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 16-JAN-2019, entry version 69.
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 /
OS NBRC 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
RT in 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=[2-aminoadipate-carrier protein]-C-terminal-L-glutamate +
CC ATP + L-2-aminoadipate = [2-aminoadipate-carrier protein]-C-
CC terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:41940, Rhea:RHEA-COMP:9693, Rhea:RHEA-
CC COMP:9694, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58672, ChEBI:CHEBI:78503,
CC ChEBI:CHEBI:78525, 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
CC 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.
CC {ECO:0000305}.
DR EMBL; CP000077; AAY80130.1; -; Genomic_DNA.
DR ProteinModelPortal; 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 eggNOG; COG0189; LUCA.
DR HOGENOM; HOG000228553; -.
DR KO; K05827; -.
DR OMA; YEHKVFY; -.
DR BRENDA; 6.3.2.B13; 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:0006464; P:cellular protein modification process; IEA:InterPro.
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; Complete proteome; Ligase;
KW Lysine biosynthesis; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1 276 Alpha-aminoadipate--LysW ligase LysX.
FT /FTId=PRO_0000422992.
FT DOMAIN 86 271 ATP-grasp. {ECO:0000255|PROSITE-
FT ProRule:PRU00409}.
FT NP_BIND 126 132 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00409}.
FT NP_BIND 162 173 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00409}.
FT MOTIF 253 254 N-[TS] motif that is essential for LysX
FT substrate specificity.
FT METAL 231 231 Magnesium 1. {ECO:0000250}.
FT METAL 244 244 Magnesium 1. {ECO:0000250}.
FT METAL 244 244 Magnesium 2. {ECO:0000250}.
FT METAL 246 246 Magnesium 2. {ECO:0000250}.
FT BINDING 82 82 ATP. {ECO:0000250}.
FT BINDING 122 122 ATP. {ECO:0000250}.
FT BINDING 187 187 ATP. {ECO:0000250}.
FT BINDING 196 196 ATP. {ECO:0000250}.
FT MUTAGEN 253 254 NT->GF: Alters substrate specificity, so
FT that glutamate is preferred over alpha-
FT aminoadipate.
FT {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
//
