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Database: UniProt
Entry: V4YSY1_9PROT
LinkDB: V4YSY1_9PROT
Original site: V4YSY1_9PROT 
ID   V4YSY1_9PROT            Unreviewed;       438 AA.
AC   V4YSY1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
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   Name=aceA {ECO:0000313|EMBL:ESS14767.1};
GN   ORFNames=MOLA814_00329 {ECO:0000313|EMBL:ESS14767.1};
OS   Betaproteobacteria bacterium MOLA814.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1408164 {ECO:0000313|EMBL:ESS14767.1, ECO:0000313|Proteomes:UP000017838};
RN   [1] {ECO:0000313|EMBL:ESS14767.1, ECO:0000313|Proteomes:UP000017838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MOLA814 {ECO:0000313|EMBL:ESS14767.1,
RC   ECO:0000313|Proteomes:UP000017838};
RX   PubMed=24356832;
RA   Courties A., Riedel T., Jarek M., Intertaglia L., Lebaron P., Suzuki M.T.;
RT   "Genome Sequence of Strain MOLA814, a Proteorhodopsin-Containing
RT   Representative of the Betaproteobacteria Common in the Ocean.";
RL   Genome Announc. 1:e01062-13(2013).
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:ESS14767.1}.
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DR   EMBL; AYMW01000001; ESS14767.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4YSY1; -.
DR   STRING; 1408164.MOLA814_00329; -.
DR   PATRIC; fig|1408164.3.peg.654; -.
DR   eggNOG; COG2224; Bacteria.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000017838; 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; 1.
DR   PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR   PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR   Pfam; PF00463; ICL; 1.
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:ESS14767.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017838}.
FT   ACT_SITE        198
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         94..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         160
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         199..200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         320..324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   438 AA;  47986 MW;  CDB879C3B6679F44 CRC64;
     MVQLTREQQV AALKQDWADN PRWTGVKRNY TAEDVVRLRG SLQPEYTLAK RGAEKLWDKV
     NGGAKKGYVN AFGAISAGQA MQQAKAGLEA VYLSGWQVAA DGNTSETMYP DQSLYAYDSV
     PAMVRRINNT FKRADEIQWA RGINPGDGEF IDYFLPIVAD AEAGFGGVLN AFELMKNMIS
     AGAAGVHFED QLAAVKKCGH MGGKVLVPTK EAIEKLNAAR FAADVMGVST IVLARTDAEA
     ANLITSDHDD NDKPFLTGER TPEGFYRVRN GMEQAISRGV AYAPHADLVW CETGVPDIGF
     AREFAQAVHA ACPGKLLSYN CSPSFNWKKN LNDSQIATFQ EDLAALGYKY QFITLAGIHI
     NWFNTFKFAK AYAGGEGMKH YTEMVQEPEF AAREDGYTFV SHQQEVGAGY FDEVTTVIQG
     GASSVRALTG STEEEQFH
//
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