LYSX_SULAC
ID LYSX_SULAC Reviewed; 276 AA.
AC Q4JAP9;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Alpha-aminoadipate--LysW ligase LysX;
DE Short=AAA--LysW ligase LysX;
DE EC=6.3.2.43 {ECO:0000269|PubMed:23434852};
GN Name=lysX; OrderedLocusNames=Saci_0754;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 253-ASN-THR-254.
RX PubMed=23434852; DOI=10.1038/nchembio.1200;
RA Ouchi T., Tomita T., Horie A., Yoshida A., Takahashi K., Nishida H.,
RA Lassak K., Taka H., Mineki R., Fujimura T., Kosono S., Nishiyama C.,
RA Masui R., Kuramitsu S., Albers S.V., Kuzuyama T., Nishiyama M.;
RT "Lysine and arginine biosyntheses mediated by a common carrier protein in
RT Sulfolobus.";
RL Nat. Chem. Biol. 9:277-283(2013).
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:0000269|PubMed:23434852}.
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:0000269|PubMed:23434852};
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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene require lysine for
CC growth. {ECO:0000269|PubMed:23434852}.
CC -!- SIMILARITY: Belongs to the RimK family. LysX subfamily. {ECO:0000305}.
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DR EMBL; CP000077; AAY80130.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4JAP9; -.
DR SMR; Q4JAP9; -.
DR STRING; 330779.Saci_0754; -.
DR EnsemblBacteria; AAY80130; AAY80130; Saci_0754.
DR KEGG; sai:Saci_0754; -.
DR PATRIC; fig|330779.12.peg.723; -.
DR eggNOG; arCOG01589; Archaea.
DR HOGENOM; CLU_054353_2_1_2; -.
DR OMA; YEHKVFY; -.
DR BRENDA; 6.3.2.43; 6160.
DR UniPathway; UPA00033; UER00035.
DR Proteomes; UP000001018; 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 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Ligase; Lysine biosynthesis;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..276
FT /note="Alpha-aminoadipate--LysW ligase LysX"
FT /id="PRO_0000422992"
FT DOMAIN 86..271
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT MOTIF 253..254
FT /note="N-[TS] motif that is essential for LysX substrate
FT specificity"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 126..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 162..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MUTAGEN 253..254
FT /note="NT->GF: Alters substrate specificity, so that
FT glutamate is preferred over alpha-aminoadipate."
FT /evidence="ECO:0000269|PubMed:23434852"
SQ SEQUENCE 276 AA; 31712 MW; 3BA4CE0980E8B635 CRC64;
MRWEEKDIIT EAKKSGFKAI PIFTKDFYSA IGVGENYSEL EADVIIQRNT SHARALTTSL
IFEGWNYNVV NDATSLFKCG NKLYTLSLLA KHNIKTPRTI VTFSKDKAVD LAKKIGFPAV
IKPIEGSWGR MVAKAVDEDI LYSFLEYQEY TTSQFRQIYL VQEFVKKPNR DIRIFVMGDE
APVGIYRVNE RNWKTNTALG ARALPLKIDD ELRDLALKVR DIMGGFFLGI DIFEDPERGY
LVNEVNGVPE YKNTVRVNNF NVSSYLLNKL REWIKK
