TRPE_VIBPA
ID TRPE_VIBPA Reviewed; 541 AA.
AC P22099;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=VP1956;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BB22;
RX PubMed=1773058; DOI=10.3109/10425179109020770;
RA Crawford I.P., Han C.Y., Silverman M.;
RT "Sequence and features of the tryptophan operon of Vibrio
RT parahemolyticus.";
RL DNA Seq. 1:189-196(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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=BAC60219.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X17149; CAA35031.1; -; Genomic_DNA.
DR EMBL; BA000031; BAC60219.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_798335.1; NC_004603.1.
DR AlphaFoldDB; P22099; -.
DR SMR; P22099; -.
DR STRING; 223926.28806948; -.
DR EnsemblBacteria; BAC60219; BAC60219; BAC60219.
DR KEGG; vpa:VP1956; -.
DR PATRIC; fig|223926.6.peg.1871; -.
DR eggNOG; COG0147; Bacteria.
DR HOGENOM; CLU_006493_9_4_6; -.
DR OMA; AYRSFMN; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000002493; Chromosome 1.
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; IEA:UniProtKB-UniPathway.
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; IPR005257; Anth_synth_I_TrpE.
DR InterPro; IPR015890; Chorismate_C.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR PANTHER; PTHR11236:SF22; PTHR11236:SF22; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PIRSF; PIRSF001373; TrpE; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00565; trpE_proteo; 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..541
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154119"
FT BINDING 61
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 311..313
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 348..349
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 469
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 489
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 503..505
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 505
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 518
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT CONFLICT 105
FT /note="V -> L (in Ref. 1; CAA35031)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="D -> S (in Ref. 1; CAA35031)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="E -> A (in Ref. 1; CAA35031)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="P -> S (in Ref. 1; CAA35031)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="S -> G (in Ref. 1; CAA35031)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="S -> L (in Ref. 1; CAA35031)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 59771 MW; CE186C09CAB8AA0D CRC64;
MRLCTAGRLK QLQGGLVNKA IEIKKLGQLE VLKASVPYTQ DPTRLFHTIC ENKTDSLLLE
SAEIDSKQNL KSLLIVDSAV RIVCYGHTVS FHALTENGKN LLTHVNQNVR GEVASQFDGE
TLTLEFIQPC DTIDEDSRLR EASSFDALRL VQHSFDLSSQ DKHAIFLGGL FAYDLVANFE
PLGDAVATNQ CPDYVFYVAE TLLVVDHQTE SCQLQATLFV DGSQKAALES RIEDIRAQCT
SPKRLPDATQ VANITAQPSV PDQDFCQIVR DLKEFVVKGD IFQVVPSRRF TLPCPSPLAA
YKELKQSNPS PYMFYMQDEL FTLFGASPES ALKYETDTNQ IEIYPIAGTR RRGKRPNGEI
DFDLDSRIEL ELRSDKKENA EHMMLVDLAR NDVARISQAG TRHVADLLKV DRYSHVMHLV
SRVVGQLRDD LDALHAYQAC MNMGTLTGAP KIRAMQLIRD VEGARRGSYG GAVGYLTGEG
TLDTCIVIRS AYVENGIAQV QAGAGVVFDS DPQAEADETR GKAQAVISAI QAAHSQPANK
E
