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Database: UniProt
Entry: A0A147GU11_9BURK
LinkDB: A0A147GU11_9BURK
Original site: A0A147GU11_9BURK 
ID   A0A147GU11_9BURK        Unreviewed;       443 AA.
AC   A0A147GU11;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=NS331_12840 {ECO:0000313|EMBL:KTT21086.1};
OS   Pseudacidovorax intermedius.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Pseudacidovorax.
OX   NCBI_TaxID=433924 {ECO:0000313|EMBL:KTT21086.1, ECO:0000313|Proteomes:UP000072741};
RN   [1] {ECO:0000313|EMBL:KTT21086.1, ECO:0000313|Proteomes:UP000072741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NS331 {ECO:0000313|EMBL:KTT21086.1,
RC   ECO:0000313|Proteomes:UP000072741};
RX   PubMed=26793183;
RA   Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA   Patil P.B.;
RT   "Genomic Resource of Rice Seed Associated Bacteria.";
RL   Front. Microbiol. 6:1551-1551(2016).
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:KTT21086.1}.
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DR   EMBL; LDSL01000073; KTT21086.1; -; Genomic_DNA.
DR   RefSeq; WP_058642395.1; NZ_LDSL01000073.1.
DR   AlphaFoldDB; A0A147GU11; -.
DR   PATRIC; fig|433924.3.peg.4624; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000072741; 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; 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:KTT21086.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000072741}.
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;  48701 MW;  308238396C45D791 CRC64;
     MPQAIREQLS RDQQISALEK DWASNPRWKG VKRGYSAADV VRLRGSFPIE YTLAQRGAEK
     LWEKINGGAK KGYVNAFGAI SAGQAMQQAK AGLEAVYLSG WQVAADGNTS ETMYPDQSLY
     AYDSVPTMVR RINNTFKRAD EIQWGRGINP GDQEFVDYFL PIVADAEAGF GGVLNAFELM
     KNMIAAGAAG VHFEDQLAAV KKCGHMGGKV LVPTQEAVEK LIAARFAADV MGVPSIVLAR
     TDAEAANLIT SDHDANDKPF LTGERTQEGF YRVRNGLEQS ISRGVAYAPY ADLVWCETGV
     PDIGFAREFA QAVHAACPGK LLSYNCSPSF NWKKNLNEKQ IASFQEDLSA LGYKFQFITL
     AGIHINWFQT FQFAHAYARG EGMKHYTEMV QEPEFAAREK GYTFVSHQQE VGAGYFDDVT
     TVIQGGSSSV KALTGSTEEE QFH
//
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