ID   PHZE_PSEFL              Reviewed;         637 AA.
AC   Q51791;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Anthranilate synthase, phenazine specific;
DE            EC=4.1.3.27;
DE   Includes:
DE     RecName: Full=Glutamine amidotransferase;
GN   Name=phzE;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL B-15132 / 2-79;
RX   PubMed=9573209; DOI=10.1128/jb.180.9.2541-2548.1998;
RA   Mavrodi D.V., Ksenzenko V.N., Bonsall R.F., Cook R.J., Boronin A.M.,
RA   Thomashow L.S.;
RT   "A seven-gene locus for synthesis of phenazine-1-carboxylic acid by
RT   Pseudomonas fluorescens 2-79.";
RL   J. Bacteriol. 180:2541-2548(1998).
CC   -!- FUNCTION: Involved in the biosynthesis of the antibiotic, phenazine, a
CC       nitrogen-containing heterocyclic molecule having important roles in
CC       virulence, competition and biological control.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC         pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58359; EC=4.1.3.27;
CC   -!- PATHWAY: Antibiotic biosynthesis; phenazine biosynthesis.
CC   -!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
CC       using ammonia rather than glutamine, whereas component II provides
CC       glutamine amidotransferase activity.
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DR   EMBL; L48616; AAC18904.1; -; Genomic_DNA.
DR   RefSeq; WP_043050174.1; NZ_JXCQ01000041.1.
DR   AlphaFoldDB; Q51791; -.
DR   SMR; Q51791; -.
DR   PRIDE; Q51791; -.
DR   KEGG; ag:AAC18904; -.
DR   BioCyc; MetaCyc:MON-13690; -.
DR   UniPathway; UPA00099; -.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0002047; P:phenazine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.60.120.10; -; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR019999; Anth_synth_I-like.
DR   InterPro; IPR015890; Chorismate_C.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   PANTHER; PTHR11236; PTHR11236; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF56322; SSF56322; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Antibiotic biosynthesis; Glutamine amidotransferase; Lyase; Transferase;
KW   Virulence.
FT   CHAIN           1..637
FT                   /note="Anthranilate synthase, phenazine specific"
FT                   /id="PRO_0000056908"
FT   DOMAIN          437..628
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   REGION          1..434
FT                   /note="Anthranilate synthase component I"
FT   ACT_SITE        517
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        602
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        604
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   637 AA;  69873 MW;  D65235CA6139E0FE CRC64;
     MSQAAARLME RILQPVPEPF ALLYRPESSG PGLLNVLIGE MSQPQVLADI DLPAPSIGAP
     RLDVLTLIPY CQIAERGFAA VDDQSPLLAM NITEQQTISI EQMLALLPNV PIQLNNERFD
     LSDASYAEIV SQVIANEIGS GEGANFVIKR TFLAEISEYQ PASALSFFRH LLEREKGVYW
     TFIIHTGSRT FVGASPERHI SVKDGLAVMN PISGTYRYPP AGPSLTEVMD FLADRKEADE
     LYMVVDEELK MMARICEDGG HVLGPYLKEM THLAHTEYFI EGRTRRDVRE ILHETLFAPT
     VTGSPLESAC RVIERYEPQG RAYYSGMAAL IGSDGKGGRS LDSAILIRTA DIDNCGQVRI
     SVGSTIVRHS EPLTEAAESR AKAAGLIAAL KNQAASRFGD HLQVRAALAS RNAYVSDFWL
     MNSQQRQQTQ SDFSGRQVLI VDAEDTFTSM IAKQLRALGL VVTVRSFSDE YSFDGYDLVI
     MGPGPGNPSD VQLPKIDHLH VAIRSLLNQQ RPFLAVCLSH QVLSLCLGLE LQRKAIPNQG
     VQKQIDLFGN AERVGFYNTF AARSSSDRLD IDGIGTVEIS RDSETGEVHA LRGPAFASMQ
     FHAESLLTQE GPRIIADLLR HALIHTPVDS SVSAAGR