C82C2_ARATH
ID C82C2_ARATH Reviewed; 523 AA.
AC O49394; A0MFB5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Xanthotoxin 5-hydroxylase CYP82C2 {ECO:0000305|PubMed:18291319};
DE Short=8-methoxypsoralen 5-hydroxylase CYP82C2 {ECO:0000303|PubMed:18291319};
DE EC=1.14.14.- {ECO:0000269|PubMed:18291319};
DE AltName: Full=Cytochrome P450 82C2 {ECO:0000303|PubMed:18291319};
DE AltName: Full=Indole-3-carbonyl nitrile 4-hydroxylase CYP82C2;
DE EC=1.14.14.165 {ECO:0000269|PubMed:26352477};
GN Name=CYP82C2 {ECO:0000303|PubMed:18291319};
GN OrderedLocusNames=At4g31970 {ECO:0000312|Araport:AT4G31970};
GN ORFNames=F10N7.220 {ECO:0000312|EMBL:CAA16592.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18291319; DOI=10.1016/j.chembiol.2008.01.008;
RA Kruse T., Ho K., Yoo H.D., Johnson T., Hippely M., Park J.H., Flavell R.,
RA Bobzin S.;
RT "In planta biocatalysis screen of P450s identifies 8-methoxypsoralen as a
RT substrate for the CYP82C subfamily, yielding original chemical
RT structures.";
RL Chem. Biol. 15:149-156(2008).
RN [5]
RP FUNCTION, INDUCTION BY PATHOGEN, DISRUPTION PHENOTYPE, AND CATALYTIC
RP ACTIVITY.
RX PubMed=26352477; DOI=10.1038/nature14907;
RA Rajniak J., Barco B., Clay N.K., Sattely E.S.;
RT "A new cyanogenic metabolite in Arabidopsis required for inducible pathogen
RT defence.";
RL Nature 525:376-379(2015).
CC -!- FUNCTION: Involved in the biosynthetic pathway to 4-hydroxyindole-3-
CC carbonyl nitrile (4-OH-ICN), a cyanogenic metabolite required for
CC inducible pathogen defense. Converts indole-3-carbonyl nitrile (ICN)
CC into 4-OH-ICN (PubMed:26352477). Can hydroxylate xanthotoxin (8-
CC methoxypsoralen) to form 5-hydroxyxanthotoxin (5-hydroxy-8-
CC methoxypsoralen) in vivo and in vitro (PubMed:18291319).
CC {ECO:0000269|PubMed:18291319, ECO:0000269|PubMed:26352477}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + xanthotoxin = 5-
CC hydroxyxanthotoxin + 2 H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:58064, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18358, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:78326; Evidence={ECO:0000269|PubMed:18291319};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=indole-3-carbonyl nitrile + O2 + reduced [NADPH--hemoprotein
CC reductase] = 4-hydroxy-indole-3-carbonyl nitrile + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:57864,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:142138, ChEBI:CHEBI:142139;
CC EC=1.14.14.165; Evidence={ECO:0000269|PubMed:26352477};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated upon pathogen infection.
CC {ECO:0000269|PubMed:26352477}.
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to virulent Pseudomonas
CC syringae. {ECO:0000269|PubMed:26352477}.
CC -!- MISCELLANEOUS: Plants overexpressing CYP82C2, can hydroxylate and
CC subsequently glycosylate 8-methoxypsoralen.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28662.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL021636; CAA16592.1; -; Genomic_DNA.
DR EMBL; AL161580; CAB79915.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85984.1; -; Genomic_DNA.
DR EMBL; DQ653241; ABK28662.1; ALT_SEQ; mRNA.
DR PIR; T04648; T04648.
DR RefSeq; NP_194925.1; NM_119348.2.
DR AlphaFoldDB; O49394; -.
DR SMR; O49394; -.
DR STRING; 3702.AT4G31970.1; -.
DR PaxDb; O49394; -.
DR PRIDE; O49394; -.
DR ProteomicsDB; 239143; -.
DR EnsemblPlants; AT4G31970.1; AT4G31970.1; AT4G31970.
DR GeneID; 829327; -.
DR Gramene; AT4G31970.1; AT4G31970.1; AT4G31970.
DR KEGG; ath:AT4G31970; -.
DR Araport; AT4G31970; -.
DR TAIR; locus:2116652; AT4G31970.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; O49394; -.
DR OMA; EARQCRK; -.
DR OrthoDB; 871849at2759; -.
DR PhylomeDB; O49394; -.
DR BioCyc; ARA:AT4G31970-MON; -.
DR BioCyc; MetaCyc:AT4G31970-MON; -.
DR BRENDA; 1.14.14.165; 399.
DR PRO; PR:O49394; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49394; baseline and differential.
DR Genevisible; O49394; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0106149; F:indole-3-carbonyl nitrile 4-hydroxylase activity; IDA:TAIR.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:TAIR.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0098542; P:defense response to other organism; 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..523
FT /note="Xanthotoxin 5-hydroxylase CYP82C2"
FT /id="PRO_0000411197"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 462
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:P04798"
SQ SEQUENCE 523 AA; 59002 MW; 0FE5D79217DFDAA9 CRC64;
MDTSLFSLFV PILVFVFIAL FKKSKKPKHV KAPAPSGAWP IIGHLHLLSG KEQLLYRTLG
KMADQYGPAM SLRLGSSETF VVSSFEVAKD CFTVNDKALA SRPITAAAKH MGYDCAVFGF
APYSAFWREM RKIATLELLS NRRLQMLKHV RVSEISMVMQ DLYSLWVKKG GSEPVMVDLK
SWLEDMSLNM MVRMVAGKRY FGGGSLSPED AEEARQCRKG VANFFHLVGI FTVSDAFPKL
GWFDFQGHEK EMKQTGRELD VILERWIENH RQQRKVSGTK HNDSDFVDVM LSLAEQGKFS
HLQHDAITSI KSTCLALILG GSETSPSTLT WAISLLLNNK DMLKKAQDEI DIHVGRDRNV
EDSDIENLVY IQAIIKETLR LYPAGPLLGH REAIEDCTVA GYNVRRGTRM LVNVWKIQRD
PRVYMEPNEF RPERFITGEA KEFDVRGQNF ELMPFGSGRR SCPGSSLAMQ VLHLGLARFL
QSFDVKTVMD MPVDMTESPG LTIPKATPLE ILISPRLKEG LYV
