ID   A0A0M4LPJ7_9GAMM        Unreviewed;       435 AA.
AC   A0A0M4LPJ7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446};
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   ORFNames=W908_04120 {ECO:0000313|EMBL:ALE01834.1};
OS   Candidatus Pseudothioglobus singularis PS1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Pseudothioglobus.
OX   NCBI_TaxID=1125411 {ECO:0000313|EMBL:ALE01834.1, ECO:0000313|Proteomes:UP000068905};
RN   [1] {ECO:0000313|EMBL:ALE01834.1, ECO:0000313|Proteomes:UP000068905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PS1 {ECO:0000313|EMBL:ALE01834.1,
RC   ECO:0000313|Proteomes:UP000068905};
RX   PubMed=26494659;
RA   Marshall K.T., Morris R.M.;
RT   "Genome Sequence of 'Candidatus Thioglobus singularis' Strain PS1, a
RT   Mixotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL   Genome Announc. 3:e01155-e01115(2015).
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; CP006911; ALE01834.1; -; Genomic_DNA.
DR   RefSeq; WP_020025409.1; NZ_CP006911.1.
DR   AlphaFoldDB; A0A0M4LPJ7; -.
DR   STRING; 1125411.W908_04120; -.
DR   KEGG; tsn:W908_04120; -.
DR   PATRIC; fig|1125411.7.peg.806; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000068905; 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; 2.
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:ALE01834.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068905}.
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         91..93
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         317..321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         351
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   435 AA;  48040 MW;  E515043BCAB552F3 CRC64;
     MNRKEQIKAL EKDWQDNPRW SNVKRTYSAE DVVRLRGSVQ PECTYARRGA EKLWDLVNGS
     SKKGYVNCMG AITAGQAMQQ AKAGIEAIYL SGWQVAADGN TSETMYPDQS LYAYDSVPTM
     VRRINNTFKR ADEIQWSQGI DPSDDKYIDF FLPIVADAEA GFGGVLNSFE LMKNMIANGA
     AGAHFEDQLA AVKKCGHMGG KVLVPTQEAV QKLISARLAS DVMGVPTLLL ARTDAEAANL
     LTSDVDPHDA AFITGKRTAE GFYVVKNGLE QSISRGVAYA PYADLVWCET GKPDLGFARE
     FAEAVLAENP GQLLAYNCSP SFNWKKNLND SQIASFQEKI SEMGYKYQFI TLAGIHNMWY
     NMFDLAYEYA KGEGMKHYVE KVQEPEFNAA KKGYTFASHQ QEVGAGYFDD VTTVIQGGES
     SVTALKGSTE EEQFS
//