LYSX_SACS2
ID LYSX_SACS2 Reviewed; 275 AA.
AC Q7SI95; Q980W7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Alpha-aminoadipate--LysW ligase LysX;
DE Short=AAA--LysW ligase LysX;
DE EC=6.3.2.43;
GN Name=lysX; OrderedLocusNames=SSO0159;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION IN LYSINE BIOSYNTHESIS, AND INDUCTION.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=12042311; DOI=10.1074/jbc.m203528200;
RA Brinkman A.B., Bell S.D., Lebbink R.J., de Vos W.M., van der Oost J.;
RT "The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine
RT biosynthesis in response to lysine availability.";
RL J. Biol. Chem. 277:29537-29549(2002).
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:0000305|PubMed:12042311}.
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 -!- INDUCTION: Activated by LysM and repressed by lysine.
CC {ECO:0000269|PubMed:12042311}.
CC -!- SIMILARITY: Belongs to the RimK family. LysX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK40505.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE006641; AAK40505.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK000545; DAA00053.1; -; Genomic_DNA.
DR PIR; B90156; B90156.
DR AlphaFoldDB; Q7SI95; -.
DR SMR; Q7SI95; -.
DR STRING; 273057.SSO0159; -.
DR EnsemblBacteria; AAK40505; AAK40505; SSO0159.
DR KEGG; sso:SSO0159; -.
DR PATRIC; fig|273057.12.peg.156; -.
DR eggNOG; arCOG01589; Archaea.
DR HOGENOM; CLU_054353_2_1_2; -.
DR InParanoid; Q7SI95; -.
DR OMA; YEHKVFY; -.
DR PhylomeDB; Q7SI95; -.
DR UniPathway; UPA00033; UER00035.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043774; F:coenzyme F420-2 alpha-glutamyl ligase activity; IBA:GO_Central.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IBA:GO_Central.
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..275
FT /note="Alpha-aminoadipate--LysW ligase LysX"
FT /id="PRO_0000205500"
FT DOMAIN 85..270
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT MOTIF 252..253
FT /note="N-[TS] motif that is essential for LysX substrate
FT specificity"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 125..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 161..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 275 AA; 32028 MW; 038E3DD3B4FC8800 CRC64;
MPRWEEKNLI EEGKKLGYQV ATIYSKDFVL FSNDFTIDND TDLFIQRNVS HNRALITSFL
VEQVGYPVIN DHTTLIRCEN KIFTTYILAR HNIPTPKTFI AFDKTNAIEY SKKLGYPVVI
KPVEGSWGRM VAKADNLDVL YSYLEYQEFS TQKYKDIYYI QEFVNKPNRD IRIFVIGDET
PVGIYRVNEN NWRTNTALGA KAYPLKIDEE LRELALKVKD IIGGFFLGID IFEDKDRGYL
VDEVNGVPEY KNTVRVNNFN VSKFLLEKAA EWVKK
