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Database: UniProt
Entry: A0A0N7Z4W8_9CYAN
LinkDB: A0A0N7Z4W8_9CYAN
Original site: A0A0N7Z4W8_9CYAN 
ID   A0A0N7Z4W8_9CYAN        Unreviewed;       508 AA.
AC   A0A0N7Z4W8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=NIES2104_38120 {ECO:0000313|EMBL:GAP97265.1};
OS   Leptolyngbya sp. NIES-2104.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya.
OX   NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAP97265.1, ECO:0000313|Proteomes:UP000052243};
RN   [1] {ECO:0000313|EMBL:GAP97265.1, ECO:0000313|Proteomes:UP000052243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2104 {ECO:0000313|EMBL:GAP97265.1,
RC   ECO:0000313|Proteomes:UP000052243};
RX   PubMed=26494835; DOI=10.1093/dnares/dsv022;
RA   Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H.,
RA   Kawachi M.;
RT   "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES-2104
RT   and the freshwater Leptolyngbya boryana PCC 6306 genomes.";
RL   DNA Res. 22:403-412(2015).
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:GAP97265.1}.
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DR   EMBL; BBWW01000001; GAP97265.1; -; Genomic_DNA.
DR   RefSeq; WP_058999525.1; NZ_BBWW01000001.1.
DR   AlphaFoldDB; A0A0N7Z4W8; -.
DR   STRING; 1552121.NIES2104_38120; -.
DR   InParanoid; A0A0N7Z4W8; -.
DR   OrthoDB; 9803598at2; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000052243; 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          28..169
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          230..495
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
SQ   SEQUENCE   508 AA;  56749 MW;  4A3E6CAFD319C2C0 CRC64;
     MISPDFSQFK QLAQQGNFVP VYQEWVADLD TPVSAWYRVC DGQPYSFLLE SVEGGETIGR
     YSFLGCDPLW VLEAKGDRTT QTHRDGTQQV FEGDPFAALS QCLAPYHPVK LPELPPGIGG
     LFGFWGYELI KWIEPRVPIY EATEDDLPDG LWMQIDQVLI FDQVKRKIWA IAYADLRDPN
     TDLETAYQQA CDRVSQLVSK LQSPLPEKTR LLSWQPNNDS AISWTSNTTK EQYCASVETA
     KAHIKAGDIF QVVISQQLNS EFIGEPFALY RSLRLINPSP YMGYFHFNNW QIIGSSPEVL
     VKAEQSIDPT EPKIATVRPI AGTRKRGKTH AEDLALEQDL LADPKEVAEH VMLVDLGRND
     LGRVCINGTV KVDELMVIER YSHVMHIVSN VIGQLSPDKT AWDLLKAGFP AGTVSGAPKI
     RAMEIIHTLE PCRRGVYSGA YGYYDFEGQL NSAIAIRTMV VRDQGNGKHR VQVQAGAGLV
     ADSVPESEYQ ETLNKARGLL EAIRCLQG
//
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