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Database: UniProt
Entry: A0A0S9MV47_9BURK
LinkDB: A0A0S9MV47_9BURK
Original site: A0A0S9MV47_9BURK 
ID   A0A0S9MV47_9BURK        Unreviewed;       443 AA.
AC   A0A0S9MV47;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, 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=ASF44_17545 {ECO:0000313|EMBL:KQP36352.1};
OS   Pseudorhodoferax sp. Leaf274.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP36352.1, ECO:0000313|Proteomes:UP000051759};
RN   [1] {ECO:0000313|EMBL:KQP36352.1, ECO:0000313|Proteomes:UP000051759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf274 {ECO:0000313|EMBL:KQP36352.1,
RC   ECO:0000313|Proteomes:UP000051759};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP36352.1, ECO:0000313|Proteomes:UP000051759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf274 {ECO:0000313|EMBL:KQP36352.1,
RC   ECO:0000313|Proteomes:UP000051759};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQP36352.1}.
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DR   EMBL; LMNA01000029; KQP36352.1; -; Genomic_DNA.
DR   RefSeq; WP_056902313.1; NZ_LMNA01000029.1.
DR   AlphaFoldDB; A0A0S9MV47; -.
DR   STRING; 1736318.ASF44_17545; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000051759; 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:KQP36352.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051759}.
FT   ACT_SITE        203
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         99..101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         165
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         204..205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         325..329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   443 AA;  48673 MW;  F6300B8D386C416F CRC64;
     MPQSLTEQLS RDQQIAALEK DWATNPRWKG VKRGYSAADV VRLRGSLPIE YTLAKRGADK
     LWEKINGGAK KGYVNAFGAI SAGQAMQQAK AGLEAVYLSG WQVAADGNTS ETMYPDQSLY
     AYDSVPTMVR RINNTFKRAD EIQWGRGIEP GNKDFIDYFL PIVADAEAGF GGVLNAFELM
     KNMIAAGAAG VHFEDQLAAV KKCGHMGGKV LVPTHEACEK LIAARFAADV MGVSTIVLAR
     TDAEAANLIT SDHDANDKPF LTGERTQEGF YRVKNGLEQA ISRGVAYAPY ADLVWCETGT
     PDLGFAREFA QAVHAKSPGK LLSYNCSPSF NWRKNLDDKT IAKFQDELSA LGYKYQFITL
     AGIHVNWYNT FKFAHAYARG EGMKHYVEMV QEPEFAAREQ GYTFVSHQQE VGAGYFDDVT
     TVIQGGSSSV KALTGSTEEE QFH
//
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