CP74A_ARATH
ID CP74A_ARATH Reviewed; 518 AA.
AC Q96242; P93720; Q9ZR51;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Allene oxide synthase, chloroplastic;
DE EC=4.2.1.92 {ECO:0000269|PubMed:8756596};
DE AltName: Full=Cytochrome P450 74A;
DE AltName: Full=Hydroperoxide dehydrase;
DE Flags: Precursor;
GN Name=CYP74A; Synonyms=AOS; OrderedLocusNames=At5g42650; ORFNames=MJB21.2;
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], CATALYTIC ACTIVITY, AND INDUCTION BY WOUNDING.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8756596; DOI=10.1007/bf00021793;
RA Laudert D., Pfannschmidt U., Lottspeich F., Hollanderczytko H.,
RA Weiler E.W.;
RT "Cloning, molecular and functional characterization of Arabidopsis thaliana
RT allene oxide synthase (CYP 74), the first enzyme of the octadecanoid
RT pathway to jasmonates.";
RL Plant Mol. Biol. 31:323-335(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10420644; DOI=10.1007/s004250050583;
RA Kubigsteltig I., Laudert D., Weiler E.W.;
RT "Structure and regulation of the Arabidopsis thaliana allene oxide synthase
RT gene.";
RL Planta 208:463-471(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Staswick P.E.;
RT "Sequence of an allene oxide synthase cDNA from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR99-130(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 CLEAVAGE OF TRANSIT PEPTIDE AFTER ALA-33, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Col-2;
RX PubMed=16414959; DOI=10.1074/jbc.m511939200;
RA Vidi P.-A., Kanwischer M., Baginsky S., Austin J.R., Csucs G., Doermann P.,
RA Kessler F., Brehelin C.;
RT "Tocopherol cyclase (VTE1) localization and vitamin E accumulation in
RT chloroplast plastoglobule lipoprotein particles.";
RL J. Biol. Chem. 281:11225-11234(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=16461379; DOI=10.1104/pp.105.076083;
RA Ytterberg A.J., Peltier J.-B., van Wijk K.J.;
RT "Protein profiling of plastoglobules in chloroplasts and chromoplasts. A
RT surprising site for differential accumulation of metabolic enzymes.";
RL Plant Physiol. 140:984-997(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 34-518 IN COMPLEX WITH HEME AND
RP SUBSTRATE ANALOGS, AND MUTAGENESIS OF PHE-137; SER-155 AND ASN-321.
RX PubMed=18716621; DOI=10.1038/nature07307;
RA Lee D.-S., Nioche P., Hamberg M., Raman C.S.;
RT "Structural insights into the evolutionary paths of oxylipin biosynthetic
RT enzymes.";
RL Nature 455:363-368(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate =
CC (9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O;
CC Xref=Rhea:RHEA:25074, ChEBI:CHEBI:15377, ChEBI:CHEBI:36438,
CC ChEBI:CHEBI:58757; EC=4.2.1.92;
CC Evidence={ECO:0000269|PubMed:8756596};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:18716621};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
CC {ECO:0000269|PubMed:12766230, ECO:0000269|PubMed:16414959,
CC ECO:0000269|PubMed:16461379}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:8756596}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; X92510; CAA63266.1; -; mRNA.
DR EMBL; Y12636; CAA73184.1; -; Genomic_DNA.
DR EMBL; AF172727; AAF00225.1; -; mRNA.
DR EMBL; AB007647; BAB10621.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94842.1; -; Genomic_DNA.
DR EMBL; AY062828; AAL32906.1; -; mRNA.
DR EMBL; AY065089; AAL38265.1; -; mRNA.
DR EMBL; AY128733; AAM91133.1; -; mRNA.
DR EMBL; AY128755; AAM91155.1; -; mRNA.
DR RefSeq; NP_199079.1; NM_123629.4.
DR PDB; 2RCH; X-ray; 1.85 A; A/B=34-518.
DR PDB; 2RCL; X-ray; 2.41 A; A/B=34-518.
DR PDB; 2RCM; X-ray; 1.73 A; A/B=34-518.
DR PDB; 3CLI; X-ray; 1.80 A; A/B=34-518.
DR PDB; 3DSI; X-ray; 1.60 A; A/B=34-518.
DR PDB; 3DSJ; X-ray; 1.60 A; A/B=34-518.
DR PDB; 3DSK; X-ray; 1.55 A; A/B=34-518.
DR PDBsum; 2RCH; -.
DR PDBsum; 2RCL; -.
DR PDBsum; 2RCM; -.
DR PDBsum; 3CLI; -.
DR PDBsum; 3DSI; -.
DR PDBsum; 3DSJ; -.
DR PDBsum; 3DSK; -.
DR AlphaFoldDB; Q96242; -.
DR SMR; Q96242; -.
DR BioGRID; 19523; 2.
