ID C71C1_MAIZE Reviewed; 535 AA.
AC Q43250; Q43254;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=3-hydroxyindolin-2-one monooxygenase;
DE EC=1.14.14.109 {ECO:0000269|PubMed:11393516, ECO:0000269|PubMed:9235894};
DE AltName: Full=Cytochrome P450 71C1;
DE AltName: Full=Protein benzoxazineless 4;
GN Name=CYP71C1; Synonyms=BX4;
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 [GENOMIC DNA / 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 FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN [3]
RP CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=11393516; DOI=10.1016/s0031-9422(01)00037-1;
RA Spiteller P., Glawischnig E., Gierl A., Steglich W.;
RT "Studies on the biosynthesis of 2-hydroxy-1,4-benzoxazin-3-one (HBOA) from
RT 3-hydroxyindolin-2-one in Zea mays.";
RL Phytochemistry 57:373-376(2001).
CC -!- FUNCTION: Catalyzes the conversion of 3-hydroxyindolin-2-one to 2-
CC hydroxy-1,4-benzoxazin-3-one (HBOA). {ECO:0000269|PubMed:9235894}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxyindolin-2-one + O2 + reduced [NADPH--hemoprotein
CC reductase] = 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:31927,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28536,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:63559;
CC EC=1.14.14.109; Evidence={ECO:0000269|PubMed:11393516,
CC 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 4/5.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; X81828; CAA57422.1; -; Genomic_DNA.
DR EMBL; X81827; CAA57421.1; -; mRNA.
DR PIR; T03258; T03258.
DR AlphaFoldDB; Q43250; -.
DR SMR; Q43250; -.
DR STRING; 4577.Q43250; -.
DR PaxDb; 4577-GRMZM2G172491_P01; -.
DR KEGG; ag:CAA57422; -.
DR MaizeGDB; 114044; -.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; Q43250; -.
DR BioCyc; MetaCyc:MONOMER-10171; -.
DR BRENDA; 1.14.14.109; 6752.
DR UniPathway; UPA00872; UER00850.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q43250; baseline and differential.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0036192; F:3-hydroxyindolin-2-one monooxygenase activity; IEA:UniProtKB-EC.
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 CDD; cd11072; CYP71-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR47956:SF4; CYTOCHROME P450 71A16-RELATED; 1.
DR PANTHER; PTHR47956; CYTOCHROME P450 71B11-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; NAD; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..535
FT /note="3-hydroxyindolin-2-one monooxygenase"
FT /id="PRO_0000052113"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 470
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"
FT CONFLICT 6
FT /note="G -> A (in Ref. 1; CAA57421)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="S -> C (in Ref. 1; CAA57421)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="V -> E (in Ref. 1; CAA57421)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="S -> G (in Ref. 1; CAA57421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 59716 MW; 77ADF6889FD6FCF5 CRC64;
MALEAGYDYL HVAVVQCTPT QAAAVLGVLL LLAIRLAAAA RSSSATSPKW KQHRLPPTPP
GKLPIIGHLH LIGSHPHVSF RDLHAKYGHN GLMLVQVGAV PTIVVSTPQA AEAVLRTHDH
VLASRPRNPV ADIIRYNSTD VAFAPYGVYW RTARKVVNTH LLSAKMVFSK RREREEEVRL
VVARIRDAAE ASPGTALDMT ELLGGYASDF VCRAVLGESH RKQGRNKLFR ELTETSAALL
GGFNVEDYFP KLADVDLFLR IICAKAKSVS KRWDSLFNEL LSEYALSGGK QGDHNSEDFV
HLLLSLQKDY GLTTDNIKGI LVNMFEAAIE TSFLVLEYSM SELMNNRHVL AKLQKEVRTA
TPDGRMVMEE DLSRMPYLKA TIKESMRIHP PAPFLLPHFS THDCEINGYT IPAGTRVIVN
AWALARDPTC WDKAEEFFPE RFLEQGRDAE VDMYGKDIRF VPFGAGRRIC AGATFAIATV
EIMLANLIYH FDWEMPAEME RTGAKVDMSD QFGMTLRRTQ KLYLVPRIPK CVSSS
//
