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Database: UniProt
Entry: Q7SI95
LinkDB: Q7SI95
Original site: Q7SI95 
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   16-JAN-2019, entry version 85.
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 /
OS   P2) (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.,
RA   Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A.,
RA   De Moors A., Erauso G., Fletcher C., Gordon P.M.K.,
RA   Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X.,
RA   Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N.,
RA   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=[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   -!- INDUCTION: Activated by LysM and repressed by lysine.
CC       {ECO:0000269|PubMed:12042311}.
CC   -!- SIMILARITY: Belongs to the RimK family. LysX subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK40505.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; AE006641; AAK40505.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK000545; DAA00053.1; -; Genomic_DNA.
DR   PIR; B90156; B90156.
DR   ProteinModelPortal; 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   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000228553; -.
DR   InParanoid; Q7SI95; -.
DR   KO; K05827; -.
DR   OMA; YEHKVFY; -.
DR   UniPathway; UPA00033; UER00035.
DR   Proteomes; UP000001974; Chromosome.
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: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    275       Alpha-aminoadipate--LysW ligase LysX.
FT                                /FTId=PRO_0000205500.
FT   DOMAIN       85    270       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     125    131       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     161    172       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   MOTIF       252    253       N-[TS] motif that is essential for LysX
FT                                substrate specificity.
FT   METAL       230    230       Magnesium 1. {ECO:0000250}.
FT   METAL       243    243       Magnesium 1. {ECO:0000250}.
FT   METAL       243    243       Magnesium 2. {ECO:0000250}.
FT   METAL       245    245       Magnesium 2. {ECO:0000250}.
FT   BINDING      81     81       ATP. {ECO:0000250}.
FT   BINDING     121    121       ATP. {ECO:0000250}.
FT   BINDING     186    186       ATP. {ECO:0000250}.
FT   BINDING     195    195       ATP. {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
//
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