ID F3G1V5_PSESJ Unreviewed; 286 AA.
AC F3G1V5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:EGH41055.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:EGH41055.1};
GN ORFNames=PSYPI_00905 {ECO:0000313|EMBL:EGH41055.1};
OS Pseudomonas syringae pv. pisi str. 1704B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH41055.1, ECO:0000313|Proteomes:UP000004986};
RN [1] {ECO:0000313|EMBL:EGH41055.1, ECO:0000313|Proteomes:UP000004986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1704B {ECO:0000313|EMBL:EGH41055.1,
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:EGH41055.1}.
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DR EMBL; AEAI01000037; EGH41055.1; -; Genomic_DNA.
DR AlphaFoldDB; F3G1V5; -.
DR PATRIC; fig|629263.4.peg.154; -.
DR HOGENOM; CLU_001031_4_0_6; -.
DR BioCyc; PSYR629263:G11X0-161-MONOMER; -.
DR Proteomes; UP000004986; Unassembled WGS sequence.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000313|EMBL:EGH41055.1}.
FT ACT_SITE 126
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 286 AA; 31462 MW; F14344947F559161 CRC64;
MEEDNPGLTV KLGFDVNEDI AAPYIKTGVR PQVAVLREQG VNGQVEMAAA FDRAGFNAID
VHMSDILAGR VDLNDFKGMV ACGGFSYGDV LGAGEGWAKS ALFNSRARDA FQGFFERSDS
FTLGVCNGCQ MLSNLHELIP GSEFWPHFVR NRSEQFEARV AMVQVQESAS IFLQGMAGSR
MPIAIAHGEG HAEFRNDDAL LEADVSGTVA LRFVDNHGKV TETYPANPNG SPRGIGGMTT
LDGRVTIMMP HPERVFRAVQ NSWRPEDWNE DGAWMRMFRN ARAWVN
//
