TRPE2_HALMA
ID TRPE2_HALMA Reviewed; 536 AA.
AC Q5V213;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=rrnAC1518;
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}.
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DR EMBL; AY596297; AAV46439.1; -; Genomic_DNA.
DR RefSeq; WP_011223672.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V213; -.
DR SMR; Q5V213; -.
DR STRING; 272569.rrnAC1518; -.
DR EnsemblBacteria; AAV46439; AAV46439; rrnAC1518.
DR GeneID; 40152480; -.
DR KEGG; hma:rrnAC1518; -.
DR PATRIC; fig|272569.17.peg.2207; -.
DR eggNOG; arCOG02014; Archaea.
DR HOGENOM; CLU_006493_9_0_2; -.
DR OMA; HARFSFV; -.
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; 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..536
FT /note="Anthranilate synthase component 1 2"
FT /id="PRO_0000154123"
FT BINDING 59
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 299..301
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 334..335
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 449
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 469
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 487..489
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 489
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 502
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
SQ SEQUENCE 536 AA; 58526 MW; B6E6E61722F155A4 CRC64;
MTLDISREEF VEHAKADRPV VVRTAAELDV DVEPLTAYAA LTGRTSDVAA NDYTFLLESA
EKVASSDPDG AFAPETDDRH ARFSFVGYDP RAVVTVTGDE SEVEAFDDRY ADLVTTDGGD
VVDDLRAAMP DVALRNFPAM DRQHLEGGLV GFLSYDAVYD LWLDEVGLDR PDSRFPDAQF
VLTTSTVRFD HVEDTVSLVF TPVVRQGEDA GERYGELVAE AERVEAVLSD LSPLSTGGFR
REDEVAGPRD EYEDAVERAK EYVLSGDIYQ GVISRTRELY GDVDPLGFYE ALRAVNPSPY
MYLLGYDDLT IVGASPETLV SVAGDHVVSN PIAGTCPRGN SPVEDRRLAG EMLADGKERA
EHTMLVDLAR NDVRRVAEAG SVRVPEFMNV LKYSHVQHIE STVTGRLAED KDAFDAARAT
FPAGTLSGAP KIRAMEIIDE LERSPRGPYG GGVGYFDWDG DTDFAIVIRS ATVEDEGDRD
RITVQAGAGI VADSDPESEY VETEQKMDGV LTALEEIEGE PVDVAERAAG HEEVTR
