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Database: UniProt
Entry: Q4WJ77_ASPFU
LinkDB: Q4WJ77_ASPFU
Original site: Q4WJ77_ASPFU 
ID   Q4WJ77_ASPFU            Unreviewed;       412 AA.
AC   Q4WJ77;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=AFUA_1G06940 {ECO:0000313|EMBL:EAL88405.1};
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL88405.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL88405.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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}.
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:EAL88405.1}.
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DR   EMBL; AAHF01000007; EAL88405.1; -; Genomic_DNA.
DR   RefSeq; XP_750443.1; XM_745350.1.
DR   AlphaFoldDB; Q4WJ77; -.
DR   STRING; 330879.Q4WJ77; -.
DR   EnsemblFungi; EAL88405; EAL88405; AFUA_1G06940.
DR   GeneID; 3507702; -.
DR   KEGG; afm:AFUA_1G06940; -.
DR   VEuPathDB; FungiDB:Afu1g06940; -.
DR   eggNOG; KOG4492; Eukaryota.
DR   HOGENOM; CLU_034547_0_1_1; -.
DR   InParanoid; Q4WJ77; -.
DR   OMA; NAVKGFE; -.
DR   OrthoDB; 275401at2759; -.
DR   UniPathway; UPA00053; UER00090.
DR   PHI-base; PHI:7654; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004107; F:chorismate synthase activity; IBA:GO_Central.
DR   GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR   GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IEA:EnsemblFungi.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
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:UP000002530}.
FT   REGION          41..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  44186 MW;  BB822B957FD92C76 CRC64;
     MSTWGEYFRV TTYGESHCRS VGCIVDGCPP GMELTEEDIQ PQMTRRRPGQ SALTTPRNEK
     DRVEIQSGTE FGITLGTPIG MMVRNEDQRP KDYGGSTMDL YPRPSHADYT YLEKYGVKAS
     SGGGRSSARE TIGRVAAGAI AEKYLRLSHG VEIVAFVSSV GNEHLFPPTP EHPSPSTNPE
     FLKLIETIDR KTVDAFVPTR CPNEEAAARM TKVIETFRDN QDSIGGTVTC VIRNVPVGLG
     EPCFDKLEAK LAHAMLSIPA TKGFEIGSGF GGCEVPGSIH NDPFTVSEVQ TRTGSTQRLT
     TKTNNSGGIQ GGISNGAPIY FRVAFKPPAT IGQAQTTASY SFEEGILEAK GRHDPCVTPR
     AVPIVEAMSA LVVMDALMAQ YARESAKNLL PPLPSTLPTK PTLGSSGAPA SS
//
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