ID A0A3S8YQC0_9GAMM Unreviewed; 532 AA. AC A0A3S8YQC0; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 24-JAN-2024, entry version 18. DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446}; DE AltName: Full=Isocitrase {ECO:0000256|ARBA:ARBA00031022}; DE AltName: Full=Isocitratase {ECO:0000256|ARBA:ARBA00031921}; GN ORFNames=EI420_05715 {ECO:0000313|EMBL:AZM95221.1}; OS Halomonas venusta. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=44935 {ECO:0000313|EMBL:AZM95221.1, ECO:0000313|Proteomes:UP000275808}; RN [1] {ECO:0000313|EMBL:AZM95221.1, ECO:0000313|Proteomes:UP000275808} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MA-ZP17-13 {ECO:0000313|EMBL:AZM95221.1, RC ECO:0000313|Proteomes:UP000275808}; RA Li G.; RT "Halomonas venusta MA-ZP17-13."; RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP034367; AZM95221.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3S8YQC0; -. DR KEGG; hvn:EI420_05715; -. DR OrthoDB; 8629576at2; -. DR Proteomes; UP000275808; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf. DR PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1. DR PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1. DR Pfam; PF00463; ICL; 3. DR PIRSF; PIRSF001362; Isocit_lyase; 3. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. PE 4: Predicted; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AZM95221.1}; KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}. FT ACT_SITE 222 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1" FT BINDING 101..103 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2" FT BINDING 184 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3" FT BINDING 223..224 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2" FT BINDING 260 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2" FT BINDING 381..385 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2" FT BINDING 452 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2" SQ SEQUENCE 532 AA; 59103 MW; 4CE56DA38A1ED81D CRC64; MSGLLDDIKA MAQLREAQGG KWEAIKPEYA ARMRAQNRFH TGLDIARYTA KIMRDDMAAY DADTSKYTQS LGCWHGFIGQ QKLISIKKHF GTTKRSYLYL SGWMVAALRS EFGPLPDQSM HEKTSVADLI EELYTFLKQA DAWELNHLFR ALDDAKEAGD SAKEQELISK IDNYETHIVP IIADIDAGFG NAEATYLLAK KFIQAGACCI QLENQVSDEK QCGHQDGKVT VPHEDFLAKI NAVRYAFLEL GIEDGVIVAR TDSLGAGLTQ KIAVTNEPGD LGDQYNSFLD GDVIENASDI NNGDVVIKQN GQLVKPKRLA SGLYQFKPGT GEDRVVLDCI TSLQNGADLL WIETEKPHVG QIASMVNRIR AVVPDAKLVY NNSPSFNWTL NFRQQVFDAW EKEGKDVSAY QRDKLMGVEY DNTELGQLAD EWTRNFQRDG AREAGIFHHL ITLPTYHTAA LSTDNLAKGY FGDEGMLAYV AGVQRQEIRQ GIATVKHQDM AGSNIGDDHK EFFHGDAALK AGGKDNTMNQ FG //