ID E1VQB1_9GAMM Unreviewed; 531 AA.
AC E1VQB1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=HDN1F_34200 {ECO:0000313|EMBL:CBL47003.1};
OS gamma proteobacterium HdN1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL47003.1, ECO:0000313|Proteomes:UP000002677};
RN [1] {ECO:0000313|EMBL:CBL47003.1, ECO:0000313|Proteomes:UP000002677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT "Alkane degradation by a new type of denitrifying bacterium with possible
RT involvement of the electron acceptor in substrate activation.";
RL Environ. Microbiol. 0:0-0(2010).
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; FP929140; CBL47003.1; -; Genomic_DNA.
DR AlphaFoldDB; E1VQB1; -.
DR STRING; 83406.HDN1F_34200; -.
DR KEGG; gpb:HDN1F_34200; -.
DR eggNOG; COG2224; Bacteria.
DR HOGENOM; CLU_038243_0_0_6; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000002677; 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; 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:CBL47003.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000002677}.
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; 59244 MW; 81BC3F5D87885C5E CRC64;
MSNFSQIADQ AATEISAFGP SWASINPENV ARMRLQNRFR TGLDIAKYTA KIMRADMAAY
DKDSSQYTQS LGCWHGFVGQ QKMIAVKKHH GTTKRRYLYL SGWMVAALRS EFGPLPDQSM
HEKTVVANLI EELYTFLRQA DARELGGLFR ELDAARSAGD KAKEAEILNK VENFETHVVP
IIADIDAGFG NAEATYLLAK RMIEAGACAI QIENQVSDEK QCGHQDGKVT VPHEDFLAKI
RAVRYAFMEM GVEDGIIVAR TDSLGAGLTK QIAFTRKPGD LGDQYNSFLD CEEVTPESMK
NGDVIINRNG KLLRPKRLPS NLFQFRKGSG EDRCVLDCIT SLQNGADLLW IETEKPHVSQ
IKGMVDRIRE VIPNAKLVYN NSPSFNWTLN FRQQVYDAWQ QAGKDVSAFD RAKLMSVDYD
STELAAEADR RIQSFQKDAA AQAGIFHHLI TLPTYHTTAL STDNLAKGYF GEEGMLAYVY
NVQRKEIRQG IACVKHQNMA GSDIGDDHKE YFAGESALLA GGKDNTMNQF S
//
