TRPE_BACSU
ID TRPE_BACSU Reviewed; 515 AA.
AC P03963;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=BSU22680;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3924737; DOI=10.1016/0378-1119(85)90125-8;
RA Henner D.J., Band L., Shimotsu H.;
RT "Nucleotide sequence of the Bacillus subtilis tryptophan operon.";
RL Gene 34:169-177(1985).
RN [2]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6425119; DOI=10.1016/0378-1119(84)90238-5;
RA Band L., Shimotsu H., Henner D.J.;
RT "Nucleotide sequence of the Bacillus subtilis trpE and trpD genes.";
RL Gene 27:55-65(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Henner D.J.;
RT "Sequence of Bacillus subtilis dbpA, mtr(A,B), gerC(1-3), ndk, cheR,
RT aro(B,E,F,H), trp(A-F), hisH, and tyrA genes.";
RL Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RX PubMed=6436812; DOI=10.1073/pnas.81.20.6315;
RA Shimotsu H., Henner D.J.;
RT "Characterization of the Bacillus subtilis tryptophan promoter region.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:6315-6319(1984).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RX PubMed=2422155; DOI=10.1128/jb.166.2.461-471.1986;
RA Shimotsu H., Kuroda M.I., Yanofsky C., Henner D.J.;
RT "Novel form of transcription attenuation regulates expression the Bacillus
RT subtilis tryptophan operon.";
RL J. Bacteriol. 166:461-471(1986).
CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC step biosynthesis of anthranilate, an intermediate in the biosynthesis
CC of L-tryptophan. In the first step, the glutamine-binding beta subunit
CC (TrpG) of anthranilate synthase (AS) provides the glutamine
CC amidotransferase activity which generates ammonia as a substrate that,
CC along with chorismate, is used in the second step, catalyzed by the
CC large alpha subunit of AS (TrpE) to produce anthranilate. In the
CC absence of TrpG, TrpE can synthesize anthranilate directly from
CC chorismate and high concentrations of ammonia (By similarity).
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00897};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00897};
CC -!- ACTIVITY REGULATION: Feedback inhibited by tryptophan. {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large alpha subunit (TrpE). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=Ref.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; K01391; AAA22865.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M80245; AAA20862.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14184.1; -; Genomic_DNA.
DR EMBL; M27566; AAA22875.1; -; Genomic_DNA.
DR PIR; A01119; NNBS1.
DR RefSeq; NP_390149.1; NC_000964.3.
DR RefSeq; WP_003246124.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P03963; -.
DR SMR; P03963; -.
DR STRING; 224308.BSU22680; -.
DR PaxDb; P03963; -.
DR PRIDE; P03963; -.
DR EnsemblBacteria; CAB14184; CAB14184; BSU_22680.
DR GeneID; 939008; -.
DR KEGG; bsu:BSU22680; -.
DR eggNOG; COG0147; Bacteria.
DR InParanoid; P03963; -.
DR OMA; GCVGYLD; -.
DR PhylomeDB; P03963; -.
DR BioCyc; BSUB:BSU22680-MON; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR005256; Anth_synth_I_PabB.
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; TIGR00564; trpE_most; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Magnesium; Metal-binding; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..515
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154079"
FT BINDING 50
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 281..283
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 316..317
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 431
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 451
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 465..467
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 467
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 480
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT CONFLICT 80
FT /note="A -> P (in Ref. 1; AAA22865 and 2; AAA20862)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="A -> S (in Ref. 1; AAA22865 and 2; AAA20862)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 58116 MW; 33B88D9D80BCD991 CRC64;
MNFQSNISAF LEDSLSHHTI PIVETFTVDT LTPIQMIEKL DREITYLLES KDDTSTWSRY
SFIGLNPFLT IKEEQGRFSA ADQDSKSLYT GNELKEVLNW MNTTYKIKTP ELGIPFVGGA
VGYLSYDMIP LIEPSVPSHT KETDMEKCML FVCRTLIAYD HETKNVHFIQ YARLTGEETK
NEKMDVFHQN HLELQNLIEK MMDQKNIKEL FLSADSYKTP SFETVSSNYE KSAFMADVEK
IKSYIKAGDI FQGVLSQKFE VPIKADAFEL YRVLRIVNPS PYMYYMKLLD REIVGSSPER
LIHVQDGHLE IHPIAGTRKR GADKAEDERL KVELMKDEKE KAEHYMLVDL ARNDIGRVAE
YGSVSVPEFT KIVSFSHVMH IISVVTGRLK KGVHPVDALM SAFPAGTLTG APKIRAMQLL
QELEPTPRET YGGCIAYIGF DGNIDSCITI RTMSVKNGVA SIQAGAGIVA DSVPEAEYEE
SCNKAGALLK TIHIAEDMFH SKEDKADEQI STIVR
