; YEHKVFY; -.
DR OrthoDB; 42812at2157; -.
DR UniPathway; UPA00033; UER00035.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.1490.20; -; 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; RpS6_RimK/Lys_biosynth_LsyX.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR02144; LysX_arch; 1.
DR TIGRFAMs; TIGR00768; rimK_fam; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Ligase; Lysine biosynthesis;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..285
FT /note="Alpha-aminoadipate--LysW ligase LysX"
FT /id="PRO_0000205501"
FT DOMAIN 95..280
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT MOTIF 262..263
FT /note="N-[TS] motif that is essential for LysX substrate
FT specificity"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 135..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 171..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 285 AA; 33107 MW; 6077CF2995B7DFBD CRC64;
MILGVIYDLL RWEEKNLIQE ARKLGHTVIP IYTKDFYYFY NNDSNETLGD LDVVIQRNTS
HARAVITSTI FENLSYKTIN DSSTLIKCEN KLYTLSLLSK HGIRVPKTIV AFSKEKALEL
ANKLSYPVVI KPVEGSWGRM VARAIDEDTL RNFLEYQEYT TLQFRYIYLI QEFVKKPDRD
IRIFTIGDEA PVGIYRVNSR NWKTNTALGA KAEPLKIDEE LQDLALKVKD IIGGFFLGID
VFEDPERGYI INEVNGVPEY KNTVRVNNFN VSEYLIRKIE EWIKK
