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Database: UniProt
Entry: A0A165L1B1_9BURK
LinkDB: A0A165L1B1_9BURK
Original site: A0A165L1B1_9BURK 
ID   A0A165L1B1_9BURK        Unreviewed;       443 AA.
AC   A0A165L1B1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-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=A1D30_13390 {ECO:0000313|EMBL:KZT16445.1};
OS   Acidovorax sp. GW101-3H11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1813946 {ECO:0000313|EMBL:KZT16445.1, ECO:0000313|Proteomes:UP000077219};
RN   [1] {ECO:0000313|Proteomes:UP000077219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GW101-3H11 {ECO:0000313|Proteomes:UP000077219};
RA   Ray J., Price M., Deutschbauer A.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KZT16445.1, ECO:0000313|Proteomes:UP000077219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GW101-3H11 {ECO:0000313|EMBL:KZT16445.1,
RC   ECO:0000313|Proteomes:UP000077219};
RX   PubMed=29769716; DOI=10.1038/s41586-018-0124-0;
RA   Price M.N., Wetmore K.M., Waters R.J., Callaghan M., Ray J., Liu H.,
RA   Kuehl J.V., Melnyk R.A., Lamson J.S., Suh Y., Carlson H.K., Esquivel Z.,
RA   Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E., Wall J.D.,
RA   Visel A., Bristow J., Blow M.J., Arkin A.P., Deutschbauer A.M.;
RT   "Mutant phenotypes for thousands of bacterial genes of unknown function.";
RL   Nature 557:503-509(2018).
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:KZT16445.1}.
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DR   EMBL; LUKZ01000009; KZT16445.1; -; Genomic_DNA.
DR   RefSeq; WP_063460702.1; NZ_LUKZ01000009.1.
DR   AlphaFoldDB; A0A165L1B1; -.
DR   STRING; 1813946.A1D30_13390; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000077219; 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:KZT16445.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
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;  48595 MW;  9B866ACD0A725D95 CRC64;
     MPQSLNEQLS REQQIAALEK DWATNPRWKG VKRGYSAADV VRLRGSLPIE HTLAKRGAEK
     LWDKINGGAK KGYVNAFGAI SAGQAMQQAK AGLEAVYLSG WQVAADGNTS ETMYPDQSLY
     AYDSVPTMVR RINNTFKRAD EIQWGRGINP GDKEFIDYFL PIVADAEAGF GGVLNAFELM
     KNMIQSGAAG VHFEDQLAAV KKCGHMGGKV LVPTQEACEK LISARFAADV MGVSTIVLAR
     TDAEAANLIT SDHDANDKPF LTGERTQEGF YRVKNGLEQA ISRGVAYAPY ADLVWCETGV
     PDIGFAREFA QAVHAACPGK LLSYNCSPSF NWKKNLNDKQ IASFQEDLSA LGYKYQFITL
     AGIHINWFNT FQFAHAYANG EGMKHYVNMV QEPEFAARDK GYTFVSHQQE VGAGYFDDVT
     TVIQGGSSSV KALTGSTEEE QFH
//
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