AROC_NEUCR
ID AROC_NEUCR Reviewed; 432 AA.
AC Q12640; Q7SC33; Q9P3J3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Chorismate synthase;
DE EC=4.2.3.5;
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase;
GN Name=aro-2; ORFNames=B7F21.10, NCU05420;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7657620; DOI=10.1074/jbc.270.35.20447;
RA Henstrand J.M., Amrhein N., Schmid J.;
RT "Cloning and characterization of a heterologously expressed bifunctional
RT chorismate synthase/flavin reductase from Neurospora crassa.";
RL J. Biol. Chem. 270:20447-20452(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Bifunctional enzyme that possesses chorismate synthase and
CC intrinsic flavin reductase activity, it uses NADPH to reduce FMN.
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 -!- COFACTOR:
CC Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 7/7.
CC -!- SIMILARITY: Belongs to the chorismate synthase family. {ECO:0000305}.
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DR EMBL; U25818; AAC49056.1; -; mRNA.
DR EMBL; AL389901; CAB97473.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA34007.1; -; Genomic_DNA.
DR PIR; T46725; T46725.
DR RefSeq; XP_963243.1; XM_958150.3.
DR AlphaFoldDB; Q12640; -.
DR SMR; Q12640; -.
DR STRING; 5141.EFNCRP00000006557; -.
DR EnsemblFungi; EAA34007; EAA34007; NCU05420.
DR GeneID; 3879391; -.
DR KEGG; ncr:NCU05420; -.
DR VEuPathDB; FungiDB:NCU05420; -.
DR HOGENOM; CLU_034547_0_1_1; -.
DR InParanoid; Q12640; -.
DR OMA; MLSINAV; -.
DR BRENDA; 4.2.3.5; 3627.
DR SABIO-RK; Q12640; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR CDD; cd07304; Chorismate_synthase; 1.
DR Gene3D; 3.60.150.10; -; 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 PANTHER; PTHR21085; PTHR21085; 1.
DR Pfam; PF01264; Chorismate_synt; 1.
DR PIRSF; PIRSF001456; Chorismate_synth; 1.
DR SUPFAM; SSF103263; SSF103263; 1.
DR TIGRFAMs; TIGR00033; aroC; 1.
DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Multifunctional enzyme; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..432
FT /note="Chorismate synthase"
FT /id="PRO_0000140702"
FT REGION 406..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 260..291
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT CONFLICT 89
FT /note="R -> P (in Ref. 1; AAC49056)"
FT /evidence="ECO:0000305"
FT CONFLICT 147..148
FT /note="LA -> PR (in Ref. 1; AAC49056)"
FT /evidence="ECO:0000305"
FT CONFLICT 393..394
FT /note="QQ -> HE (in Ref. 1; AAC49056)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="H -> V (in Ref. 1; AAC49056)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 45985 MW; C81DAA2FFA53A8CE CRC64;
MSTFGHYFRV TTYGESHCKS VGCIVDGVPP GMELTEDDIQ PQMTRRRPGQ SAITTPRDEK
DRVIIQSGTE FGVTLGTPIG MLVMNEDQRP KDYGNKTMDI YPRPSHADWT YLEKYGVKAS
SGGGRSSARE TIGRVAAGAI AEKYLKLAYG VEIVAFVSSV GSEHLFPPTA EHPSPSTNPE
FLKLVNSITR ETVDSFLPVR CPDAEANKRM EDLITKFRDN HDSIGGTVTC VIRNVPSGLG
EPAFDKLEAM LAHAMLSIPA TKGFEVGSGF GGCEVPGSIH NDPFVSAENT EIPPSVAASG
AARNGIPRPK LTTKTNFSGG IQGGISNGAP IYFRVGFKPA ATIGQEQTTA TYDGTSEGVL
AAKGRHDPSV VPRAVPIVEA MAALVIMDAV LAQQARHTAK SLLPPLKQTI NSGKDTVGNG
VSENVQESDL AQ