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Database: UniProt
Entry: W0AJG2_9SPHN
LinkDB: W0AJG2_9SPHN
Original site: W0AJG2_9SPHN 
ID   W0AJG2_9SPHN            Unreviewed;       531 AA.
AC   W0AJG2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446};
DE   AltName: Full=Isocitrase {ECO:0000256|ARBA:ARBA00031022};
DE   AltName: Full=Isocitratase {ECO:0000256|ARBA:ARBA00031921};
GN   ORFNames=NX02_24125 {ECO:0000313|EMBL:AHE56433.1};
OS   Sphingomonas sanxanigenens DSM 19645 = NX02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1123269 {ECO:0000313|EMBL:AHE56433.1, ECO:0000313|Proteomes:UP000018851};
RN   [1] {ECO:0000313|EMBL:AHE56433.1, ECO:0000313|Proteomes:UP000018851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NX02 {ECO:0000313|EMBL:AHE56433.1,
RC   ECO:0000313|Proteomes:UP000018851};
RA   Ma T., Huang H., Wu M., Li X., Li G.;
RT   "Completed genome of Sphingomonas sanxanigenens NX02.";
RL   Submitted (JUL-2013) 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; CP006644; AHE56433.1; -; Genomic_DNA.
DR   RefSeq; WP_025294545.1; NZ_CP006644.1.
DR   AlphaFoldDB; W0AJG2; -.
DR   STRING; 1123269.NX02_24125; -.
DR   KEGG; ssan:NX02_24125; -.
DR   PATRIC; fig|1123269.5.peg.4724; -.
DR   eggNOG; COG2224; Bacteria.
DR   HOGENOM; CLU_038243_0_0_5; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000018851; Chromosome.
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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR   PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR   Pfam; PF00463; ICL; 3.
DR   PIRSF; PIRSF001362; Isocit_lyase; 3.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AHE56433.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018851}.
FT   ACT_SITE        221
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
SQ   SEQUENCE   531 AA;  59213 MW;  95966BA63779F68A CRC64;
     MTYQTHIAET GQLIQSHQGT WDGISAEAVA RMRLQNRFRT GLDIARYTAA IMRRDMAAYD
     ADPAAYTQSL GCWHGFIGQQ KMISIKKHFG TTKRRYLYLS GWMIAALRSD FGPLPDQSMH
     EKTSVPALIE ELYTFLRQAD ARELGMMFRE LDAARAAGNR IEEQRLLQAI DNYETHVVPI
     IADIDAGFGN AEATYLLAKK MIEAGACALQ IENQVSDEKQ CGHQDGKVTV PHEDFLAKVR
     ACRYAFLELG VEDGVIVTRT DSLGAGLTKQ IAFSKEPGDL GDQYNAFLDC AEVTDLSTVN
     GDVIINRDGK LMRPKRLPSN LFQFREGTGE DRCVLDCITS LQNGADLLWI ETEKPHIEQI
     ASMVDRIREV IPNAKLVYNN SPSFNWTLNF RQQVFDAWAA EGRDVSAYDR ARLMSVDYDG
     TDLAAEADER IRTFQKDAAA RAGIFHHLIT LPTYHTAALS TDNLAREYFG EAGMLGYVLN
     VQRQEIRQGI ACVKHQNMSG SDIGDDHKEY FAGEAALKAG GAHNTMNQFA A
//
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