ID A0A0F5VJA7_9GAMM Unreviewed; 435 AA.
AC A0A0F5VJA7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=KY46_01685 {ECO:0000313|EMBL:KKD01555.1};
OS Photobacterium halotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=265726 {ECO:0000313|EMBL:KKD01555.1, ECO:0000313|Proteomes:UP000033633};
RN [1] {ECO:0000313|EMBL:KKD01555.1, ECO:0000313|Proteomes:UP000033633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MELD1 {ECO:0000313|EMBL:KKD01555.1,
RC ECO:0000313|Proteomes:UP000033633};
RA Mathew D.C., Huang C.-C.;
RT "Mercury Reductase activity and rhizosphere competence traits in the genome
RT of root associated Photobacterium halotolerans MELD1.";
RL Submitted (DEC-2014) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKD01555.1}.
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DR EMBL; JWYV01000001; KKD01555.1; -; Genomic_DNA.
DR RefSeq; WP_046218876.1; NZ_JWYV01000001.1.
DR AlphaFoldDB; A0A0F5VJA7; -.
DR STRING; 265726.KY46_01685; -.
DR PATRIC; fig|265726.11.peg.362; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000033633; Unassembled WGS sequence.
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:KKD01555.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000033633}.
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 93..95
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 197..198
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 233
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 435 AA; 47751 MW; 17F13F934E814684 CRC64;
MTLTRQQQIE AIEKDWAENP RWKHVKRTYT AEEVVNLRGS VVPANTLAQR GADKLWDLVN
GSAKKGYVNC LGALTGGQAV QQAKAGIEAI YLSGWQVAAD NNTASSMYPD QSLYPVDSVP
AVVKRINNSF RRADQIQWAN GKSPEEGGID YFLPIVADAE AGFGGVLNAY ELMRSMIDAG
AAGVHFEDQL ASVKKCGHMG GKVLVPTQEA VQKLIAARLA ADVAGTTTLV IARTDANAAD
LLTSDCDPYD ADFITGERTQ EGFYRVRAGI DQAIARGLAY APYADLIWCE TATPCLEEAR
QFAEAIHAKY PDQLLAYNCS PSFNWEKNLD AETIAKFQQE LSDMGYKYQF ITLAGIHNMW
FNMFELAHAY AQGEGMRHYV EKVQRPEFAA AEKGYTFVAH QQEVGTGYFD KMTNVIQGGN
SSVTALTGST EEDQF
//
