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C71C4_MAIZE
ID   C71C4_MAIZE             Reviewed;         538 AA.
AC   Q43257; O04990;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=indole-2-monooxygenase;
DE            EC=1.14.14.153 {ECO:0000269|PubMed:9235894};
DE   AltName: Full=Cytochrome P450 71C4;
DE   AltName: Full=Protein benzoxazineless 2;
GN   Name=CYP71C4; Synonyms=BX2;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. CI31A;
RX   PubMed=7823905; DOI=10.1007/bf00290138;
RA   Frey M., Kliem R., Saedler H., Gierl A.;
RT   "Expression of a cytochrome P450 gene family in maize.";
RL   Mol. Gen. Genet. 246:100-109(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=cv. CI31A;
RX   PubMed=9235894; DOI=10.1126/science.277.5326.696;
RA   Frey M., Chomet P., Glawischnig E., Stettner C., Grun S., Winklmair A.,
RA   Eisenreich W., Bacher A., Meeley R.B., Briggs S.P., Simcox K., Gierl A.;
RT   "Analysis of a chemical plant defense mechanism in grasses.";
RL   Science 277:696-699(1997).
CC   -!- FUNCTION: Catalyzes the conversion of indole to indolin-2-one.
CC       {ECO:0000269|PubMed:9235894}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=indole + O2 + reduced [NADPH--hemoprotein reductase] = H(+) +
CC         H2O + indolin-2-one + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:31899, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16881, ChEBI:CHEBI:31697, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.153;
CC         Evidence={ECO:0000269|PubMed:9235894};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; 2,4-dihydroxy-1,4-
CC       benzoxazin-3-one biosynthesis; 2,4-dihydroxy-1,4-benzoxazin-3-one from
CC       indoleglycerol phosphate: step 2/5.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; X81831; CAA57425.1; -; mRNA.
DR   EMBL; Y11368; CAA72196.1; -; Genomic_DNA.
DR   PIR; T03262; T03262.
DR   AlphaFoldDB; Q43257; -.
DR   SMR; Q43257; -.
DR   STRING; 4577.GRMZM2G085661_P01; -.
DR   PaxDb; Q43257; -.
DR   PRIDE; Q43257; -.
DR   KEGG; ag:CAA72196; -.
DR   MaizeGDB; 299155; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   BioCyc; MetaCyc:MON-10169; -.
DR   BRENDA; 1.14.14.153; 6752.
DR   UniPathway; UPA00872; UER00848.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q43257; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0036190; F:indole-2-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..538
FT                   /note="indole-2-monooxygenase"
FT                   /id="PRO_0000052116"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         481
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   538 AA;  60048 MW;  D2F8CC0E62891D46 CRC64;
     MAAQLHHALY ELLHEAAAAQ RALLLAIPFS LLLLPLLLRY LAASASASAT KNDGAAPASD
     PDKLLSLLPS PPMKLPIIGH LHLMGDIPYV SLAALATRYG PDLMLLRLGA VPTVVVSSPR
     VAEAVLRTYD HVFSSRPRSL VSDIIMYGAT DSCFAPYGDH FRKARKLVTV HLLNASKVRS
     QRPAREEEVR GALDRVRRAA AAREPVDMSE LLHSFVNNLV CRAVSGKFSM EEGRNRLFRE
     LTDINAGLLG GFHIQDYFPR LGRIELVRKV ACAKTRRVRK RWDDLLDKLI DDHAARMATH
     QDEDDDKDFI YVLLSLQKEY GLTRDHIKAI LIDMFEAGTD TSYMTLEFAM TELIRKPHLM
     KKLQEEVRRN VPAGQEMVTE DNLPGMTDLK AVIKETLRLH PPVPLLLPHY SLDACEVAGY
     TIPANTRVVV NAWALGRHSG YWERENEFVP ERFLSGDVAG GVDLKPNEFQ FLAFGSGRRM
     CPGVHSASAT IEAMLSNLMY RFDWQLPAGM KAEDVDMTEV FGITVSRKEK LLLVPQAA
 
 
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