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Database: UniProt
Entry: Q4JAP9
LinkDB: Q4JAP9
Original site: Q4JAP9 
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
//
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