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Database: UniProt
Entry: Q88A05_PSESM
LinkDB: Q88A05_PSESM
Original site: Q88A05_PSESM 
ID   Q88A05_PSESM            Unreviewed;       199 AA.
AC   Q88A05;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 126.
DE   SubName: Full=Anthranilate synthase, component II {ECO:0000313|EMBL:AAO54134.1};
GN   Name=trpG {ECO:0000313|EMBL:AAO54134.1};
GN   OrderedLocusNames=PSPTO_0592 {ECO:0000313|EMBL:AAO54134.1};
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO54134.1, ECO:0000313|Proteomes:UP000002515};
RN   [1] {ECO:0000313|EMBL:AAO54134.1, ECO:0000313|Proteomes:UP000002515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515};
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.,
RA   Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B.,
RA   Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V.,
RA   D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S.,
RA   Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B.,
RA   Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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DR   EMBL; AE016853; AAO54134.1; -; Genomic_DNA.
DR   RefSeq; NP_790439.1; NC_004578.1.
DR   RefSeq; WP_005767895.1; NC_004578.1.
DR   AlphaFoldDB; Q88A05; -.
DR   STRING; 223283.PSPTO_0592; -.
DR   MEROPS; C26.955; -.
DR   GeneID; 1182203; -.
DR   KEGG; pst:PSPTO_0592; -.
DR   PATRIC; fig|223283.9.peg.597; -.
DR   eggNOG; COG0512; Bacteria.
DR   HOGENOM; CLU_014340_1_2_6; -.
DR   OMA; TEHGHAM; -.
DR   OrthoDB; 9786812at2; -.
DR   PhylomeDB; Q88A05; -.
DR   Proteomes; UP000002515; Chromosome.
DR   GO; GO:0004049; F:anthranilate synthase activity; ISS:JCVI.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; ISS:JCVI.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
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   Reference proteome {ECO:0000313|Proteomes:UP000002515}.
FT   DOMAIN          3..191
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        79
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   199 AA;  21646 MW;  913D5157544F20C7 CRC64;
     MLLMIDNYDS FTYNVVQYLG ELGADVKVIR NDELTIAQIE ALNPERIVVS PGPCTPNEAG
     VSLEVIKHFA GKLPILGVCL GHQSIGQAFG GDVVRARQVM HGKTSPVVHE DGGVFAGLNH
     PLVVTRYHSL VVKSDTLPEC LEVTAWTALE DGSVDEIMGL RHKTLNVEGV QFHPESILTE
     QGHELFANFL KQSGGHRQG
//
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