ID   PABB_STRLI              Reviewed;         475 AA.
AC   P27630;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   28-JUN-2023, entry version 93.
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   Streptomyces lividans.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=66 / 1326;
RX   PubMed=8472953; DOI=10.1016/0378-1119(93)90601-x;
RA   Arhin F.F., Vining L.C.;
RT   "Organization of the genes encoding p-aminobenzoic acid synthetase from
RT   Streptomyces lividans 1326.";
RL   Gene 126:129-133(1993).
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   -!- MISCELLANEOUS: The catalytically active amino acid residue K274 of the
CC       E.coli enzyme is missing.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC       {ECO:0000305}.
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DR   EMBL; M64859; AAA26798.1; -; Genomic_DNA.
DR   PIR; JN0578; JN0578.
DR   AlphaFoldDB; P27630; -.
DR   SMR; P27630; -.
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; Anthranilate synthase; 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; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF41; AMINODEOXYCHORISMATE SYNTHASE COMPONENT 1; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; ADC synthase; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis; Magnesium; Transferase.
FT   CHAIN           1..475
FT                   /note="Aminodeoxychorismate synthase component 1"
FT                   /id="PRO_0000154140"
SQ   SEQUENCE   475 AA;  52042 MW;  978A05EB35F2BEB3 CRC64;
     MASCRMGARS ALEPCQVDCL DEAADERCAE TPRCHAELLE SVTGASRMSR YSIIVLDPIG
     TIRAAEALTA LVDADDVIFK DEDPLKGIRS VFELGDLDPT NHEEIEFQGG ALGRFAYDIA
     RRLEAIRDLG DRELAGPDAG TALYDLILYD HQDDVIWILV PNEAGEQDPS EDFRDLVNAW
     SYDDEFDIGA EFGANYTDDA YADGVDRLKD YLGSGDMYQV NLAQRRVGMI SAEDYQLYIR
     LRDANPAPYM AYLDIDEGLL VASPERIILD EASDLDTRPI AGTLRGRPRA GGDDEDDGRA
     IDLLRVDKDR AERIMIVDLD RNDIARVGVG GSVKVREIMG LERYSGVMHL VSQVTGDLQE
     AIEAVDLIRA GFPGGTLTGA PKVRTMEIID ELEPQRRAAY CGSIGYIAYK GNIDFKIAIP
     TLYALAGQLF CQAGGGVVGD SVPDGEYRES FEKGNALIRG LEIRHGAVVA QSEDK
//