ID A0A0Q4FF23_9SPHN Unreviewed; 531 AA.
AC A0A0Q4FF23;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=ASE75_12795 {ECO:0000313|EMBL:KQM63333.1};
OS Sphingomonas sp. Leaf17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735683 {ECO:0000313|EMBL:KQM63333.1, ECO:0000313|Proteomes:UP000051777};
RN [1] {ECO:0000313|EMBL:KQM63333.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM63333.1,
RC ECO:0000313|Proteomes:UP000051777};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM63333.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM63333.1,
RC ECO:0000313|Proteomes:UP000051777};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQM63333.1}.
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DR EMBL; LMKL01000008; KQM63333.1; -; Genomic_DNA.
DR RefSeq; WP_055934206.1; NZ_LMKL01000008.1.
DR AlphaFoldDB; A0A0Q4FF23; -.
DR STRING; 1735683.ASE75_12795; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000051777; 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:KQM63333.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000051777}.
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
SQ SEQUENCE 531 AA; 58741 MW; 6D05B128A9B3F5C3 CRC64;
MTYQTHIARI DTLIRDHAGT WDGISAESVA RMRLQNRFAT GLDIARYTAK IMRADMAAYD
ADPARYTQSL GCWHGFIGQQ KMIAIKKHFG STQGRYLYLS GWMIAALRSE FGPLPDQSMH
EKTSVPALIA ELYTFLRQAD ARELGMLFRE VDAARAAGNS IEEQRLLNAI ENHQTHVVPI
IADIDAGFGN AEATYLLARK MIEAGACALQ IENQVSDEKQ CGHQDGKVTV PHEDFLAKVR
ACRYAFLELG VEDGIIVTRT DSLGAGLTKQ IAVSKTPGDI GDQYNGFLDC EEIDPATARN
GDVILNRDGK LLRPKRLPSN LFQFRAGTGE DRCVLDCITS LQNGADLLWI ETEKPHIEQI
AGMVDRIRAV VPNAKLVYNN SPSFNWTLNF RQQVYDAWVD AGQDVSAYDR ARLMSAEYDE
TPLGAQADER IRTFQSDSAK RAGIFHHLIT LPTYHTAALS TDNLAKAYFG DAGMLGYVKG
VQRKEIREGI ACVRHQNMSG SDIGDDHKDY FAGEAALKAG GAHNTMNQFA A
//
