TRPE_HALVD
ID TRPE_HALVD Reviewed; 524 AA.
AC P33975; D4GT37;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE; OrderedLocusNames=HVO_2454;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DS2 / DSM 5716 / WFD11;
RX PubMed=1537810; DOI=10.1128/jb.174.5.1694-1697.1992;
RA Lam W.L., Logan S.M., Doolittle W.F.;
RT "Genes for tryptophan biosynthesis in the halophilic archaebacterium
RT Haloferax volcanii: the trpDFEG cluster.";
RL J. Bacteriol. 174:1694-1697(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(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; M83788; AAA73177.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE02423.1; -; Genomic_DNA.
DR PIR; A42301; A42301.
DR RefSeq; WP_004042367.1; NZ_AOHU01000044.1.
DR AlphaFoldDB; P33975; -.
DR SMR; P33975; -.
DR STRING; 309800.C498_07570; -.
DR EnsemblBacteria; ADE02423; ADE02423; HVO_2454.
DR GeneID; 8924704; -.
DR KEGG; hvo:HVO_2454; -.
DR eggNOG; arCOG02014; Archaea.
DR HOGENOM; CLU_006493_9_0_2; -.
DR OMA; HARFSFV; -.
DR OrthoDB; 13784at2157; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000008243; 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; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..524
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154127"
FT BINDING 55
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 297..299
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 332..333
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 447
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 467
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 485..487
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 487
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT CONFLICT 66..72
FT /note="GAFSAPA -> ARSPRPR (in Ref. 1; AAA73177)"
FT /evidence="ECO:0000305"
FT CONFLICT 140..143
FT /note="RQTL -> ADV (in Ref. 1; AAA73177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 55915 MW; FB1D1CCD3A4132AC CRC64;
MTAPDTDREE FVSLAGDADG PVVTHLVADL DVSVDPLAAY TTLADRSDYG FLLESAEKVS
SSNPQGAFSA PATAADSHAR FSFVGYDPEA VVTVGPDGVD VTDLGGPAAE FVGAGDGDVL
DSLRGALPDL PRVNFPETDR QTLTGGLVGF LAYEAVYDLW LDEVGRERPD TDDPDAEFVL
TTRTLSFDHR EDAVRLVCTP VVSPDDDPGE VYDGVVAEAE RVAEKLRAAD DPAPGGFERT
GEDAGSREEY EAAVRKTKEH VRDGDIYQGV ISRTRKLRGQ VDPVGLYASL REVNPSPYMF
LLRHGDRRVV GASPETLVSV RGDRVVVNPI AGTCQRGSGP VEDRRLAGEL LADAKERAEH
TMLVDLGRND VRRVSTPGSV RVEDFMSIIK YSHVQHIEST VSGTLDADAD AFDATRATFP
AGTLTGAPKV RAMEIIDDLE AEPRGVYGGG VGYYSWTGDA DVAIVIRTAT VDSGGADDAI
TVRAGAGIVA DSDPTAEYEE TEQKMGGVLD AVRRIEYGTE EASQ
