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C71C3_MAIZE
ID   C71C3_MAIZE             Reviewed;         535 AA.
AC   P93703; Q43256;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Cytochrome P450 71C3;
DE            EC=1.14.-.-;
DE   AltName: Full=Protein benzoxazineless 5;
GN   Name=CYP71C3; Synonyms=BX5;
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] OF 2-535.
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].
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 2-hydroxy-1,4-benzoxazin-3-one
CC       (HBOA) to 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA).
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 5/5.
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; X81830; CAA57424.2; -; mRNA.
DR   EMBL; Y11403; CAA72207.1; -; Genomic_DNA.
DR   PIR; T03246; T03246.
DR   PIR; T03260; T03260.
DR   AlphaFoldDB; P93703; -.
DR   SMR; P93703; -.
DR   STRING; 4577.GRMZM2G063756_P01; -.
DR   PaxDb; P93703; -.
DR   PRIDE; P93703; -.
DR   KEGG; ag:CAA72207; -.
DR   MaizeGDB; 299157; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   BioCyc; MetaCyc:MON-10172; -.
DR   UniPathway; UPA00872; UER00851.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P93703; 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: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   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..535
FT                   /note="Cytochrome P450 71C3"
FT                   /id="PRO_0000052115"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         475
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   535 AA;  60716 MW;  F92A696108E2ADAF CRC64;
     MALQAAYEYL QQAVGHGAWS STQTLTLLLI AVPTVLLLLA SLAKSTSSSG RGKPPLPPSP
     PGTLPIVGHL HHIGPQTHIS LQELVAKYGH NGFLFLRAGA VPTLIVSSPS AAEAVMRTHD
     HICASRPWSM ASHILRYNTC DVAFSPLGEY WQQTRKLMNT HLLSNKKVYS FRHGREEEVC
     LVVDNLREAA AKSPSTAVDM SEVLAAYTND VVSRSVLGST HRKKGRNTLF REMTMTNVDL
     LVGFNLEYYI PRWPLTDLLF RLVCWKVTRH LKRWDALLEE VIHEHVEMRK LSGDKEKESD
     DFIDIFLSRY EEYGFTMDNV KSLLMNVFEA AIETSYLVLE SAMAELMNHR RVMKKLQAEV
     RAYGAEKKLD MIREDDLSSL PYLKASMKEA LRLHPPGPLL LPHYSTADCQ IDGYHIPANP
     RVLVNGWAIG RDPAVWEKPE EFMPERFMRD GWDKSNSYSG QDFRYLPFGS GRRICPGANF
     GLATMEIMLA NLMYHFDWEV PNEKEDGCWK VSMDEKFGLM LRRNELLYLV PRASS
 
 
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