TRPE_SYNY3
ID TRPE_SYNY3 Reviewed; 508 AA.
AC P20170; P20168;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=slr0738;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-408.
RX PubMed=3141423; DOI=10.1016/s0021-9258(19)77887-9;
RA Reilly P., Hulmes J.D., Pan Y.-C.E., Nelson N.;
RT "Molecular cloning and sequencing of the psaD gene encoding subunit II of
RT photosystem I from the cyanobacterium, Synechocystis sp. PCC 6803.";
RL J. Biol. Chem. 263:17658-17662(1988).
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=AAA88627.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BA000022; BAA16689.1; -; Genomic_DNA.
DR EMBL; J04195; AAA88626.1; ALT_FRAME; Genomic_DNA.
DR EMBL; J04195; AAA88627.1; ALT_FRAME; Genomic_DNA.
DR PIR; S74537; S74537.
DR AlphaFoldDB; P20170; -.
DR SMR; P20170; -.
DR IntAct; P20170; 1.
DR STRING; 1148.1651761; -.
DR PaxDb; P20170; -.
DR EnsemblBacteria; BAA16689; BAA16689; BAA16689.
DR KEGG; syn:slr0738; -.
DR eggNOG; COG0147; Bacteria.
DR InParanoid; P20170; -.
DR OMA; GCVGYLD; -.
DR PhylomeDB; P20170; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000001425; 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..508
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154114"
FT BINDING 51
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 283..285
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 323..324
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 350
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 438
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 458
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 477..479
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 479
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 492
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
SQ SEQUENCE 508 AA; 57147 MW; A3308E9A7B8A1FC1 CRC64;
MISPGFSHFT ELAQQGNFIP VYQEWVADLE TPVSAWYKVC SSQPYNFLLE SVEGGESIGR
YSFLGCDPMW VLEARGDETT QVLRNGQTET FRGNPLDILS QCLESIRPVN LPQLPPGIGG
LFGVWGYELI RWMEPRVPVY EPQPEDPPDG IWMQVDHLLI FDQVKRKIWA IAFADLRGEN
VDLETAYRNA CQRVTKLVLQ LQLPLPPEAT ALELLTKTQL EGKELNYSSN TEQEKFLEEV
AIAKDYITAG DIFQVVLSQR LSTIYRDDPF KLYRSLRLIN PSPYMAYYNF GHWQIIGSSP
EVMVKADRQL DGKLMATVRP IAGTRPRGKT HPEDEQLAEE LLNDPKEIAE HVMLVDLGRN
DLGRVCVQGS VKVNELMVIE RYSHVMHIVS NVVGELASDK TAWDLLKACF PAGTVSGAPK
IRAMEIINEL EPERRGPYSG VYGYYDFEGQ LNTAIAIRTM VVQEQPDGAH RVSVQTGAGI
VADSDPQKEY EETLNKARGL LEAIRALS
