PABA_KLEAE
ID PABA_KLEAE Reviewed; 187 AA.
AC P06194;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 98.
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;
OS Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=548;
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).
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; X02604; CAA26451.1; -; Genomic_DNA.
DR AlphaFoldDB; P06194; -.
DR SMR; P06194; -.
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..187
FT /note="Aminodeoxychorismate synthase component 2"
FT /id="PRO_0000056850"
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; 20564 MW; 89997A6C05E10B79 CRC64;
MILLIDNYDS FTWNLYQYFC ELGAEVLVRR NDELTLADII SLAPAKIVIS PGPCTPDESG
ISLAAIRHFS GQTPILGVCL GHQAIAQVFG AAIVRAAKVM HGKTSPVSHT GQGVFLGLNN
PLTVTRYHSL LIDPRTLPEC FEVTARSEEG EIMGIRHRVF DLEGVQFHPE SILSEQGHQL
LANFLNR
