ID   PABB_LACLL              Reviewed;         470 AA.
AC   P27629;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 92.
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   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11454 / DSM 20729 / LMG 7930 / NCDO 496 / NCIMB 8586 / Berridge
RC   X 13;
RX   PubMed=8409921; DOI=10.1099/00221287-139-8-1785;
RA   Arhin F.F., Vining L.C.;
RT   "Cloning, nucleotide sequence and expression in Streptomyces lividans and
RT   Escherichia coli of pabB from Lactococcus lactis subsp. lactis NCDO 496.";
RL   J. Gen. Microbiol. 139:1785-1793(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; M64860; AAA17025.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P27629; -.
DR   SMR; P27629; -.
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; IPR005801; ADC_synthase.
DR   InterPro; IPR019999; Anth_synth_I-like.
DR   InterPro; IPR006805; Anth_synth_I_N.
DR   InterPro; IPR015890; Chorismate_C.
DR   InterPro; IPR010118; Para-NH2Bz/anthranilate_synth.
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; TIGR01824; PabB-clade2; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis; Magnesium; Transferase.
FT   CHAIN           1..470
FT                   /note="Aminodeoxychorismate synthase component 1"
FT                   /id="PRO_0000154138"
SQ   SEQUENCE   470 AA;  50970 MW;  D2B50CD11A467817 CRC64;
     MFTISGVVLI TRPVYDEGSL NYCQSGAMNN GILLESVEGN KPRYSIGGAE PIGTINANAV
     LTAATYAEDV KFTDADPLNG TRVAICNGED TQQEEMGFQG GALGYFAYDV GRRLEGYNDL
     GIEDWAIPDL AGSSYEIGVS ADHQNDVIVL IAHASADGND VFITSSRQLS MVAGPTCCAS
     GDVEILRNKL HYYGVIPFSQ DDCGFNRLKD YLGSGDMYQV NLGNRNVGAI VMTLFQGYNQ
     LRLMNPGPYM VFLDEANIIM ASPEIVLADE ANDLNTRPIA GTLMRLNEQD EDGVNAACLG
     QHHKDRAEHM MIVDLVRNDL GRVGRFGSVN VQEIVGAENY SVVMHIVSRV TGSLNEAFEA
     MEIIRAGFPG GSITGAPKVR AMEIIEELEP QRRDGWGGSI GYIAYRGNIG YRIAIRTLFA
     CNGQLFASSG AGLVGDSMED GEYNETFEKM RALRSFFCAA VHMGKTPYLS