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 08-NOV-2023, entry version 174. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 511145-b3360; -. DR EnsemblBacteria; AAC76385; AAC76385; b3360. DR EnsemblBacteria; BAE77930; BAE77930; BAE77930. DR GeneID; 75206304; -. 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 OrthoDB; 9786812at2; -. DR PhylomeDB; P00903; -. DR BioCyc; EcoCyc:PABASYN-COMPII-MONOMER; -. DR BioCyc; MetaCyc:PABASYN-COMPII-MONOMER; -. 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; IDA:EcoCyc. DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IMP:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:EcoCyc. 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:0008153; P:para-aminobenzoic acid biosynthetic process; IMP:EcoCyc. 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 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 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 //