PABA_SERMA
ID PABA_SERMA Reviewed; 191 AA.
AC P06195;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 93.
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 Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
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}.
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; X02605; CAA26452.1; -; Genomic_DNA.
DR PIR; S09635; S09635.
DR AlphaFoldDB; P06195; -.
DR SMR; P06195; -.
DR STRING; 273526.SMDB11_3831; -.
DR MEROPS; C26.955; -.
DR PRIDE; P06195; -.
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..191
FT /note="Aminodeoxychorismate synthase component 2"
FT /id="PRO_0000056852"
FT DOMAIN 1..191
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 172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 191 AA; 21143 MW; F1063CC327BEF3E3 CRC64;
MLLLIDNYDS FTYNLYQYFC ELGAEVVVKR NDELQLTDIE RLAPQHLVIS PGPCTPNEAG
ISVAAIRHFA GKLPILGVCL GHQALGQAFG AEVVRARAVM HGKTSAIRHL GVGVFRGLSD
PLTVTRYHSL VLKADTLPDC FEVTAWSERD GVRDEIMGIR HRALALEGVQ FHPESVLSEQ
GHQLLDNFLN R
