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Entry: E8PL67_THESS
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Original site: E8PL67_THESS 
ID   E8PL67_THESS            Unreviewed;       438 AA.
AC   E8PL67;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=isocitrate lyase {ECO:0000256|ARBA:ARBA00012909};
DE            EC=4.1.3.1 {ECO:0000256|ARBA:ARBA00012909};
DE   AltName: Full=Isocitrase {ECO:0000256|ARBA:ARBA00031022};
DE   AltName: Full=Isocitratase {ECO:0000256|ARBA:ARBA00031921};
GN   Name=aceA {ECO:0000313|EMBL:ADW21031.1};
GN   OrderedLocusNames=TSC_c03940 {ECO:0000313|EMBL:ADW21031.1};
OS   Thermus scotoductus (strain ATCC 700910 / SA-01).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=743525 {ECO:0000313|EMBL:ADW21031.1, ECO:0000313|Proteomes:UP000008087};
RN   [1] {ECO:0000313|Proteomes:UP000008087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RA   Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
RA   Gottschalk G., van Heerden E., Litthauer D.;
RT   "The genome sequence of Thermus scotoductus SA-01.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADW21031.1, ECO:0000313|Proteomes:UP000008087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RX   PubMed=22115438; DOI=10.1186/1471-2164-12-577;
RA   Gounder K., Brzuszkiewicz E., Liesegang H., Wollherr A., Daniel R.,
RA   Gottschalk G., Reva O., Kumwenda B., Srivastava M., Bricio C.,
RA   Berenguer J., van Heerden E., Litthauer D.;
RT   "Sequence of the hyperplastic genome of the naturally competent Thermus
RT   scotoductus SA-01.";
RL   BMC Genomics 12:577-577(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-threo-isocitrate = glyoxylate + succinate;
CC         Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:36655; EC=4.1.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00023531};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001362-3};
CC       Note=Can also use Mn(2+) ion. {ECO:0000256|PIRSR:PIRSR001362-3};
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DR   EMBL; CP001962; ADW21031.1; -; Genomic_DNA.
DR   RefSeq; WP_015716314.1; NC_014974.1.
DR   AlphaFoldDB; E8PL67; -.
DR   STRING; 743525.TSC_c03940; -.
DR   GeneID; 66944217; -.
DR   KEGG; tsc:TSC_c03940; -.
DR   eggNOG; COG2224; Bacteria.
DR   HOGENOM; CLU_019214_2_0_0; -.
DR   Proteomes; UP000008087; Chromosome.
DR   GO; GO:0004451; F:isocitrate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR006254; Isocitrate_lyase.
DR   InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; TIGR01346; isocit_lyase; 1.
DR   PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR   PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR   Pfam; PF00463; ICL; 2.
DR   PIRSF; PIRSF001362; Isocit_lyase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ADW21031.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         96..98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         196..197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         318..322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   438 AA;  49382 MW;  7F829AE92BA1FCA3 CRC64;
     MDPLSVLTPE MRQEAEELRR DWATNPRWKG VKRDYRPEDV VRLRPSVKVE YTLAKRGAEK
     LWQLLHERPY VHTFGAYTGA MAVEMVRAGL EAIYLSGWQV AADANLAWQT YPDQSLYPYN
     SVPQIVKRIN NALMRADMIE RSEGKVTRDW YVPIVADAEA GFGGALNVFE LTKAMIEAGA
     AGIHYEDQLA SEKKCGHLGG KVLVPTFQHI RTLQAARLAA DIMGVPTVII ARTDAEAATL
     ITSDIDERDR PFILPGERTP EGFYRVKNGL EAGIARALAY APYADVIWME TSKPDLEEAR
     KFAEAVKKEF PDKLLAYNLS PSFNWKKFLD DETIAKFNRE LGEMGYKFQF ITLAGWHTVN
     YYTWELAKGY KTRGMPAFVE LQQKEFLAQA QGFTAVKHQR EVGAGYFDEV VLALTQGEAS
     TLALKGSTEE AQFNEPVH
//
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