ID A0A1F6RLV0_9BACT Unreviewed; 507 AA.
AC A0A1F6RLV0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 {ECO:0000256|RuleBase:RU364045};
GN ORFNames=A2255_01325 {ECO:0000313|EMBL:OGI21613.1};
OS Candidatus Melainabacteria bacterium RIFOXYA2_FULL_32_9.
OC Bacteria; Candidatus Melainabacteria.
OX NCBI_TaxID=1801611 {ECO:0000313|EMBL:OGI21613.1, ECO:0000313|Proteomes:UP000198209};
RN [1] {ECO:0000313|EMBL:OGI21613.1, ECO:0000313|Proteomes:UP000198209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGI21613.1}.
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DR EMBL; MFRQ01000058; OGI21613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6RLV0; -.
DR STRING; 1801611.A2255_01325; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000198209; Unassembled WGS sequence.
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; ANTHRANILATE SYNTHASE COMPONENT 1; 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 Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 33..177
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 233..488
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
SQ SEQUENCE 507 AA; 57135 MW; 560AFF0DB11A5809 CRC64;
MIEIFPAKKE LQKIISNSNN KYVIPIWCEI IADLETPVSA YYKVCKDKKY SFLLESVEGG
ESVGRYSFIG FDPLYILKSD LEETSIFNTL NKDTLMKADN PYDLLEKFLS SYSSVNYDIP
YSPGVVGYFS YDTIRHIEPT LNKEFNKIEE CHSFPEAYFM IAGSILAFDH VKHKIYVIVN
ALTDNKSDID KIYENSQVKI ESILSQLTVS HNLSPLNLTL EDTHQEISSN ISKEEWINAI
NAAKEHIKAG DIFQAVLSQR FCVERNNVEP FTIYRALRSI NPSPYLYYLD FNDFKIIGSS
PEIMVKCSSD RIAEIRPIAG TKKRGKTQEQ DLLLEEELLN DPKERAEHIM LVDLGRNDLG
KVCEYGSVKV NRLMAVEKFS HVQHIVSDVT GKLREDLGSV DLVKACFPAG TVSGAPKVRA
MEIIYNLEKS ARGPYAGCIG CFGFNNEVNT AITIRTMLVR DNKVFIQAGA GIVADSDPEL
EYQETQNKAA ALIQALSRLA NEKCSKV
//