ID   A0A363UPS7_9GAMM        Unreviewed;       531 AA.
AC   A0A363UPS7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=DEH80_02760 {ECO:0000313|EMBL:PWN57429.1};
OS   Abyssibacter profundi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC   Salinisphaeraceae; Abyssibacter.
OX   NCBI_TaxID=2182787 {ECO:0000313|EMBL:PWN57429.1, ECO:0000313|Proteomes:UP000251800};
RN   [1] {ECO:0000313|EMBL:PWN57429.1, ECO:0000313|Proteomes:UP000251800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUC007 {ECO:0000313|EMBL:PWN57429.1,
RC   ECO:0000313|Proteomes:UP000251800};
RA   Zhou S.;
RT   "Abyssibacter profundi OUC007T gen. nov., sp. nov, a marine bacterium
RT   isolated from seawater of the Mariana Trench.";
RL   Submitted (MAY-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   -!- 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:PWN57429.1}.
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DR   EMBL; QEQK01000002; PWN57429.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A363UPS7; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000251800; 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; 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:PWN57429.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000251800}.
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         380..384
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         451
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   531 AA;  59277 MW;  26F9388E390B125A CRC64;
     MSQYKDEIAA IQRVKDAAGS PWDEINAESA ARMRIQNRFK TGLEIAQYTA DIMRRDMAEF
     DKDKTKYTQS LGCWHGFVGQ QKLISIKKHF GTTDKKYLYL SGWMVAALRS EFGPLPDQSM
     HEKTAVASLV EELYTFLRQA DARELGMLFR ELDKAREAGD AAKEAEIQDA IDNYETHVVP
     IIADIDAGFG NAEATYLLAK QMIEAGACAL QIENQVADEK QCGHQDGKVT VPHEDFHAKI
     RALRYAFLEL GIDNGIIVAR TDSEGAGLTK EIAVVNEPGD QGDRYNSYLD CEEIDVSEMA
     EGDVCINRDG KLLRPKRLAS GLYQFREGTG PERCVFDSVE ALRAGADLIW IETATPSVAD
     IKAMMDGVRK EIPDAKLVYN NSPSFNWTLN FRKQAYDRWV EEGKDVSGYD RDDLMNAKYD
     DSELAADADA KVRSFQEDCS REANIFHHLI TLPTYHTTAL SVDNLAKEYF GDQGMLGYVA
     GVQRKEIRQG IACVKHQNMS GSDIGDDHKE YFAGDRALKA GGAKNTSNQF N
//