C79B3_ARATH
ID C79B3_ARATH Reviewed; 543 AA.
AC Q501D8; Q0WMS4; Q9SK00;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Tryptophan N-monooxygenase 2;
DE EC=1.14.14.156 {ECO:0000269|PubMed:10681464};
DE AltName: Full=Cytochrome P450 79B3;
DE AltName: Full=Tryptophan N-hydroxylase 2;
GN Name=CYP79B3; OrderedLocusNames=At2g22330; ORFNames=T26C19.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10681464; DOI=10.1073/pnas.040569997;
RA Hull A.K., Vij R., Celenza J.L.;
RT "Arabidopsis cytochrome P450s that catalyze the first step of tryptophan-
RT dependent indole-3-acetic acid biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2379-2384(2000).
CC -!- FUNCTION: Converts tryptophan to indole-3-acetaldoxime, a precursor for
CC tryptophan derived glucosinolates and indole-3-acetic acid (IAA).
CC {ECO:0000269|PubMed:10681464}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan + 2 O2 + 2 reduced [NADPH--hemoprotein reductase]
CC = (E)-(indol-3-yl)acetaldehyde oxime + CO2 + 2 H(+) + 3 H2O + 2
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:33279,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17545, ChEBI:CHEBI:57618, ChEBI:CHEBI:57912,
CC ChEBI:CHEBI:58210; EC=1.14.14.156;
CC Evidence={ECO:0000269|PubMed:10681464};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD22364.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM15431.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006592; AAD22364.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC007168; AAM15431.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC07294.1; -; Genomic_DNA.
DR EMBL; BT022029; AAY25441.1; -; mRNA.
DR EMBL; AK229739; BAF01576.1; -; mRNA.
DR PIR; D84611; D84611.
DR RefSeq; NP_001323954.1; NM_001335798.1.
DR RefSeq; NP_179820.2; NM_127798.4.
DR AlphaFoldDB; Q501D8; -.
DR SMR; Q501D8; -.
DR STRING; 3702.AT2G22330.1; -.
DR PaxDb; Q501D8; -.
DR PRIDE; Q501D8; -.
DR ProteomicsDB; 239171; -.
DR EnsemblPlants; AT2G22330.1; AT2G22330.1; AT2G22330.
DR GeneID; 816765; -.
DR Gramene; AT2G22330.1; AT2G22330.1; AT2G22330.
DR KEGG; ath:AT2G22330; -.
DR Araport; AT2G22330; -.
DR TAIR; locus:2041293; AT2G22330.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q501D8; -.
DR OMA; TAITVMM; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q501D8; -.
DR BioCyc; ARA:AT2G22330-MON; -.
DR BioCyc; MetaCyc:AT2G22330-MON; -.
DR BRENDA; 1.14.14.156; 399.
DR PRO; PR:Q501D8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q501D8; baseline and differential.
DR Genevisible; Q501D8; AT.
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 GO; GO:0010120; P:camalexin biosynthetic process; TAS:TAIR.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0002229; P:defense response to oomycetes; IGI:TAIR.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; TAS:TAIR.
DR GO; GO:0009684; P:indoleacetic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009682; P:induced systemic resistance; IMP:TAIR.
DR GO; GO:0010112; P:regulation of systemic acquired resistance; IEP:TAIR.
DR GO; GO:0009617; P:response to bacterium; IMP:TAIR.
DR GO; GO:0009625; P:response to insect; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0006569; P:tryptophan catabolic process; IDA:TAIR.
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; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..543
FT /note="Tryptophan N-monooxygenase 2"
FT /id="PRO_0000350735"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 479
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|UniProtKB:Q96242"
FT CONFLICT 326
FT /note="D -> N (in Ref. 4; BAF01576)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="E -> G (in Ref. 4; BAF01576)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="N -> Y (in Ref. 4; BAF01576)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 61438 MW; 84E5DF567BEE0862 CRC64;
MDTLASNSSD LTTKSSLGMS SFTNMYLLTT LQALAALCFL MILNKIKSSS RNKKLHPLPP
GPTGFPIVGM IPAMLKNRPV FRWLHSLMKE LNTEIACVRL GNTHVIPVTC PKIAREIFKQ
QDALFASRPL TYAQKILSNG YKTCVITPFG EQFKKMRKVI MTEIVCPARH RWLHDNRAEE
TDHLTAWLYN MVKNSEPVDL RFVTRHYCGN AIKRLMFGTR TFSEKTEADG GPTLEDIEHM
DAMFEGLGFT FAFCISDYLP MLTGLDLNGH EKIMRESSAI MDKYHDPIID ERIKMWREGK
RTQIEDFLDI FISIKDEAGQ PLLTADEIKP TIKELVMAAP DNPSNAVEWA IAEMINKPEI
LHKAMEEIDR VVGKERFVQE SDIPKLNYVK AIIREAFRLH PVAAFNLPHV ALSDTTVAGY
HIPKGSQVLL SRYGLGRNPK VWSDPLSFKP ERHLNECSEV TLTENDLRFI SFSTGKRGCA
APALGTAITT MMLARLLQGF KWKLAGSETR VELMESSHDM FLSKPLVLVG ELRLSEDLYP
MVK
