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Database: UniProt
Entry: A0A1L9TIV1_9EURO
LinkDB: A0A1L9TIV1_9EURO
Original site: A0A1L9TIV1_9EURO 
ID   A0A1L9TIV1_9EURO        Unreviewed;       410 AA.
AC   A0A1L9TIV1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   08-NOV-2023, entry version 21.
DE   RecName: Full=Chorismate synthase {ECO:0000256|ARBA:ARBA00013036, ECO:0000256|RuleBase:RU000605};
DE            EC=4.2.3.5 {ECO:0000256|ARBA:ARBA00013036, ECO:0000256|RuleBase:RU000605};
GN   ORFNames=ASPSYDRAFT_199769 {ECO:0000313|EMBL:OJJ59358.1};
OS   Aspergillus sydowii CBS 593.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=1036612 {ECO:0000313|EMBL:OJJ59358.1, ECO:0000313|Proteomes:UP000184356};
RN   [1] {ECO:0000313|Proteomes:UP000184356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 593.65 {ECO:0000313|Proteomes:UP000184356};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate +
CC         phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5;
CC         Evidence={ECO:0000256|RuleBase:RU000605};
CC   -!- COFACTOR:
CC       Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC         Evidence={ECO:0000256|RuleBase:RU000605};
CC       Note=Reduced FMN (FMNH(2)). {ECO:0000256|RuleBase:RU000605};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       7/7. {ECO:0000256|ARBA:ARBA00005044, ECO:0000256|RuleBase:RU000605}.
CC   -!- SIMILARITY: Belongs to the chorismate synthase family.
CC       {ECO:0000256|ARBA:ARBA00008014, ECO:0000256|RuleBase:RU000605}.
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DR   EMBL; KV878585; OJJ59358.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9TIV1; -.
DR   STRING; 1036612.A0A1L9TIV1; -.
DR   VEuPathDB; FungiDB:ASPSYDRAFT_199769; -.
DR   OrthoDB; 275401at2759; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000184356; Unassembled WGS sequence.
DR   GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07304; Chorismate_synthase; 1.
DR   Gene3D; 3.60.150.10; Chorismate synthase AroC; 1.
DR   HAMAP; MF_00300; Chorismate_synth; 1.
DR   InterPro; IPR000453; Chorismate_synth.
DR   InterPro; IPR035904; Chorismate_synth_AroC_sf.
DR   InterPro; IPR020541; Chorismate_synthase_CS.
DR   NCBIfam; TIGR00033; aroC; 1.
DR   PANTHER; PTHR21085; CHORISMATE SYNTHASE; 1.
DR   PANTHER; PTHR21085:SF0; CHORISMATE SYNTHASE; 1.
DR   Pfam; PF01264; Chorismate_synt; 1.
DR   PIRSF; PIRSF001456; Chorismate_synth; 1.
DR   SUPFAM; SSF103263; Chorismate synthase, AroC; 1.
DR   PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR   PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR   PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU000605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|RuleBase:RU000605};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000605};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184356}.
FT   REGION          36..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   410 AA;  44176 MW;  F720DEA9759C5312 CRC64;
     MSTWGDYFRV TTYGESHCRS VGCIVDGCPP GMELTEDDIQ PQMTRRRPGQ SALTTPRNEK
     DRVEIQSGTE FGVTLGTPIG MVVRNEDQRP KDYGNKTMDM YPRPSHADFT YLEKYGVKAS
     SGGGRSSARE TIGRVAAGAI AEKYLRLSHG VEIIAFVSSV GNEHLFPATA EHPTPSTNPE
     FLNLIEKIDR KTVDAFVPTR CPSEDAAARM TKIIEHFRDN NDSIGGTVTC VIRNVPVGLG
     EPCFDKLEAQ LAHAMLSIPA TKGFEIGSGF GGCEVPGSIH NDPFVASEVQ TQLGSENTTK
     QRLTTKTNNS GGIQGGISNG ASIYFRVAFK PPATIGQAQQ TATYDLGDGV LEAKGRHDPC
     VVPRAVPIVE AMSALVVMDS LMAQYARESA KTLLPPLPKT IPTRPTTGTN
//
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