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Database: UniProt
Entry: F3FFS5_PSESX
LinkDB: F3FFS5_PSESX
Original site: F3FFS5_PSESX 
ID   F3FFS5_PSESX            Unreviewed;       230 AA.
AC   F3FFS5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Amidotransferase {ECO:0000313|EMBL:EGH29061.1};
DE   Flags: Fragment;
GN   ORFNames=PSYJA_08790 {ECO:0000313|EMBL:EGH29061.1};
OS   Pseudomonas syringae pv. japonica str. M301072.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=629262 {ECO:0000313|EMBL:EGH29061.1, ECO:0000313|Proteomes:UP000004471};
RN   [1] {ECO:0000313|EMBL:EGH29061.1, ECO:0000313|Proteomes:UP000004471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M301072PT {ECO:0000313|Proteomes:UP000004471};
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:EGH29061.1}.
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DR   EMBL; AEAH01000390; EGH29061.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3FFS5; -.
DR   HOGENOM; CLU_054974_0_2_6; -.
DR   Proteomes; UP000004471; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01741; GATase1_1; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR044992; ChyE-like.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   PANTHER; PTHR42695; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR   PANTHER; PTHR42695:SF5; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR   Pfam; PF00117; GATase; 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   Transferase {ECO:0000313|EMBL:EGH29061.1}.
FT   DOMAIN          86..191
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        98
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   NON_TER         230
FT                   /evidence="ECO:0000313|EMBL:EGH29061.1"
SQ   SEQUENCE   230 AA;  26016 MW;  3698687777BA98E0 CRC64;
     MSLRICILET DNLRPELVEQ YHGYGRMFEL LFARQPIAAE LTVYNVVQGD YPPADEQFDA
     YLVTGSKADS FGTDPWIQTL KVYLLELYQR GEKLLGICFG HQLLALLLGG RTERAVQGWG
     VGIHHYQLAP ARPWMTPAMD TLTLLISHQD QVTALPENAT VLASSEFCPF AAYHINDQVL
     CFQGHPEFIH DFSRTLLDLR QEALGEQIYQ QGVVSLDHDH HGATVAEWMM
//
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