ID A0A0H5BJR5_BLAVI Unreviewed; 502 AA.
AC A0A0H5BJR5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653, ECO:0000256|RuleBase:RU364045};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266, ECO:0000256|RuleBase:RU364045};
GN Name=trpE_1 {ECO:0000313|EMBL:CUU42047.1};
GN Synonyms=trpE {ECO:0000256|RuleBase:RU364045};
GN ORFNames=BV133_3143 {ECO:0000313|EMBL:BAS00737.1}, BVIRIDIS_10480
GN {ECO:0000313|EMBL:CUU42047.1};
OS Blastochloris viridis (Rhodopseudomonas viridis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Blastochloridaceae; Blastochloris.
OX NCBI_TaxID=1079 {ECO:0000313|EMBL:CUU42047.1, ECO:0000313|Proteomes:UP000065734};
RN [1] {ECO:0000313|EMBL:BAS00737.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 133 {ECO:0000313|EMBL:BAS00737.1};
RA Tsukatani Y., Hirose Y., Harada J., Misawa N., Mori K., Inoue K.,
RA Tamiaki H.;
RT "Complete Genome Sequence of the Bacteriochlorophyll b-Producing
RT Photosynthetic Bacterium Blastochloris viridis.";
RL Genome Announc. 3:e01006-15(2015).
RN [2] {ECO:0000313|EMBL:CUU42047.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1 {ECO:0000313|EMBL:CUU42047.1};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000065734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19567 / DSM 133 / F {ECO:0000313|Proteomes:UP000065734};
RX PubMed=26798090; DOI=10.1128/genomeA.01520-15;
RA Liu L.N., Faulkner M., Liu X., Huang F., Darby A.C., Hall N.;
RT "Revised genome sequence of the purple photosynthetic bacterium
RT Blastochloris viridis.";
RL Genome Announc. 4:0-0(2016).
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.
CC {ECO:0000256|RuleBase:RU364045}.
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 Evidence={ECO:0000256|ARBA:ARBA00000329,
CC ECO:0000256|RuleBase:RU364045};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU364045};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000256|ARBA:ARBA00004873,
CC ECO:0000256|RuleBase:RU364045}.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large alpha subunit (TrpE).
CC {ECO:0000256|ARBA:ARBA00011575, ECO:0000256|RuleBase:RU364045}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000256|ARBA:ARBA00009562, ECO:0000256|RuleBase:RU364045}.
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DR EMBL; AP014854; BAS00737.1; -; Genomic_DNA.
DR EMBL; LN907867; CUU42047.1; -; Genomic_DNA.
DR RefSeq; WP_055037184.1; NZ_LN907867.1.
DR AlphaFoldDB; A0A0H5BJR5; -.
DR STRING; 1079.BVIR_1603; -.
DR KEGG; bvr:BVIR_1603; -.
DR PATRIC; fig|1079.6.peg.1660; -.
DR OrthoDB; 9803598at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000065734; 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; Anthranilate synthase; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR006805; Anth_synth_I_N.
DR InterPro; IPR005256; Anth_synth_I_PabB.
DR InterPro; IPR015890; Chorismate_C.
DR NCBIfam; TIGR00564; trpE_most; 1.
DR PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR PANTHER; PTHR11236:SF48; ISOCHORISMATE SYNTHASE MENF; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; ADC synthase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU364045};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|RuleBase:RU364045};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU364045};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364045};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364045};
KW Reference proteome {ECO:0000313|Proteomes:UP000065734};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 26..171
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 228..480
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
SQ SEQUENCE 502 AA; 53887 MW; A9EAE312B7F5B887 CRC64;
MLKIEPDVDA FPTDRPTVVW ATLVADLETP VSAFLKLAEG RPNAVLLESV EGGAVRGRYS
ILALAPDVIW RCQGAVAAIN RHALTAPDAF EPCAEPPLEA LRALIAESAI ELPPGLPPMA
AGIFGYLGYD MVRLMEKLAP AKPDPIGVPD AILVRPTIVV VFDAVRDEIT VVTPVRPAPG
GTPRQAYDRA VDRLTEIVER LDAPLDKTTP AADPGALTAE LTSNTTPAEY HAMVAKAKEY
ILAGDIFQVV LAQRFEAPFT LPPFALYRAL RRVNPAPFLV YLSFDDFSLV CSSPEILVRL
REGKVTIRPI AGTRPRGSTP AEDHALEAEL LADPKELSEH LMLLDLGRND VGRVSAIGTV
TVTDKFFIER YSHVMHIVSN VEGTLDSKQD ALDALIAGFP AGTVSGAPKV RAMQIIDELE
KDKRGPYAGA IGYFGAGGDM DSCIVLRTSV VKDGRMYVQA GAGIVHDSVP ASEQAECVNK
AKAQFRAADE ARRFAASVGR GQ
//
