ID F3GEK2_PSESJ Unreviewed; 176 AA.
AC F3GEK2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=2-methylisocitrate lyase {ECO:0000313|EMBL:EGH45502.1};
DE EC=4.1.3.30 {ECO:0000313|EMBL:EGH45502.1};
DE Flags: Fragment;
GN Name=prpB {ECO:0000313|EMBL:EGH45502.1};
GN ORFNames=PSYPI_25594 {ECO:0000313|EMBL:EGH45502.1};
OS Pseudomonas syringae pv. pisi str. 1704B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH45502.1, ECO:0000313|Proteomes:UP000004986};
RN [1] {ECO:0000313|EMBL:EGH45502.1, ECO:0000313|Proteomes:UP000004986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1704B {ECO:0000313|EMBL:EGH45502.1,
RC ECO:0000313|Proteomes:UP000004986};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
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:EGH45502.1}.
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DR EMBL; AEAI01001310; EGH45502.1; -; Genomic_DNA.
DR AlphaFoldDB; F3GEK2; -.
DR HOGENOM; CLU_027389_3_2_6; -.
DR Proteomes; UP000004986; Unassembled WGS sequence.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-EC.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR42905:SF5; CARBOXYVINYL-CARBOXYPHOSPHONATE PHOSPHORYLMUTASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:EGH45502.1}.
FT NON_TER 176
FT /evidence="ECO:0000313|EMBL:EGH45502.1"
SQ SEQUENCE 176 AA; 18590 MW; B9B5F4C900EFBBA9 CRC64;
MSHNNSTPGQ RFRDAVASEQ PLQVVGAINA NHALLARRAG FKAIYLSGGG VAAGSLGIPD
LGITGLEDVL IDVRRITDVC DLPLLVDVDT GFGSSAFNVA RTVRSMIKAG AAAIHIEDQV
GAKRCGHRPN KEIVSQQEMV DRIKAAVDAR TDDSFVIMAR TDALAVEGLE SALERA
//