ID   ADCS_STRPR              Reviewed;         719 AA.
AC   P72539;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   23-FEB-2022, entry version 93.
DE   RecName: Full=Aminodeoxychorismate synthase {ECO:0000305};
DE            Short=ADC synthase {ECO:0000305};
DE            EC=2.6.1.85 {ECO:0000250|UniProtKB:Q8LPN3};
DE   AltName: Full=4-amino-4-deoxychorismate synthase {ECO:0000305};
GN   Name=papA {ECO:0000303|PubMed:9044253};
OS   Streptomyces pristinaespiralis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=38300;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=SP92;
RX   PubMed=9044253; DOI=10.1046/j.1365-2958.1997.2031574.x;
RA   Blanc V., Gil P., Bamas-Jacques N., Lorenzon S., Zagorec M.,
RA   Schleuniger J., Bisch D., Blanche F., Debussche L., Crouzet J., Thibaut D.;
RT   "Identification and analysis of genes from Streptomyces pristinaespiralis
RT   encoding enzymes involved in the biosynthesis of the 4-dimethylamino-L-
RT   phenylalanine precursor of pristinamycin I.";
RL   Mol. Microbiol. 23:191-202(1997).
CC   -!- FUNCTION: Involved in pristinamycin I biosynthesis (PubMed:9044253).
CC       Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from
CC       chorismate and glutamine (By similarity).
CC       {ECO:0000250|UniProtKB:Q8LPN3, ECO:0000269|PubMed:9044253}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-
CC         glutamate; Xref=Rhea:RHEA:11672, ChEBI:CHEBI:29748,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58406; EC=2.6.1.85;
CC         Evidence={ECO:0000250|UniProtKB:Q8LPN3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11673;
CC         Evidence={ECO:0000305|PubMed:9044253};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:9044253}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene abolishes pristinamycin I
CC       biosynthesis. {ECO:0000269|PubMed:9044253}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC       synthase component I family. {ECO:0000305}.
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DR   EMBL; U60417; AAC44866.1; -; Genomic_DNA.
DR   SMR; P72539; -.
DR   MEROPS; C26.959; -.
DR   GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.60.120.10; -; 1.
DR   InterPro; IPR005802; ADC_synth_comp_1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR019999; Anth_synth_I-like.
DR   InterPro; IPR006805; Anth_synth_I_N.
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; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF56322; SSF56322; 1.
DR   TIGRFAMs; TIGR00553; pabB; 1.
DR   TIGRFAMs; TIGR00566; trpG_papA; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Glutamine amidotransferase; Transferase.
FT   CHAIN           1..719
FT                   /note="Aminodeoxychorismate synthase"
FT                   /id="PRO_0000453960"
FT   DOMAIN          5..199
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   REGION          199..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..224
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   719 AA;  77364 MW;  BFEBFCBDA91D8368 CRC64;
     MRTVRTLLID NYDSFTYNLF QMLAEVNGAA PLVVRNDDTR TWQALAPGDF DNVVVSPGPG
     HPATDTDLGL SRRVITEWDL PLLGVCLGHQ ALCLLAGAAV VHAPEPFHGR TSDIRHDGQG
     LFANIPSPLT VVRYHSLTVR QLPADLRATA HTADGQLMAV AHRHLPRFGV QFHPESISSE
     HGHRMLANFR DLSLRAAGHR PPHTERIPAP APAPAPAPAP APPASAPVGE YRLHVREVAC
     VPDADAAFTA LFADAPARFW LDSSRVEPGL ARFTFLGAPA GPLGEQITYD VADRAVRVKD
     GSGGETRRPG TLFDHLEHEL AARALPATGL PFEFNLGYVG YLGYETKADS GGEDAHRGEL
     PDGAFMFADR MLALDHEQGR AWLLALSSTR RPATAPAAER WLTDAARTLA TTAPRPPFTL
     LPDDQLPALD VHYRHSLPRY RELVEECRRL ITDGETYEVC LTNMLRVPGR IDPLTAYRAL
     RTVSPAPYAA YLQFPGATVL SSSPERFLRI GADGWAESKP IKGTRPRGAG PAQDAAVKAS
     LAAAEKDRSE NLMIVDLVRN DLGQVCDIGS VHVPGLFEVE TYATVHQLVS TVRGRLAADV
     SRPRAVRAAF PGGSMTGAPK VRTMQFIDRL EKGPRGVYSG ALGYFALSGA ADLSIVIRTI
     VATEEAATIG VGGAVVALSD PDDEVREMLL KAQTTLAALR QAHAGATASD RELLAGSLR