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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
 
 
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