ID   PABA_SALTY              Reviewed;         187 AA.
AC   P06193;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   02-SEP-2026, entry version 157.
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;
GN   Name=pabA; OrderedLocusNames=STM3469;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3894673; DOI=10.1016/0022-2836(85)90004-x;
RA   Kaplan J.B., Merkel W.K., Nichols B.P.;
RT   "Evolution of glutamine amidotransferase genes. Nucleotide sequences of the
RT   pabA genes from Salmonella typhimurium, Klebsiella aerogenes and Serratia
RT   marcescens.";
RL   J. Mol. Biol. 183:327-340(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2403545; DOI=10.1128/jb.172.1.397-410.1990;
RA   Tran P.V., Bannor T.A., Doktor S.Z., Nichols B.P.;
RT   "Chromosomal organization and expression of Escherichia coli pabA.";
RL   J. Bacteriol. 172:397-410(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; X02603; CAA26450.1; -; Genomic_DNA.
DR   EMBL; M32355; AAA27177.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22331.1; -; Genomic_DNA.
DR   PIR; S09636; S09636.
DR   RefSeq; NP_462372.1; NC_003197.2.
DR   RefSeq; WP_000601880.1; NC_003197.2.
DR   AlphaFoldDB; P06193; -.
DR   SMR; P06193; -.
DR   STRING; 99287.STM3469; -.
DR   MEROPS; C26.955; -.
DR   PaxDb; 99287-STM3469; -.
DR   GeneID; 1254992; -.
DR   KEGG; stm:STM3469; -.
DR   PATRIC; fig|99287.12.peg.3666; -.
DR   HOGENOM; CLU_014340_1_2_6; -.
DR   OMA; YEVAVYQ; -.
DR   PhylomeDB; P06193; -.
DR   BioCyc; SENT99287:STM3469-MONOMER; -.
DR   UniPathway; UPA00077; UER00149.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0046820; F:aminodeoxychorismate synthase activity; ISS:UniProtKB.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; ISS:UniProtKB.
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   InterPro; IPR050472; Anth_synth/Amidotransfase.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   NCBIfam; NF005946; PRK08007.1; 1.
DR   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis; Glutamine amidotransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..187
FT                   /note="Aminodeoxychorismate synthase component 2"
FT                   /id="PRO_0000056851"
FT   DOMAIN          1..187
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   187 AA;  20801 MW;  AB283D23FA543846 CRC64;
     MILLIDNYDS FTWNLYQYFC ELGAEVQVRR NDALTLAHID ALNPQKIVIS PGPCTPNDAG
     ISLAVIRHYA GRIPMLGVCL GHQAMAQAFG ASVVRAAKVM HGKTSPVTHN GQGVFRGLPS
     PLTVTRYHSL IVDPATLPEC FEITAWSETQ EIMGIRHREW DLEGVQFHPE SILSEQGHAL
     LKNFLRR
//