(data stored in SCRATCH zone)

SWISSPROT: PABA_BACSU

ID   PABA_BACSU              Reviewed;         194 AA.
AC   P28819;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   11-DEC-2019, entry version 134.
DE   RecName: Full=Aminodeoxychorismate/anthranilate synthase component 2;
DE            Short=ADC synthase;
DE            Short=ADCS;
DE            EC=2.6.1.85;
DE            EC=4.1.3.27;
DE   AltName: Full=4-amino-4-deoxychorismate synthase component 2;
DE   AltName: Full=Aminodeoxychorismate synthase, glutamine amidotransferase component;
GN   Name=pabA; Synonyms=trpG; OrderedLocusNames=BSU00750;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
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).
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. Also involved in the biosynthesis of anthranilate.
CC       {ECO:0000269|PubMed:2123867}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC         pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58359; EC=4.1.3.27;
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: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
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   -!- INDUCTION: Repressed by tryptophan. {ECO:0000269|PubMed:2123867}.
DR   EMBL; M34053; AAA22695.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05310.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11851.1; -; Genomic_DNA.
DR   PIR; B37854; B37854.
DR   RefSeq; NP_387956.1; NC_000964.3.
DR   RefSeq; WP_003243797.1; NZ_JNCM01000028.1.
DR   SMR; P28819; -.
DR   STRING; 224308.BSU00750; -.
DR   MEROPS; C26.955; -.
DR   PaxDb; P28819; -.
DR   PRIDE; P28819; -.
DR   EnsemblBacteria; CAB11851; CAB11851; BSU00750.
DR   GeneID; 936441; -.
DR   KEGG; bsu:BSU00750; -.
DR   PATRIC; fig|224308.179.peg.75; -.
DR   eggNOG; ENOG4105DDQ; Bacteria.
DR   eggNOG; COG0512; LUCA.
DR   HOGENOM; HOG000025029; -.
DR   InParanoid; P28819; -.
DR   KO; K01664; -.
DR   OMA; HQVVIYR; -.
DR   PhylomeDB; P28819; -.
DR   BioCyc; BSUB:BSU00750-MONOMER; -.
DR   UniPathway; UPA00035; UER00040.
DR   UniPathway; UPA00077; UER00149.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IMP:UniProtKB.
DR   GO; GO:0004049; F:anthranilate synthase activity; IMP: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; IMP:UniProtKB.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IMP:UniProtKB.
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   2: Evidence at transcript level;
DR   PRODOM; P28819.
DR   SWISS-2DPAGE; P28819.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Folate biosynthesis; Glutamine amidotransferase; Lyase; Reference proteome;
KW   Transferase; Tryptophan biosynthesis.
FT   CHAIN           1..194
FT                   /note="Aminodeoxychorismate/anthranilate synthase component
FT                   2"
FT                   /id="PRO_0000056848"
FT   DOMAIN          1..194
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   194 AA;  21685 MW;  7167D43557DEB37A CRC64;
     MILMIDNYDS FTYNLVQYLG ELGEELVVKR NDSITIDEIE ELSPDFLMIS PGPCSPDEAG
     ISLEAIKHFA GKIPIFGVCL GHQSIAQVFG GDVVRAERLM HGKTSDIEHD GKTIFEGLKN
     PLVATRYHSL IVKPETLPSC FTVTAQTKEG EIMAIRHNDL PIEGVQFHPE SIMTSFGKEM
     LRNFIETYRK EVIA
//

If you have problems or comments...

PBIL Back to PBIL home page