ID   PABB_KLEAE              Reviewed;         451 AA.
AC   P12679;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Aminodeoxychorismate synthase component 1;
DE            Short=ADC synthase;
DE            Short=ADCS;
DE            EC=2.6.1.85;
DE   AltName: Full=4-amino-4-deoxychorismate synthase component 1;
GN   Name=pabB;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3057324; DOI=10.1093/oxfordjournals.molbev.a040512;
RA   Goncharoff P., Nichols B.P.;
RT   "Evolution of aminobenzoate synthases: nucleotide sequences of Salmonella
RT   typhimurium and Klebsiella aerogenes pabB.";
RL   Mol. Biol. Evol. 5:531-548(1988).
CC   -!- FUNCTION: Part of a heterodimeric complex that catalyzes the two-step
CC       biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-
CC       aminobenzoate (PABA) and tetrahydrofolate. In the first step, a
CC       glutamine amidotransferase (PabA) generates ammonia as a substrate
CC       that, along with chorismate, is used in the second step, catalyzed by
CC       aminodeoxychorismate synthase (PabB) to produce ADC (By similarity).
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC       aminobenzoate from chorismate: step 1/2.
CC   -!- SUBUNIT: Monomer. Heterodimer consisting of two non-identical subunits:
CC       a glutamine amidotransferase subunit (PabA) and a aminodeoxychorismate
CC       synthase subunit (PabB) (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC       {ECO:0000305}.
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DR   EMBL; M22078; AAA88207.1; -; Genomic_DNA.
DR   AlphaFoldDB; P12679; -.
DR   SMR; P12679; -.
DR   UniPathway; UPA00077; UER00149.
DR   GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; ISS:UniProtKB.
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   PANTHER; PTHR11236; PTHR11236; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; SSF56322; 1.
DR   TIGRFAMs; TIGR00553; pabB; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis; Magnesium; Transferase.
FT   CHAIN           1..451
FT                   /note="Aminodeoxychorismate synthase component 1"
FT                   /id="PRO_0000154137"
FT   ACT_SITE        256
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        272
FT                   /note="N6-(4-deoxychorismate)-lysine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         34
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..44
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250"
FT   BINDING         238..240
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   451 AA;  50363 MW;  952C6887158E228C CRC64;
     MLSPAMISLP WRPDAAEYYF SPLSSQPWAM LLHSGFAEHA HNRFDIIVAQ PRATLVTHGQ
     LTTLREGETV STSAADPLTL VHQQLAHCNL QPQPHPHLPF LGGALGLFGY DLGRRFEHLP
     ARADADIELP DMAVGIYDWA LIVDHQRREV SLFSYDDPQA RLAWLEAQTA PVAATFTLTS
     AWRANMSREE YGEKFRQIQA YLHSGDCYQV NLAQRFTATY RGDEWQAFRQ LNRANRAPFS
     AFIRLDEGAV LSLSPERFIQ LRQGDIQTRP IKGTLPRLAD PEQDALQQQK LANSPKDRAE
     NLMIVDLMRN DIGRVAEPGS VRVPELFVVE PFPAVHHLVS TVTARLPAHL HAADLLRAAF
     PGGSITGAPK VRAMEIIDEL EPQRRNAWCG SIGYLSFCGN MDSSITIRTL TAWQGHLYCS
     AGGGIVADSE EAAEYQETFD KVNRILHQLE S