C83A1_ARATH
ID C83A1_ARATH Reviewed; 502 AA.
AC P48421; O24429;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Cytochrome P450 83A1;
DE EC=1.14.14.43 {ECO:0000269|PubMed:12970475};
DE AltName: Full=CYPLXXXIII;
DE AltName: Full=Protein REDUCED EPIDERMAL FLUORESCENCE 2 {ECO:0000303|PubMed:12509530};
GN Name=CYP83A1; Synonyms=CYP83, REF2 {ECO:0000303|PubMed:12509530};
GN OrderedLocusNames=At4g13770; ORFNames=F18A5.160;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=7610196; DOI=10.1104/pp.108.2.875;
RA Chapple C.C.S.;
RT "A cDNA encoding a novel cytochrome P450-dependent monooxygenase from
RT Arabidopsis thaliana.";
RL Plant Physiol. 108:875-876(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=9620263; DOI=10.1023/a:1005921406884;
RA Mizutani M., Ward E., Ohta D.;
RT "Cytochrome P450 superfamily in Arabidopsis thaliana: isolation of cDNAs,
RT differential expression, and RFLP mapping of multiple cytochromes P450.";
RL Plant Mol. Biol. 37:39-52(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. C24;
RA Bilodeau P., Udvardi M.K., Peacock W.J., Dennis E.S.;
RT "Molecular cloning and characterisation of a vernalisation-induced
RT cytochrome P450 gene from Arabidopsis thaliana.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12509530; DOI=10.1105/tpc.006544;
RA Hemm M.R., Ruegger M.O., Chapple C.;
RT "The Arabidopsis ref2 mutant is defective in the gene encoding CYP83A1 and
RT shows both phenylpropanoid and glucosinolate phenotypes.";
RL Plant Cell 15:179-194(2003).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12970475; DOI=10.1104/pp.102.019240;
RA Naur P., Petersen B.L., Mikkelsen M.D., Bak S., Rasmussen H., Olsen C.E.,
RA Halkier B.A.;
RT "CYP83A1 and CYP83B1, two nonredundant cytochrome P450 enzymes metabolizing
RT oximes in the biosynthesis of glucosinolates in Arabidopsis.";
RL Plant Physiol. 133:63-72(2003).
CC -!- FUNCTION: Involved in the metabolism of aliphatic and aromatic oximes
CC (PubMed:12970475). Involved in the biosynthesis of both short-chain and
CC long-chain aliphatic glucosinolates (PubMed:12509530).
CC {ECO:0000269|PubMed:12509530, ECO:0000269|PubMed:12970475}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (E)-omega-(methylsulfanyl)-alkanal oxime + glutathione + O2
CC + reduced [NADPH--hemoprotein reductase] = an S-[(1E)-1-
CC (hydroxyimino)-omega-(methylsulfanyl)alkyl]-L-glutathione + H(+) + 2
CC H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51992,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, Rhea:RHEA-COMP:13114,
CC Rhea:RHEA-COMP:13138, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:134680, ChEBI:CHEBI:136061;
CC EC=1.14.14.43; Evidence={ECO:0000269|PubMed:12970475};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=150 uM for indole-3-acetaldoxime {ECO:0000269|PubMed:12970475};
CC KM=156 uM for p-hydroxyphenylacetaldoxime
CC {ECO:0000269|PubMed:12970475};
CC KM=556 uM for phenylacetaldoxime {ECO:0000269|PubMed:12970475};
CC Note=kcat is 140 min(-1) with indole-3-acetaldoxime as substrate.
CC kcat is 26 min(-1) with p-hydroxyphenylacetaldoxime as substrate.
CC kcat is 25 min(-1) with phenylacetaldoxime as substrate.
CC {ECO:0000269|PubMed:12970475};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of all aliphatic glucosinolates
CC and increased levels of indole-derived glucosinolates in leaves.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; U18929; AAA79982.1; -; mRNA.
DR EMBL; D78599; BAA28532.1; -; mRNA.
DR EMBL; U69134; AAB71623.1; -; Genomic_DNA.
DR EMBL; AL035528; CAB36841.1; -; Genomic_DNA.
DR EMBL; AL161537; CAB78419.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83323.1; -; Genomic_DNA.
DR EMBL; AF428469; AAL16238.1; -; mRNA.
DR EMBL; AY075697; AAL77703.1; -; mRNA.
DR EMBL; AY102146; AAM26713.1; -; mRNA.
DR PIR; T05246; T05246.
DR RefSeq; NP_193113.1; NM_117451.4.
DR AlphaFoldDB; P48421; -.
DR SMR; P48421; -.
DR BioGRID; 12308; 16.
DR IntAct; P48421; 12.
DR STRING; 3702.AT4G13770.1; -.
DR PaxDb; P48421; -.
DR PRIDE; P48421; -.
DR ProteomicsDB; 240583; -.
DR EnsemblPlants; AT4G13770.1; AT4G13770.1; AT4G13770.
DR GeneID; 827011; -.
DR Gramene; AT4G13770.1; AT4G13770.1; AT4G13770.
DR KEGG; ath:AT4G13770; -.
DR Araport; AT4G13770; -.
DR TAIR; locus:2119500; AT4G13770.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_1_1; -.
DR InParanoid; P48421; -.
DR OMA; QIDGDKW; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P48421; -.
DR BioCyc; ARA:AT4G13770-MON; -.
DR BioCyc; MetaCyc:AT4G13770-MON; -.
DR BRENDA; 1.14.14.43; 399.
DR SABIO-RK; P48421; -.
DR PRO; PR:P48421; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P48421; baseline and differential.
DR Genevisible; P48421; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IDA:TAIR.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IDA:TAIR.
DR GO; GO:0009625; P:response to insect; IEP: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 Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..502
FT /note="Cytochrome P450 83A1"
FT /id="PRO_0000052166"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 442
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 277
FT /note="K -> T (in Ref. 1; AAA79982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 57449 MW; 7A0F6F36FD5D7577 CRC64;
MEDIIIGVVA LAAVLLFFLY QKPKTKRYKL PPGPSPLPVI GNLLQLQKLN PQRFFAGWAK
KYGPILSYRI GSRTMVVISS AELAKELLKT QDVNFADRPP HRGHEFISYG RRDMALNHYT
PYYREIRKMG MNHLFSPTRV ATFKHVREEE ARRMMDKINK AADKSEVVDI SELMLTFTNS
VVCRQAFGKK YNEDGEEMKR FIKILYGTQS VLGKIFFSDF FPYCGFLDDL SGLTAYMKEC
FERQDTYIQE VVNETLDPKR VKPETESMID LLMGIYKEQP FASEFTVDNV KAVILDIVVA
GTDTAAAAVV WGMTYLMKYP QVLKKAQAEV REYMKEKGST FVTEDDVKNL PYFRALVKET
LRIEPVIPLL IPRACIQDTK IAGYDIPAGT TVNVNAWAVS RDEKEWGPNP DEFRPERFLE
KEVDFKGTDY EFIPFGSGRR MCPGMRLGAA MLEVPYANLL LSFNFKLPNG MKPDDINMDV
MTGLAMHKSQ HLKLVPEKVN KY
