ID A0A261VT67_9BORD Unreviewed; 440 AA.
AC A0A261VT67;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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 ORFNames=CAL24_15095 {ECO:0000313|EMBL:OZI76453.1};
OS Bordetella genomosp. 2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1983456 {ECO:0000313|EMBL:OZI76453.1, ECO:0000313|Proteomes:UP000215633};
RN [1] {ECO:0000313|EMBL:OZI76453.1, ECO:0000313|Proteomes:UP000215633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU8256 {ECO:0000313|EMBL:OZI76453.1,
RC ECO:0000313|Proteomes:UP000215633};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZI76453.1}.
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DR EMBL; NEVT01000006; OZI76453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261VT67; -.
DR Proteomes; UP000215633; 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; 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:OZI76453.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT REGION 415..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
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 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 194..195
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 315..319
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 440 AA; 48303 MW; 5123DE097D25B36D CRC64;
MSNRETEIRN LQKDWAENTR WQGIKRAYSA EDVIRLRGSV AAEHTLARRG ATRLWELMHS
EPFVNSLGAL TGNQAMQQVK AGLKAIYLSG WQVAGDANLA GEMYPDQSLY PANSVPQVVR
RINNALARCD QIQWMEGKNP GDEGYIDYYA PIVADAEAGF GGVLNAFELM KAMIEAGAAG
VHFEDQLASV KKCGHMGGKV LVPTREAVSK LVSARLAADV MGTPTVLLAR TDADAADLVT
SDIDENDRPF ITGERTVEGF FRTKAGIEQA ISRGLAYAPY ADLIWCETST PNLDYARKFA
EAIHRQFPGK LLAYNCSPSF NWKKNLDDAT VAKFQRELGA MGYKFQFITL AGFHALNYGM
FELAHGYARR QMSAFVELQQ KEFAAAELGF TAVKHQREVG TGYFDAVTQT IEGGQSSTTA
LTGSTEEAQF EHGHQETAAA
//
