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Database: UniProt
Entry: F3GR88_PSESJ
LinkDB: F3GR88_PSESJ
Original site: F3GR88_PSESJ 
ID   F3GR88_PSESJ            Unreviewed;        42 AA.
AC   F3GR88;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Ketol-acid reductoisomerase {ECO:0000313|EMBL:EGH49591.1};
DE            EC=1.1.1.86 {ECO:0000313|EMBL:EGH49591.1};
DE   Flags: Fragment;
GN   ORFNames=PSYPI_47291 {ECO:0000313|EMBL:EGH49591.1};
OS   Pseudomonas syringae pv. pisi str. 1704B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH49591.1, ECO:0000313|Proteomes:UP000004986};
RN   [1] {ECO:0000313|EMBL:EGH49591.1, ECO:0000313|Proteomes:UP000004986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1704B {ECO:0000313|EMBL:EGH49591.1,
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:EGH49591.1}.
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DR   EMBL; AEAI01004460; EGH49591.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3GR88; -.
DR   HOGENOM; CLU_3262654_0_0_6; -.
DR   Proteomes; UP000004986; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013116; KARI_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF07991; IlvN; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:EGH49591.1};
KW   Oxidoreductase {ECO:0000313|EMBL:EGH49591.1}.
FT   DOMAIN          1..36
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000259|Pfam:PF07991"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGH49591.1"
FT   NON_TER         42
FT                   /evidence="ECO:0000313|EMBL:EGH49591.1"
SQ   SEQUENCE   42 AA;  4067 MW;  B061E61DE98EA88E CRC64;
     EFVKGGGIPD LIAVYQDASG NAKNVALSYA SGVGGGLPAS SK
//
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