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Database: UniProt
Entry: H8KZT4_FRAAD
LinkDB: H8KZT4_FRAAD
Original site: H8KZT4_FRAAD 
ID   H8KZT4_FRAAD            Unreviewed;       434 AA.
AC   H8KZT4;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
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   OrderedLocusNames=Fraau_0095 {ECO:0000313|EMBL:AFC84595.1};
OS   Frateuria aurantia (strain ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 /
OS   NBRC 3245 / NCIMB 13370) (Acetobacter aurantius).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Frateuria.
OX   NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC84595.1, ECO:0000313|Proteomes:UP000005234};
RN   [1] {ECO:0000313|Proteomes:UP000005234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 / NBRC 3245 /
RC   NCIMB 13370 {ECO:0000313|Proteomes:UP000005234};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Frateuria aurantia DSM 6220.";
RL   Submitted (FEB-2012) 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; CP003350; AFC84595.1; -; Genomic_DNA.
DR   RefSeq; WP_014401601.1; NC_017033.1.
DR   AlphaFoldDB; H8KZT4; -.
DR   STRING; 767434.Fraau_0095; -.
DR   KEGG; fau:Fraau_0095; -.
DR   eggNOG; COG2224; Bacteria.
DR   HOGENOM; CLU_019214_2_0_6; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000005234; 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; 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:AFC84595.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005234}.
FT   REGION          410..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         89..91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         189..190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         310..314
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   434 AA;  47532 MW;  54DC1DCF7157237E CRC64;
     MSQIHATAAE LNQAWSTDPR WKGIVRNYSA EDVLRLRGTV HVEHSLARRG AERLWKSLHE
     EDFVNALGAL TGNQAMQQVK AGLKAIYLSG WQVAADANLA GEMYPDQSLY PANSVPQVVK
     RINNTLLRAD QLQHAEGKDG TDWLVPIVAD AEAGFGGVLN AFELMKAMIE AGAAGVHFED
     QLASVKKCGH MGGKVLVPTR EAIDKLTAAR LAADVSGVPT ILVARTDADA ADLLTADIDD
     NDRPFITGER TVEGFFRVRP GVDQAISRGL AYAPYADLLW CETSKPNLED ARKFAEAIHK
     QFPGKLLAYN CSPSFNWRKN LDDATIARFQ KELGAMGYKF QFITLAGFHS LNYGMFDLAY
     GYARHQMSAF VELQEKEFAA AERGFTAVKH QREVGTGYFD AVTQTIQQGQ SSTTALTGST
     EEAQFDHDGT EKAA
//
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