TRE2_SYNY3
ID TRE2_SYNY3 Reviewed; 485 AA.
AC P74130;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Anthranilate synthase component I-like protein;
DE EC=4.1.3.27;
GN Name=trpE2; OrderedLocusNames=slr1979;
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).
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 -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- SUBUNIT: Tetramer of two components I and two components II.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
CC using ammonia rather than glutamine, whereas component II provides
CC glutamine amidotransferase activity.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
CC -!- CAUTION: This is a divergent form of trpE. It is not obvious if it is
CC active in Trp biosynthesis. {ECO:0000305}.
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DR EMBL; BA000022; BAA18216.1; -; Genomic_DNA.
DR PIR; S75655; S75655.
DR AlphaFoldDB; P74130; -.
DR SMR; P74130; -.
DR STRING; 1148.1653301; -.
DR PaxDb; P74130; -.
DR EnsemblBacteria; BAA18216; BAA18216; BAA18216.
DR KEGG; syn:slr1979; -.
DR eggNOG; COG0147; Bacteria.
DR InParanoid; P74130; -.
DR OMA; NMDFNIA; -.
DR PhylomeDB; P74130; -.
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; IPR015890; Chorismate_C.
DR InterPro; IPR010118; Para-NH2Bz/anthranilate_synth.
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; TIGR01824; PabB-clade2; 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..485
FT /note="Anthranilate synthase component I-like protein"
FT /id="PRO_0000154115"
FT BINDING 69
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 271..273
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 306..307
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 441
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 455..457
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 457
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
SQ SEQUENCE 485 AA; 54271 MW; 4F25ECCB3897BC7C CRC64;
MASIAHCSGG LVGAGNFDFI LGGSDPVGRH GLMELQPWHW CCLPLEGRTG SEIFSQLFGH
QGIATLLESP YPASPDHPHL GRYSLCAGQP RKGRLWTPKP EEIFSFLNQL CPCNHDVNLT
KNIPEHLPFH GGWLGWLGYD TAWAIEKLPY SKADDLPFPV AYWYEPENFV ILDHQEQLLW
LATTDQEKIK FFQTQLADKI NSVSSPQVPP LNLTYTTDQD QYETMVNQAK QYIKAGDIFQ
ANLTLRFIAK TEQKLNSWQV YQHLQTINPS PFASYWRSPW GDVVSCSPER LVKLEGNVAQ
TRPIAGTRAR GKNLAEDEQL LQELLVNTKE LAEHIMLVDL ERNDLGRVCT WGTVEVDELL
AIERYSHVSH LVSNVKGILQ PDKTGVDLVK ALFPGGTITG CPKIRCLEII EELEPVRRSL
FYGSCGYWDQ RGNLDLNILI RTLLFTSGQV TGQVGAGIVA DSDPAKEWLE SLQKAKALLA
ALEGL
