PABA_SALTY
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 03-AUG-2022, entry version 142.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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; P06193; -.
DR EnsemblBacteria; AAL22331; AAL22331; STM3469.
DR GeneID; 1254992; -.
DR KEGG; stm:STM3469; -.
DR PATRIC; fig|99287.12.peg.3666; -.
DR HOGENOM; CLU_014340_1_2_6; -.
DR OMA; TEHGHAM; -.
DR PhylomeDB; P06193; -.
DR BioCyc; SENT99287:STM3469-MON; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000001014; Chromosome.
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 GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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; 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
