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
//