PABB_SALTY
ID PABB_SALTY Reviewed; 454 AA.
AC P12680;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Aminodeoxychorismate synthase component 1;
DE Short=ADC synthase;
DE Short=ADCS;
DE EC=2.6.1.85;
DE AltName: Full=4-amino-4-deoxychorismate synthase component 1;
GN Name=pabB; OrderedLocusNames=STM1824;
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=3057324; DOI=10.1093/oxfordjournals.molbev.a040512;
RA Goncharoff P., Nichols B.P.;
RT "Evolution of aminobenzoate synthases: nucleotide sequences of Salmonella
RT typhimurium and Klebsiella aerogenes pabB.";
RL Mol. Biol. Evol. 5:531-548(1988).
RN [2]
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 (By similarity).
CC {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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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 -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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DR EMBL; M22079; AAA88618.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20739.1; -; Genomic_DNA.
DR PIR; A31132; A31132.
DR RefSeq; NP_460780.1; NC_003197.2.
DR RefSeq; WP_000978464.1; NC_003197.2.
DR AlphaFoldDB; P12680; -.
DR SMR; P12680; -.
DR STRING; 99287.STM1824; -.
DR PaxDb; P12680; -.
DR EnsemblBacteria; AAL20739; AAL20739; STM1824.
DR GeneID; 1253343; -.
DR KEGG; stm:STM1824; -.
DR PATRIC; fig|99287.12.peg.1924; -.
DR HOGENOM; CLU_006493_7_2_6; -.
DR OMA; HGRMDTS; -.
DR PhylomeDB; P12680; -.
DR BioCyc; SENT99287:STM1824-MON; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008153; P:para-aminobenzoic acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005802; ADC_synth_comp_1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR006805; Anth_synth_I_N.
DR InterPro; IPR015890; Chorismate_C.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00553; pabB; 1.
PE 3: Inferred from homology;
KW Folate biosynthesis; Magnesium; Reference proteome; Transferase.
FT CHAIN 1..454
FT /note="Aminodeoxychorismate synthase component 1"
FT /id="PRO_0000154139"
FT ACT_SITE 259
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /note="N6-(4-deoxychorismate)-lysine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250"
FT BINDING 44..47
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250"
FT BINDING 241..243
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250"
SQ SEQUENCE 454 AA; 50979 MW; 430B3949B4904546 CRC64;
MMKTLSPTVI TLPWRPDAAE HYFAPVNHLP WAMLLHSGDA IHPYNRFDIL VADPVTTLTT
RAQETTVCTA RTTTVTLDDP LHVLQTQLEA LPFHPQPDPD LPFQGGALGL FGYDLGRRFE
ILPDTAARDI ALPDMAIGLY DWALIVDHQK QVVSLISYHD ADARYRWLTS QRAPTRTPFR
LTSAWQSNMT RCEYGEKFRQ VQAWLHSGDC YQVNLSQRFQ ASYEGDEWQA FERLNRANRA
PFSAFLRLHD GAILSLSPER FIQLENGHIQ TRPIKGTLPR LNDPQADRQQ AQKLANSMKD
RAENLMIVDL MRNDIGRVAV PGSVKVPELF VVEPFPAVHH LVSTITARLP DSLHATDLLR
AAFPGGSITG APKVRAMEII DELEPQRRNA WCGSIGYLSF CGKMDTSITI RTVTATQGQL
YCSAGGGIVA DSNEEAEYQE TFDKVNRILH PLEN
