TRPE1_HALSA
ID TRPE1_HALSA Reviewed; 527 AA.
AC Q9HPG5;
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 1;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase component I 1;
GN Name=trpE1; OrderedLocusNames=VNG_1647G;
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}.
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DR EMBL; AE004437; AAG19902.1; -; Genomic_DNA.
DR PIR; B84317; B84317.
DR RefSeq; WP_010903200.1; NC_002607.1.
DR AlphaFoldDB; Q9HPG5; -.
DR SMR; Q9HPG5; -.
DR STRING; 64091.VNG_1647G; -.
DR PaxDb; Q9HPG5; -.
DR PRIDE; Q9HPG5; -.
DR EnsemblBacteria; AAG19902; AAG19902; VNG_1647G.
DR GeneID; 5954435; -.
DR KEGG; hal:VNG_1647G; -.
DR PATRIC; fig|64091.14.peg.1255; -.
DR HOGENOM; CLU_006493_9_0_2; -.
DR InParanoid; Q9HPG5; -.
DR OMA; HARFSFV; -.
DR OrthoDB; 13784at2157; -.
DR PhylomeDB; Q9HPG5; -.
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; 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; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..527
FT /note="Anthranilate synthase component 1 1"
FT /id="PRO_0000154125"
FT REGION 53..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 298..300
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 333..334
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 448
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 468
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 486..488
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 488
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
SQ SEQUENCE 527 AA; 56275 MW; 7B871F30685F02A3 CRC64;
MIETDRETFT ALADDGPAIV RVAADLDIDV APLTAYDALV ADADDHAFLL ESAEKTPASD
PDGAFTPDTT TEETRHARYS FVGYDPAAVV TVDPDDTTIT RLRDDPITDL LDAPDHATGD
VLDRLRSVMP AVPRRNIPTE DRQLLDGGLV GFLAYDAVYD LWLDEVGVER PPTPLPDAEF
AVTTRTLVFD RATDSVSLVC TPVADADTAT DVYDALEAEA KRVQAVLRDA TAPATAGIEV
TTERAGDRDA YTDAVETAAT AVRDGEVYQA VVSRTRELDG DIDPRALYDA LRAVNPSPYM
FLLAHGDHTV VGASPETLVA VHDDTVVTNP IAGTCQRGAS PVADRRLAGE MLADEKERAE
HTMLVDLARN DVRRVSAPGT VSVPEFMRVL KYSHVQHIES TVTGTLAADA DAFDATRAAF
PAGTLSGAPK VRAMEHIDAI EATPRGIYGG GVGYFSWTGD AELAITIRSG TITHTGDEDT
LTVRAGAGVV ADSDPDAEYE ETEAKMDGVL AAVDRLRTTD DGEAVHR
