ID   C71C2_MAIZE             Reviewed;         536 AA.
AC   Q43255; O04991;
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=indolin-2-one monooxygenase;
DE            EC=1.14.14.157 {ECO:0000269|PubMed:9235894};
DE   AltName: Full=Cytochrome P450 71C2;
DE   AltName: Full=Protein benzoxazineless 3;
GN   Name=CYP71C2; Synonyms=BX3;
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 indolin-2-one to 3-
CC       hydroxyindolin-2-one. {ECO:0000269|PubMed:9235894}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=indolin-2-one + O2 + reduced [NADPH--hemoprotein reductase] =
CC         3-hydroxyindolin-2-one + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:31919, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:28536, ChEBI:CHEBI:31697, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.157;
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 3/5.
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; X81829; CAA57423.1; -; mRNA.
DR   EMBL; Y11404; CAA72208.1; -; Genomic_DNA.
DR   PIR; T03034; T03034.
DR   AlphaFoldDB; Q43255; -.
DR   SMR; Q43255; -.
DR   STRING; 4577.GRMZM2G167549_P05; -.
DR   PaxDb; Q43255; -.
DR   PRIDE; Q43255; -.
DR   KEGG; ag:CAA72208; -.
DR   MaizeGDB; 136233; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   BioCyc; MetaCyc:MON-10170; -.
DR   BRENDA; 1.14.14.157; 6752.
DR   UniPathway; UPA00872; UER00849.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q43255; 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:0036191; F:indolin-2-one 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; NAD; NADP;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..536
FT                   /note="indolin-2-one monooxygenase"
FT                   /id="PRO_0000052114"
FT   TRANSMEM        18..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         480
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   536 AA;  59783 MW;  570240076BD9384F CRC64;
     MALGAAYHHY LQLAGDHGTA THALLLGVLI FLVIRLVSAR RTGTTSANKR KQQQRLPLPP
     WPPGKLPIIG HLHLIGAETH ISIRDLDAKH GRNGLLLLRI GAVPTLFVSS PSAADAVLRT
     QDHIFASRPP WMAAEIIRYG PSDVAFVPYG EYGRQGRKLL TTHMLSTKKV QSFRHGRQEE
     VRLVMDKIRA AATAAPPAAV DLSDLLSGYT NDVVSRAVLG ASHRNQGRNR LFSELTEINV
     SLLAGFNLED YFPPNMAMAD VLLRLVSVKA RRLNQRWNDV FDELIQEHVQ SRPSGESEES
     EADFIHVLLS IQQEYGLTTD NLKAILVDMF EAGIETSYLT LEYGMAELIN NRHVMEKLQT
     EVRTTMGSPD GKKLDMLAEE DLGSMPYLKA TIKETLRLHP PAPFLLPHYS TADSEIDGYF
     VPAGTRVLVH AWALGRDRTT WEKPEEFMPE RFVQEPGAVD VHMKGKDLRF IPFGSGRRIC
     PGMNFGFATM EVMLANLMYH FDWEVPGSGA GVSMEESFGL TLRRKEKLLL VPRIAS