TRPE_METTM
ID TRPE_METTM Reviewed; 461 AA.
AC P26940; D9PUE5;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=MTBMA_c02340;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=1860817; DOI=10.1128/jb.173.16.5017-5023.1991;
RA Meile L., Stettler R., Banholzer R., Kotik M., Leisinger T.;
RT "Tryptophan gene cluster of Methanobacterium thermoautotrophicum Marburg:
RT molecular cloning and nucleotide sequence of a putative trpEGCFBAD
RT operon.";
RL J. Bacteriol. 173:5017-5023(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
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}.
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DR EMBL; M65060; AAA73028.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL57843.1; -; Genomic_DNA.
DR RefSeq; WP_013295070.1; NC_014408.1.
DR AlphaFoldDB; P26940; -.
DR SMR; P26940; -.
DR STRING; 79929.MTBMA_c02340; -.
DR EnsemblBacteria; ADL57843; ADL57843; MTBMA_c02340.
DR GeneID; 9703940; -.
DR KEGG; mmg:MTBMA_c02340; -.
DR PATRIC; fig|79929.8.peg.230; -.
DR HOGENOM; CLU_006493_9_3_2; -.
DR OMA; HGRMDTS; -.
DR OrthoDB; 13784at2157; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000000345; 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; 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; IPR010116; Anthranilate_synth_I_arc_typ.
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; TIGR01820; TrpE-arch; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Magnesium; Metal-binding; Tryptophan biosynthesis.
FT CHAIN 1..461
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154130"
FT BINDING 43
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 238..240
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 273..274
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 388
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 408
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 422..424
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 424
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 437
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT CONFLICT 7
FT /note="G -> K (in Ref. 1; AAA73028)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="E -> EQ (in Ref. 1; AAA73028)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="D -> Y (in Ref. 1; AAA73028)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 51911 MW; 4A90AD4B91846E2A CRC64;
MGVNVFGIIN LEKPRKEKLE FREPFEVFKS IYSEYESSFL LESMESDTGL ARYSFIGFEP
EMIIRAREGV IEIDDGDSRE EFDSKNPFED LRGFLKMEKN SGGFCGGLVG YISYQAARFF
DTIRLSEGDF PDFEFGLFLD GIMFNHLTGE CSYISRHGNR LPDISPLLGD EVPTGTLGYR
RERTLLSKRR YMDMVLEAKE RIREGEIFQA VLSSATDYRL RGDRLAFYES LRRINPSPYM
YHLKLGEREI TGSSPEMLVR VEDRRIETFP IAGTRPRGRT EEEDGVIASD LLSDEKELAE
HLMLVDLARN DIGRVSEFGS VEVPEYMTIK RFSHVQHILS HVTGKLRDGM DAVDALGAVF
PAGTVSGAPK IRAMEIIESL EGVPRNAYAG ALGYLSLNGN ADFAITIRSM VCQGKTGRIQ
AGAGIVHDSI PEMEYLECQN KARALLKSME MAGEQVDPDN R
