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Database: UniProt
Entry: A0A1I2HIN6_9FLAO
LinkDB: A0A1I2HIN6_9FLAO
Original site: A0A1I2HIN6_9FLAO 
ID   A0A1I2HIN6_9FLAO        Unreviewed;       426 AA.
AC   A0A1I2HIN6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=SAMN04488131_11460 {ECO:0000313|EMBL:SFF30145.1};
OS   Flavobacterium xueshanense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=935223 {ECO:0000313|EMBL:SFF30145.1, ECO:0000313|Proteomes:UP000198596};
RN   [1] {ECO:0000313|EMBL:SFF30145.1, ECO:0000313|Proteomes:UP000198596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9227 {ECO:0000313|EMBL:SFF30145.1,
RC   ECO:0000313|Proteomes:UP000198596};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FONQ01000014; SFF30145.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2HIN6; -.
DR   STRING; 935223.SAMN04488131_11460; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000198596; 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:SFF30145.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT   ACT_SITE        189
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         151
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         190..191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         311..315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   426 AA;  46421 MW;  19F418868589E76E CRC64;
     MKTTETRIQE LVTDWITNPR WNGIERPYSA EEVVKLQGSY QIEHSVARIG ANNLWNKLNA
     QDFVAGLGAL TGNQAIQEVE AGLDAIYLSG WQVAADANVA GEMYPDQSLY PANSVPLVVK
     RINNALLRAD QIQVVNGTAD KKEYLVPIVA DAEAGFGGNL NAFELMKAMI EAGAAGVHFE
     DQLSSAKKCG HLGGKVLVPT QEAINKLIAA RLAADVMGTP TIVVARTDAD AANLLTSDID
     PRDAKFITGE KTGEGFFYVN CGVEQGIDRG LSYAPYADLI WMETSNPDLD YARKFAEGIH
     AKFPGKMLAY NCSPSFNWAA KLSVAEMETF REDLAAMGYK FQFITLAGFH ALNTSMFELS
     KAYKERGMAG YSELQEREFA LQKHGFKAVK HQGFVGTSYF DAVQNTVTVG KSSTTAMKDS
     TEAAQF
//
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