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Database: UniProt
Entry: A0A1K1RTL4_9PSEU
LinkDB: A0A1K1RTL4_9PSEU
Original site: A0A1K1RTL4_9PSEU 
ID   A0A1K1RTL4_9PSEU        Unreviewed;       431 AA.
AC   A0A1K1RTL4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=isocitrate lyase {ECO:0000256|ARBA:ARBA00012909};
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=SAMN04489730_3956 {ECO:0000313|EMBL:SFW75603.1};
OS   Amycolatopsis australiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=546364 {ECO:0000313|EMBL:SFW75603.1, ECO:0000313|Proteomes:UP000182740};
RN   [1] {ECO:0000313|EMBL:SFW75603.1, ECO:0000313|Proteomes:UP000182740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44671 {ECO:0000313|EMBL:SFW75603.1,
RC   ECO:0000313|Proteomes:UP000182740};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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};
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DR   EMBL; FPJG01000006; SFW75603.1; -; Genomic_DNA.
DR   RefSeq; WP_072477673.1; NZ_FPJG01000006.1.
DR   AlphaFoldDB; A0A1K1RTL4; -.
DR   STRING; 546364.SAMN04489730_3956; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000182740; 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:SFW75603.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT   ACT_SITE        194
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         156
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         195..196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         316..320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   431 AA;  47281 MW;  FC816A30667BD940 CRC64;
     MTVTAAPPRE AAAAELARSW AEDSRWRGVR RDYTAEDVLR LRGSVTEEHT LARLGAERLW
     QLLHSEDYVH ALGALTGNQA VQQVRAGLKA IYLSGWQVAA DANLAGHTYP DQSLYPANSV
     PQVVRRINNA LLRADQISWA ENEPDAPHWL APIVADAEAG FGGVLNAFEL MKGMIAGGAA
     GVHWEDQLAA EKKCGHLGGK VLVPTAQHIR TLQAARLAAD VCDVPSLVIA RTDAQAANLI
     TSDVDERDRP FLTGERTAEG YHRVRGGLEP CVARGLAYAP YADLLWMETS KPDLEVARRF
     AEAVKAEYPD QLLAYNCSPS FNWKKHLDDA TIAKFQRELG HMGYKFQFIT LAGFHSLNHA
     MFALARGYAG EGMTAYVELQ EREFAAEAAG YTATRHQREV GTSYFDLVST VVNPSSTTVA
     LIDSTEKSQF Y
//
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