TRPE_THEMA
ID TRPE_THEMA Reviewed; 461 AA.
AC Q08653;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=TM_0142;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7685830; DOI=10.1006/jmbi.1993.1345;
RA Kim C.W., Markiewicz P.G., Lee J.J., Schierle C.F., Miller J.H.;
RT "Studies of the hyperthermophile Thermotoga maritima by random sequencing
RT of cDNA and genomic libraries. Identification and sequencing of the trpEG
RT (D) operon.";
RL J. Mol. Biol. 231:960-981(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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=CAA52202.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X74075; CAA52202.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE000512; AAD35235.1; -; Genomic_DNA.
DR PIR; D72414; D72414.
DR RefSeq; NP_227957.1; NC_000853.1.
DR AlphaFoldDB; Q08653; -.
DR SMR; Q08653; -.
DR STRING; 243274.THEMA_04095; -.
DR EnsemblBacteria; AAD35235; AAD35235; TM_0142.
DR KEGG; tma:TM0142; -.
DR PATRIC; fig|243274.18.peg.785; -.
DR eggNOG; COG0147; Bacteria.
DR InParanoid; Q08653; -.
DR OMA; GCVGYLD; -.
DR BioCyc; MetaCyc:MON-281; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000008183; 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 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.
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..461
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154116"
FT BINDING 36
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 234..236
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 269..270
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 384
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 409
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 423..425
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 425
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT CONFLICT 104
FT /note="A -> R (in Ref. 1; CAA52202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 52240 MW; DEA00256445C568C CRC64;
MGDSMHVLKL VSDLETPVST FMKVSRGEEF AFLLESVELG SAFGRHSFIG IGKKDVLVFE
KGILRTSNQQ LDYTSSPLKA IKDWLEVYRY SVKHDELPSF RGGAVGFVSY DYISYIEKVK
VKASVFPTFY FVVPEHLIIF DHLKNNVFII SDSPEELTSK VLSPFEEKPE KNVFVTEPES
NFEREQFYKV VEKAKKYIVE GDIFQVVLSQ AFTFKTTLDP FYIYRALRMI NPSPYMFYLK
FGDTVVLGSS PETMAKVEGD KATVKPIAGT RPRGRTVEED LKLERELLND EKEIAEHVML
VDLGRNDLGR VCKEGTVRVE KKMVIERYSH VMHIVSQVSG ELKDDKDAVD VFEATFPAGT
VSGAPKVRAM EIIEELEPTP RGPYAGAVGY FSFPDDKGRM NMDSAITIRS FFFKGKQGWL
QAGAGIVYDS VPEREYQETL NKLRALFRSL EVAQKIQGGL F
