ID   PABA_STRLI              Reviewed;         192 AA.
AC   P27627;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Aminodeoxychorismate synthase component 2;
DE            Short=ADC synthase;
DE            Short=ADCS;
DE            EC=2.6.1.85;
DE   AltName: Full=4-amino-4-deoxychorismate synthase component 2;
DE   AltName: Full=Aminodeoxychorismate synthase, glutamine amidotransferase component;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   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. PabA converts
CC       glutamine into glutamate only in the presence of stoichiometric amounts
CC       of PabB (By similarity). {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   -!- 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}.
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DR   EMBL; M64859; AAA26799.1; -; Genomic_DNA.
DR   PIR; JN0577; JN0577.
DR   AlphaFoldDB; P27627; -.
DR   SMR; P27627; -.
DR   MEROPS; C26.955; -.
DR   UniPathway; UPA00077; UER00149.
DR   GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; ISS:UniProtKB.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; ISS:UniProtKB.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR00566; trpG_papA; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis; Glutamine amidotransferase; Transferase.
FT   CHAIN           1..192
FT                   /note="Aminodeoxychorismate synthase component 2"
FT                   /id="PRO_0000056853"
FT   DOMAIN          3..192
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   192 AA;  20759 MW;  6BBA054AEC6E679E CRC64;
     MTSVLMIDNC DSFTYNLVDQ FSPHGTIVIV KRNHPFYDGE IEAIMALTSI CITPGPCYPA
     EAALNSCSII GHLAGRIPIL GICLGQQALG QARGGLVIFA HGKLSNIEHN GIFAPLFNPP
     RALPAGRYHS LVVEPARIEV TGQCNQLEVV PQEIMAIRHR DLPVEGVQFH PESILSSNGA
     AILANLIHRP CH