PABA_ECOLI
ID PABA_ECOLI Reviewed; 187 AA.
AC P00903; Q2M726;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Aminodeoxychorismate synthase component 2;
DE Short=ADC synthase;
DE Short=ADCS;
DE EC=2.6.1.85 {ECO:0000269|PubMed:7592344, ECO:0000305|PubMed:4914080};
DE AltName: Full=4-amino-4-deoxychorismate synthase component 2;
DE AltName: Full=Aminodeoxychorismate synthase, glutamine amidotransferase component;
GN Name=pabA {ECO:0000303|PubMed:4914080}; OrderedLocusNames=b3360, JW3323;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6350604; DOI=10.1016/s0022-2836(83)80295-2;
RA Kaplan J.B., Nichols B.P.;
RT "Nucleotide sequence of Escherichia coli pabA and its evolutionary
RT relationship to trp(G)D.";
RL J. Mol. Biol. 168:451-468(1983).
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=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150.
RX PubMed=2546924; DOI=10.1128/jb.171.8.4525-4529.1989;
RA Kawamukai M., Matsuda H., Fujii W., Utsumi R., Komano T.;
RT "Nucleotide sequences of fic and fic-1 genes involved in cell filamentation
RT induced by cyclic AMP in Escherichia coli.";
RL J. Bacteriol. 171:4525-4529(1989).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND NOMENCLATURE.
RC STRAIN=K12;
RX PubMed=4914080; DOI=10.1128/jb.102.3.767-773.1970;
RA Huang M., Gibson F.;
RT "Biosynthesis of 4-aminobenzoate in Escherichia coli.";
RL J. Bacteriol. 102:767-773(1970).
RN [7]
RP MUTAGENESIS OF CYS-79; HIS-168 AND GLU-170, AND ACTIVE SITE.
RX PubMed=8096767; DOI=10.1021/bi00065a031;
RA Roux B., Walsh C.T.;
RT "p-aminobenzoate synthesis in Escherichia coli: mutational analysis of
RT three conserved amino acid residues of the amidotransferase PabA.";
RL Biochemistry 32:3763-3768(1993).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=7592344; DOI=10.1128/jb.177.20.5918-5923.1995;
RA Viswanathan V.K., Green J.M., Nichols B.P.;
RT "Kinetic characterization of 4-amino 4-deoxychorismate synthase from
RT Escherichia coli.";
RL J. Bacteriol. 177:5918-5923(1995).
RN [9]
RP SUBUNIT.
RX PubMed=8679677; DOI=10.1016/0167-4838(96)00029-5;
RA Rayl E.A., Green J.M., Nichols B.P.;
RT "Escherichia coli aminodeoxychorismate synthase: analysis of pabB mutations
RT affecting catalysis and subunit association.";
RL Biochim. Biophys. Acta 1295:81-88(1996).
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. {ECO:0000269|PubMed:4914080, ECO:0000269|PubMed:7592344}.
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 Evidence={ECO:0000269|PubMed:7592344, ECO:0000305|PubMed:4914080};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11673;
CC Evidence={ECO:0000269|PubMed:7592344, ECO:0000305|PubMed:4914080};
CC -!- ACTIVITY REGULATION: Inhibited by 6-diazo-5-oxo-L-norleucine (DON). The
CC inhibition is competitive with glutamine, but uncompetitive with
CC chorismate. {ECO:0000269|PubMed:7592344}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.2 uM for chorismate (with the heterodimer PabA-PabB and
CC glutamine as the amino donor at pH 7.5) {ECO:0000269|PubMed:7592344};
CC KM=18.6 uM for chorismate (with the heterodimer PabA-PabB and ammonia
CC as the amino donor at pH 7.5) {ECO:0000269|PubMed:7592344};
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). {ECO:0000269|PubMed:8679677}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not produce 4-
CC aminobenzoate. {ECO:0000269|PubMed:4914080}.
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DR EMBL; M28363; AAA23774.1; -; Genomic_DNA.
DR EMBL; K00030; AAA24260.1; -; Genomic_DNA.
DR EMBL; M32354; AAA24264.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58157.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76385.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77930.1; -; Genomic_DNA.
DR PIR; A01124; AGEC2.
DR RefSeq; NP_417819.1; NC_000913.3.
DR RefSeq; WP_000601847.1; NZ_STEB01000004.1.
DR AlphaFoldDB; P00903; -.
DR SMR; P00903; -.
DR BioGRID; 4262475; 89.
DR BioGRID; 852184; 2.
DR ComplexPortal; CPX-5245; Aminodeoxychorismate synthase complex.
DR DIP; DIP-10433N; -.
DR IntAct; P00903; 6.
DR STRING; 511145.b3360; -.
DR MEROPS; C26.955; -.
DR jPOST; P00903; -.
DR PaxDb; P00903; -.
DR PRIDE; P00903; -.
DR EnsemblBacteria; AAC76385; AAC76385; b3360.
DR EnsemblBacteria; BAE77930; BAE77930; BAE77930.
DR GeneID; 66672759; -.
DR GeneID; 947873; -.
DR KEGG; ecj:JW3323; -.
DR KEGG; eco:b3360; -.
DR PATRIC; fig|1411691.4.peg.3370; -.
DR EchoBASE; EB0676; -.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_014340_1_2_6; -.
DR InParanoid; P00903; -.
DR OMA; TEHGHAM; -.
DR PhylomeDB; P00903; -.
DR BioCyc; EcoCyc:PABASYN-COMPII-MON; -.
DR BioCyc; MetaCyc:PABASYN-COMPII-MON; -.
DR BRENDA; 2.6.1.85; 2026.
DR BRENDA; 2.6.1.86; 2026.
DR SABIO-RK; P00903; -.
DR UniPathway; UPA00077; UER00149.
DR PRO; PR:P00903; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009356; C:aminodeoxychorismate synthase complex; IPI:ComplexPortal.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IMP:UniProtKB.
DR GO; GO:0046656; P:folic acid biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW Folate biosynthesis; Glutamine amidotransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..187
FT /note="Aminodeoxychorismate synthase component 2"
FT /id="PRO_0000056849"
FT DOMAIN 1..187
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 79
FT /evidence="ECO:0000305|PubMed:8096767"
FT ACT_SITE 168
FT /evidence="ECO:0000305|PubMed:8096767"
FT ACT_SITE 170
FT /evidence="ECO:0000305|PubMed:8096767"
FT MUTAGEN 79
FT /note="C->S: 10000-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:8096767"
FT MUTAGEN 168
FT /note="H->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8096767"
FT MUTAGEN 170
FT /note="E->A: 150-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:8096767"
FT MUTAGEN 170
FT /note="E->D: 4-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:8096767"
FT MUTAGEN 170
FT /note="E->K,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8096767"
SQ SEQUENCE 187 AA; 20772 MW; 0E5F43499D5F55C6 CRC64;
MILLIDNYDS FTWNLYQYFC ELGADVLVKR NDALTLADID ALKPQKIVIS PGPCTPDEAG
ISLDVIRHYA GRLPILGVCL GHQAMAQAFG GKVVRAAKVM HGKTSPITHN GEGVFRGLAN
PLTVTRYHSL VVEPDSLPAC FDVTAWSETR EIMGIRHRQW DLEGVQFHPE SILSEQGHQL
LANFLHR
