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Database: UniProt
Entry: Q976J9
LinkDB: Q976J9
Original site: Q976J9 
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   16-JAN-2019, entry version 92.
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 /
OS   7) (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.,
RA   Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S.,
RA   Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y.,
RA   Yoshizawa T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T.,
RA   Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic
RT   Crenarchaeon, 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=[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: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
CC       1/5.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RimK family. LysX subfamily.
CC       {ECO:0000305}.
DR   EMBL; BA000023; BAB65148.1; -; Genomic_DNA.
DR   RefSeq; WP_010978130.1; NC_003106.2.
DR   ProteinModelPortal; Q976J9; -.
DR   SMR; Q976J9; -.
DR   STRING; 273063.ST0192; -.
DR   PRIDE; Q976J9; -.
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   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000228553; -.
DR   KO; K05827; -.
DR   OMA; YEHKVFY; -.
DR   OrthoDB; 42812at2157; -.
DR   BioCyc; STOK273063:G1G3D-223-MONOMER; -.
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: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   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Complete proteome; Ligase;
KW   Lysine biosynthesis; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    285       Alpha-aminoadipate--LysW ligase LysX.
FT                                /FTId=PRO_0000205501.
FT   DOMAIN       95    280       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     135    141       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     171    182       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   MOTIF       262    263       N-[TS] motif that is essential for LysX
FT                                substrate specificity.
FT   METAL       240    240       Magnesium 1. {ECO:0000250}.
FT   METAL       253    253       Magnesium 1. {ECO:0000250}.
FT   METAL       253    253       Magnesium 2. {ECO:0000250}.
FT   METAL       255    255       Magnesium 2. {ECO:0000250}.
FT   BINDING      91     91       ATP. {ECO:0000250}.
FT   BINDING     131    131       ATP. {ECO:0000250}.
FT   BINDING     196    196       ATP. {ECO:0000250}.
FT   BINDING     205    205       ATP. {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
//
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