TRPE2_HALSA
ID TRPE2_HALSA Reviewed; 488 AA.
AC Q9HS66;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Anthranilate synthase component 1 2;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase component I 2;
GN Name=trpE2; OrderedLocusNames=VNG_0384G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004437; AAG18942.1; -; Genomic_DNA.
DR PIR; B84197; B84197.
DR RefSeq; WP_010902237.1; NC_002607.1.
DR AlphaFoldDB; Q9HS66; -.
DR SMR; Q9HS66; -.
DR STRING; 64091.VNG_0384G; -.
DR PaxDb; Q9HS66; -.
DR PRIDE; Q9HS66; -.
DR EnsemblBacteria; AAG18942; AAG18942; VNG_0384G.
DR GeneID; 5952507; -.
DR KEGG; hal:VNG_0384G; -.
DR PATRIC; fig|64091.14.peg.285; -.
DR HOGENOM; CLU_006493_9_3_2; -.
DR InParanoid; Q9HS66; -.
DR OMA; QTNVSHR; -.
DR OrthoDB; 13784at2157; -.
DR PhylomeDB; Q9HS66; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000000554; 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..488
FT /note="Anthranilate synthase component 1 2"
FT /id="PRO_0000154126"
FT BINDING 260..262
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 295..296
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 322
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 410
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 430
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 444..446
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 446
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
SQ SEQUENCE 488 AA; 51350 MW; D42982AA9A28F75E CRC64;
MPDSAALATD PAAFRDAAGD ATAPTRAVVE ARLPVTDPFA AYRRARGDAP SFHYETTGGS
DGWGYFGVDP ASMLRADGAG ALDTVQAAVG ARLARVGCDV PHPGGLFGWL SYDIARELEA
IPDTTTDARG LPRLQLGVYP TIAAWREPFT PGDDLRLIAA VPVDEYTPDG AFEAGRDRVQ
SLAAAIRDGD PAVGPPPADS PAPFESVAGR AAFESRVRRI QDAIRDGDTF QANVSHRLDA
PAAVHPVAVF EALRDTNPAP YSGIVEFPGV DLVSASPELL LARRGRELTT EPIAGTRPRG
ATPAEDDAAR AALRADDKER AEHAMLVDLE RNDLGKVSEY GSVAVPDYRR VDAYSEVLHL
VSEVTGRLRD SCSLRDAIAA VFPGGTITGA PKPRTMALID TVEATRRGPY TGSLAAIGFD
GDATLSITIR TLVRRAATYH LRVGAGIVHD STPAAEYDET LAKARALVTA LGDAGGIGRV
ADTTPDNS
