ID A0A0D6SR25_9PSED Unreviewed; 531 AA.
AC A0A0D6SR25;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=SZ55_2572 {ECO:0000313|EMBL:KIV70984.1};
OS Pseudomonas sp. FeS53a.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1604022 {ECO:0000313|EMBL:KIV70984.1, ECO:0000313|Proteomes:UP000032531};
RN [1] {ECO:0000313|EMBL:KIV70984.1, ECO:0000313|Proteomes:UP000032531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FeS53a {ECO:0000313|EMBL:KIV70984.1,
RC ECO:0000313|Proteomes:UP000032531};
RA de Souza R., Sant'Anna F.H., Ambrosini A., Tadra-Sfeir M., Faoro H.,
RA Alvarenga S.M., Pedrosa F.O., Souza E.M., Passaglia L.M.;
RT "Genome of Pseudomonas sp. FeS53a associated with rice cropped in iron-
RT stressed soils.";
RL Submitted (JAN-2015) 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:KIV70984.1}.
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DR EMBL; JYFT01000045; KIV70984.1; -; Genomic_DNA.
DR RefSeq; WP_044406275.1; NZ_JYFT01000045.1.
DR AlphaFoldDB; A0A0D6SR25; -.
DR GeneID; 57397491; -.
DR PATRIC; fig|1604022.3.peg.892; -.
DR Proteomes; UP000032531; 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; 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:KIV70984.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000032531}.
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
SQ SEQUENCE 531 AA; 58915 MW; F2D6FF9DE0FE3585 CRC64;
MSAYQNEIKA VAALKEKYGS SWSAINPEYA ARMRVQNRFK TGLDIAKYTA AIMRKDMAEY
DADSSVYTQS LGCWHGFIGQ QKLISIKKHL KTTNKRYLYL SGWMVAALRS DFGPLPDQSM
HEKTAVAGLI EELYTFLRQA DARELDLLFT ALDAARAAGD KAKEAEVQAQ IDGYETHVVP
IIADIDAGFG NPEATYLLAK KMIEAGACCI QIENQVSDEK QCGHQDGKVT VPHEDFLAKI
NAVRYAFLEL GVDDGVIVAR TDSLGAGLTK QIAVTKQPGD LGDQYNSFLD CEEISAAELK
NGDVVINREG KLLRPKRLPS NLFQFRQGTG EDRCVLDCIT SLQNGADLLW IETEKPHVGQ
IKGMVDRIRQ VIPNAKLVYN NSPSFNWTLN FRQQVFDAFV AEGKDVSAYD RAKLMSVEYD
ETELAQVADE KIRTFQRDGS AHAGIFHHLI TLPTYHTAAL STDNLAKGYF ADEGMLAYVK
GVQRQELRQG IACVKHQNMA GSDIGDNHKE YFAGEAALKA SGKDNTMNQF H
//
