ID   ADCS_STRGR              Reviewed;         723 AA.
AC   P32483; Q9EWC1;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 111.
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};
DE   AltName: Full=p-aminobenzoic acid synthase {ECO:0000303|PubMed:8472954};
DE            Short=PABA synthase {ECO:0000303|PubMed:8472954};
GN   Name=pabAB {ECO:0000303|PubMed:8472954};
GN   Synonyms=pab {ECO:0000303|PubMed:8472954};
OS   Streptomyces griseus.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IMRU 3570;
RX   PubMed=8472954; DOI=10.1016/0378-1119(93)90602-y;
RA   Criado L.M., Martin J.F., Gil J.A.;
RT   "The pab gene of Streptomyces griseus, encoding p-aminobenzoic acid
RT   synthase, is located between genes possibly involved in candicidin
RT   biosynthesis.";
RL   Gene 126:135-139(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=IMRU 3570;
RX   PubMed=11782498; DOI=10.1099/00221287-148-1-51;
RA   Campelo A.B., Gil J.A.;
RT   "The candicidin gene cluster from Streptomyces griseus IMRU 3570.";
RL   Microbiology 148:51-59(2002).
CC   -!- FUNCTION: Involved in candicidin biosynthesis (PubMed:11782498).
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:11782498}.
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:11782498};
CC   -!- PATHWAY: Antibiotic biosynthesis; candicidin biosynthesis.
CC       {ECO:0000269|PubMed:11782498}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene abolishes production of
CC       candicidin. {ECO:0000269|PubMed:11782498}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC       synthase component I family. {ECO:0000305}.
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DR   EMBL; M93058; AAA72111.1; -; Unassigned_DNA.
DR   EMBL; AJ300302; CAC22117.1; -; Genomic_DNA.
DR   PIR; JN0531; JN0531.
DR   AlphaFoldDB; P32483; -.
DR   SMR; P32483; -.
DR   MEROPS; C26.A25; -.
DR   BioCyc; MetaCyc:MONOMER-16235; -.
DR   UniPathway; UPA00101; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0046820; F:aminodeoxychorismate synthase activity; ISS:UniProtKB.
DR   GO; GO:0008153; P:4-aminobenzoate biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro.
DR   GO; GO:0000162; P:L-tryptophan biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   FunFam; 3.40.50.880:FF:000003; Anthranilate synthase component II; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR   InterPro; IPR005802; ADC_synth_comp_1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR015890; Anth_synth-like_dom.
DR   InterPro; IPR019999; Anth_synth_I-like.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   NCBIfam; TIGR00553; pabB; 1.
DR   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF18; AMINODEOXYCHORISMATE SYNTHASE; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF56322; ADC synthase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Glutamine amidotransferase;
KW   Multifunctional enzyme; Transferase.
FT   CHAIN           1..723
FT                   /note="Aminodeoxychorismate synthase"
FT                   /id="PRO_0000154141"
FT   DOMAIN          2..195
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   REGION          96..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..723
FT                   /note="PABB component"
FT                   /evidence="ECO:0000305"
FT   REGION          693..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..704
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   CONFLICT        698
FT                   /note="R -> A (in Ref. 2; CAC22117)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   723 AA;  77901 MW;  1251547F82DA100F CRC64;
     MRTLLVDNYD SFTYNLFHYL SRANGREPEV IRNDDPAWRP GLLDAFDNVV LSPGPGTPHR
     PADFGLCARI AEEGRLPVLG VCLGHQGMAL AHGARVGRAP EPRHGRTSAV RHDGTGLFEG
     LPQPLEVVRY HSLAVTELPP ELEATAWSED GVLMALRHRT LPLWGVQFHP ESIGTQDGHR
     LLANFRDLTE RHGRTRHGGR AGHGTLPPPA PARETKATTG TPRRLRVIAK SLPTRWDAEV
     AFDSLFRTGD HPFWLDSSRP GGELGQLSMM GDASGPLART AKADVHAGTV TVRADGASST
     VESAFLTWLE NDLAGLRTEV PELPFAFALG WVGCLGYELK AECDGDAAHR SPDPDAVLVF
     ADRALVLDHR TRTTYLLALV EDDAEAEARA WLAAASATLD AVAGREPEPC PEAPVCTTGP
     VELRHDRDGY LKLIDVCQQE IAAGETYEVC LTNMAEADTD LTPWAAYRAL RRVSPAPFAA
     FLDFGPMAVL SSSPERFLRI DRHGRMESKP IKGTRPRGAT PQEDAALVRA LATCEKDRAE
     NLMIVDLVRH DLGRCAEVGS VVADPVFQVE TYATVHQLVS TVTARLREDS SPVAAVRAAF
     PGGSMTGAPK IRTMQIIDRL EGGPRGVYSG AIGYFSLTGA VDLSIVIRTV VLSGGRLRYG
     VGGAVIALSD PADEFEETAV KAAPLLRLLD TAFPGRERPG KDLDGEPDDG TDAGAPKDLV
     LPG
//