ID   PHZB_PSECL              Reviewed;         637 AA.
AC   Q51519;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Anthranilate synthase, phenazine specific;
DE            EC=4.1.3.27;
DE   Includes:
DE     RecName: Full=Glutamine amidotransferase;
GN   Name=phzB;
OS   Pseudomonas chlororaphis (Pseudomonas aureofaciens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=30-84;
RX   PubMed=8586283; DOI=10.1111/j.1574-6968.1995.tb07954.x;
RA   Pierson L.S. III, Gaffney T., Lam S., Gong F.;
RT   "Molecular analysis of genes encoding phenazine biosynthesis in the
RT   biological control bacterium. Pseudomonas aureofaciens 30-84.";
RL   FEMS Microbiol. Lett. 134:299-307(1995).
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; L48339; AAB00330.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q51519; -.
DR   SMR; Q51519; -.
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_0000056907"
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;  69878 MW;  23ECC15C1455D2C7 CRC64;
     MSQTAAHLME RILQPAPEPF ALLYRPESSG PGLLDVLIGE MSEPQVLADI DLPATSIGAP
     RLDVLALIPY RQIAERGFEA VDDESPLLAM NITEQQSISI ERLLGMLPNV PIQLNSERFD
     LSDASYAEIV SQVIANEIGS GEGANFVIKR TFLAEISEYG PASALSFFRH LLEREKGAYW
     TFIIHTGSRT FVGASPERHI SIKDGLSVMN PISGTYRYPP AGPNLSEVMD FLADRKEADE
     LYMVVDEELK MMARICEDGG HVLGPYLKEM AHLAHTEYFI EGKTHRDVRE ILRETLFAPT
     VTGSPLESAC RVIQRYEPQG RAYYSGMAAL IGSDGKGGRS LDSAILIRTA DIDNSGEVRI
     SVGSTIVRHS DPMTEAAESR AKATGLISAL KNQAPSRFGN HLQVRAALAS RNAYVSDFWL
     MDSQQREQIQ ADFSGRQVLI VDAEDTFTSM IAKQLRALGL VVTVCSFSDE YSFEGYDLVI
     MGPGPGNPSE VQQPKINHLH VAIRSLLSQQ RPFLAVCLSH QVLSLCLGLE LQRKAIPNQG
     VQKQIDLFGN VERVGFYNTF AAQSSSDRLD IDGIGTVEIS RDSETGEVHA LRGPSFASMQ
     FHAESLLTQE GPRIIADLLR HALIHTPVEN NASAAGR