PABB_BACSU
ID PABB_BACSU Reviewed; 470 AA.
AC P28820;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 140.
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; Synonyms=pab {ECO:0000303|PubMed:2123867};
GN OrderedLocusNames=BSU00740;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=ASB342;
RX PubMed=2123867; DOI=10.1128/jb.172.12.7211-7226.1990;
RA Slock J., Stahly D.P., Han C.-Y., Six E.W., Crawford I.P.;
RT "An apparent Bacillus subtilis folic acid biosynthetic operon containing
RT pab, an amphibolic trpG gene, a third gene required for synthesis of para-
RT aminobenzoic acid, and the dihydropteroate synthase gene.";
RL J. Bacteriol. 172:7211-7226(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ALA-283, BIOPHYSICOCHEMICAL
RP PROPERTIES, REACTION MECHANISM, AND SUBUNIT.
RX PubMed=19275258; DOI=10.1021/ja809283u;
RA Schadt H.S., Schadt S., Oldach F., Sussmuth R.D.;
RT "2-Amino-2-deoxyisochorismate is a key intermediate in Bacillus subtilis p-
RT aminobenzoic acid biosynthesis.";
RL J. Am. Chem. Soc. 131:3481-3483(2009).
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.
CC {ECO:0000269|PubMed:19275258}.
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:19275258};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=380 uM for chorismate (with PabA and ammonia as the amino donor at
CC pH 7.5) {ECO:0000269|PubMed:19275258};
CC KM=420 uM for chorismate (with PabA and glutamine as the amino donor
CC at pH 7.5) {ECO:0000269|PubMed:19275258};
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:19275258}.
CC -!- DISRUPTION PHENOTYPE: Requires p-aminobenzoic acid but not tryptophan
CC for growth. {ECO:0000269|PubMed:2123867}.
CC -!- MISCELLANEOUS: The catalytically active amino acid residue K274 of
CC E.coli enzyme is missing and corresponds to A283 in B.subtilis. It is
CC postulated that the enzymatic mechanism for the PABA biosynthesis in
CC B.subtilis proceeds without covalent intermediate. First, ammonia is
CC added at C2 of chorismate with concomitant loss of the C4 hydroxy
CC group, yielding 2-amino-2-deoxyisochorismate (ADIC). The second step is
CC the addition of a second molecule ammonia to C4 of ADIC with
CC concomitant loss of the C2 amino group, yielding ADC. Both steps are
CC catalyzed by ADCS (PubMed:19275258). {ECO:0000305|PubMed:19275258}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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DR EMBL; M34053; AAA22694.1; -; Genomic_DNA.
DR EMBL; D26185; BAA05309.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11850.1; -; Genomic_DNA.
DR PIR; A37854; A37854.
DR RefSeq; NP_387955.1; NC_000964.3.
DR RefSeq; WP_003242468.1; NZ_JNCM01000028.1.
DR AlphaFoldDB; P28820; -.
DR SMR; P28820; -.
DR STRING; 224308.BSU00740; -.
DR PaxDb; P28820; -.
DR PRIDE; P28820; -.
DR EnsemblBacteria; CAB11850; CAB11850; BSU_00740.
DR GeneID; 936926; -.
DR KEGG; bsu:BSU00740; -.
DR PATRIC; fig|224308.179.peg.74; -.
DR eggNOG; COG0147; Bacteria.
DR InParanoid; P28820; -.
DR OMA; HGRMDTS; -.
DR PhylomeDB; P28820; -.
DR BioCyc; BSUB:BSU00740-MON; -.
DR BioCyc; MetaCyc:BSU00740-MON; -.
DR BRENDA; 2.6.1.85; 658.
DR SABIO-RK; P28820; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IDA: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:0046654; P:tetrahydrofolate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.60.120.10; -; 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.
PE 1: Evidence at protein level;
KW Folate biosynthesis; Magnesium; Reference proteome; Transferase.
FT CHAIN 1..470
FT /note="Aminodeoxychorismate synthase component 1"
FT /id="PRO_0000154135"
FT MUTAGEN 283
FT /note="A->I: Complete loss of aminodeoxychorismate synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:19275258"
FT MUTAGEN 283
FT /note="A->K: Absence of covalent intermediate."
FT /evidence="ECO:0000269|PubMed:19275258"
FT MUTAGEN 283
FT /note="A->V: Complete loss of aminodeoxychorismate synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:19275258"
SQ SEQUENCE 470 AA; 53251 MW; CA7544C30689383E CRC64;
MAQRRPAGKK IPFQKDSFLQ QFEKLAQSRK HHVLLESARG GRYSIAGLDP IATVKGKDGI
TTIKHGDEML FKEGDPLRAF HSWFKTLETE TNHEFPDFQG GAIGFLSYDY ARYIENFKML
SLDDLETPDI YFLVFDDIAV YDHQEESLWL ITHVNGSDQE TADVKLSELE QMWLTELPAV
TSREMKPETA GSFAAPFTED GFSQAVEKIK QYIASGDVFQ VNLSIRQSQS LSVHPYQIYK
TLREVNPSPY MAYLETPDFQ IICGSPELLV SKKGKLLETR PIAGTRSRGK TNEEDEALAN
ELIHNEKERA EHVMLVDLER NDLGRVSRYG SVRVNEFMAI EKYSHVMHIV SNVQGELQDG
YDAVDIIHAV FPGGTITGAP KVRTMEIIEE LEPTRRGLYT GSIGWFGYNH DLQFNIVIRT
IYATGGQAFM QSGAGVVIDS VPKHEYKESF KKAFAMQRAL ELSEEETKIR
