TRPE1_HALMA
ID TRPE1_HALMA Reviewed; 489 AA.
AC Q5V448;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=rrnAC0709;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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; AY596297; AAV45704.1; -; Genomic_DNA.
DR RefSeq; WP_011223185.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V448; -.
DR SMR; Q5V448; -.
DR STRING; 272569.rrnAC0709; -.
DR EnsemblBacteria; AAV45704; AAV45704; rrnAC0709.
DR GeneID; 40151744; -.
DR KEGG; hma:rrnAC0709; -.
DR PATRIC; fig|272569.17.peg.1454; -.
DR eggNOG; arCOG02014; Archaea.
DR HOGENOM; CLU_006493_9_3_2; -.
DR OMA; DCDVPYP; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000001169; Chromosome I.
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; 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..489
FT /note="Anthranilate synthase component 1 1"
FT /id="PRO_0000154122"
FT REGION 288..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 262..264
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 297..298
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 412
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 432
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 446..448
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
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 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
SQ SEQUENCE 489 AA; 53790 MW; 41533472289C120D CRC64;
MQSVETDRTT FTDLAADAHP AARVPVEVRV DVDDPFLAYR RARDETGGVY LATTGGQSGW
GYFGTAPADF REVDPRAGGT LAALTEFLDG ERLVRGDCDV PYPCGAVGWL SYDVARELES
LPDSADADRA LPNLQVARYD RFAAWEEPRG ESVTLRVTAC PRVDDFETPE LAYEFGKQHA
LDLARAAAQG DPSVEDPPVE TDEATFESDC TRESFADRVQ TVKQYIRDGD TFQANVSQRL
RAPAAVHPVE AFDALRTVNP APYSALLEFP GVDLVSASPE LLLHRDGDRI ETEPIAGTRP
RGETPDADDR LETDLLDDEK ERAEHAMLVD LERNDLGKVS KFGSVEVSDY RRVDRYSEVM
HLVSVVEGRL RDGASLQDAI AAVFPGGTIT GAPKPRTMEI IDEVEATRRG PYTGSIGLFG
FDGRATLNIV IRTLVRYAEE YHLRVGAGVV HDSDPDREYQ ETLDKGRALV NAVDEALGRR
VDLAMEDQQ