DR IntAct; Q96242; 2.
DR STRING; 3702.AT5G42650.1; -.
DR ChEMBL; CHEMBL2268010; -.
DR iPTMnet; Q96242; -.
DR PaxDb; Q96242; -.
DR PRIDE; Q96242; -.
DR ProteomicsDB; 222761; -.
DR EnsemblPlants; AT5G42650.1; AT5G42650.1; AT5G42650.
DR GeneID; 834273; -.
DR Gramene; AT5G42650.1; AT5G42650.1; AT5G42650.
DR KEGG; ath:AT5G42650; -.
DR Araport; AT5G42650; -.
DR TAIR; locus:2165452; AT5G42650.
DR eggNOG; ENOG502QQNS; Eukaryota.
DR HOGENOM; CLU_045757_0_0_1; -.
DR InParanoid; Q96242; -.
DR OMA; KVTMAAM; -.
DR OrthoDB; 485250at2759; -.
DR PhylomeDB; Q96242; -.
DR BioCyc; ARA:MON-1582; -.
DR BioCyc; MetaCyc:MON-1582; -.
DR BRENDA; 4.2.1.92; 399.
DR SABIO-RK; Q96242; -.
DR UniPathway; UPA00382; -.
DR EvolutionaryTrace; Q96242; -.
DR PRO; PR:Q96242; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q96242; baseline and differential.
DR Genevisible; Q96242; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0009978; F:allene oxide synthase activity; IDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0019825; F:oxygen binding; ISS:TAIR.
DR GO; GO:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0019373; P:epoxygenase P450 pathway; ISS:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009695; P:jasmonic acid biosynthetic process; IDA:TAIR.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0031407; P:oxylipin metabolic process; IDA:TAIR.
DR GO; GO:0009620; P:response to fungus; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IMP:TAIR.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW Heme; Iron; Lipid biosynthesis; Lipid metabolism; Lyase; Metal-binding;
KW Oxylipin biosynthesis; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..33
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:12766230"
FT CHAIN 34..518
FT /note="Allene oxide synthase, chloroplastic"
FT /id="PRO_0000003625"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18716621"
FT BINDING 389
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18716621"
FT BINDING 471
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:0000269|PubMed:18716621"
FT MUTAGEN 137
FT /note="F->L: Impaired allene oxide synthase (AOS) activity,
FT but some hydroperoxide lyase (HPL) activity. Strong
FT hydroperoxide lyase (HPL) activity; when associated with A-
FT 155."
FT /evidence="ECO:0000269|PubMed:18716621"
FT MUTAGEN 155
FT /note="S->A: Strong HPL activity; when associated with L-
FT 137."
FT /evidence="ECO:0000269|PubMed:18716621"
FT MUTAGEN 321
FT /note="N->Q: Abolished allene oxide synthase activity."
FT /evidence="ECO:0000269|PubMed:18716621"
FT CONFLICT 201..233
FT /note="LSLKGKADFGGSSDGTAFNFLARAFYGTNPADT -> AFPLRESGFRRFQRR
FT NRLLFLGSSFLRDESRRY (in Ref. 1; CAA63266)"
FT /evidence="ECO:0000305"
FT CONFLICT 289..293
FT /note="FLESA -> LRIR (in Ref. 1; CAA63266)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="C -> S (in Ref. 1; CAA63266)"
FT /evidence="ECO:0000305"
FT CONFLICT 339..340
FT /note="RA -> PG (in Ref. 1; CAA63266)"
FT /evidence="ECO:0000305"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:3DSK"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:3DSK"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:3DSK"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3DSK"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:3DSK"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:3DSK"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 162..177
FT /evidence="ECO:0007829|PDB:3DSK"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 182..204
FT /evidence="ECO:0007829|PDB:3DSK"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 210..226
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:3DSK"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:3DSK"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 307..319
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 322..340
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 342..358
FT /evidence="ECO:0007829|PDB:3DSK"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 365..369
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 372..384
FT /evidence="ECO:0007829|PDB:3DSK"
FT STRAND 390..397
FT /evidence="ECO:0007829|PDB:3DSK"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:3DSK"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:3DSK"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 420..424
FT /evidence="ECO:0007829|PDB:3DSK"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:3DSK"
FT TURN 431..434
FT /evidence="ECO:0007829|PDB:3DSK"
FT TURN 438..441
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 443..448
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 449..452
FT /evidence="ECO:0007829|PDB:3DSK"
FT HELIX 474..491
FT /evidence="ECO:0007829|PDB:3DSK"
FT STRAND 492..501
FT /evidence="ECO:0007829|PDB:3DSK"
FT STRAND 503..515
FT /evidence="ECO:0007829|PDB:3DSK"
SQ SEQUENCE 518 AA; 58197 MW; DCC30E428B4A9132 CRC64;
MASISTPFPI SLHPKTVRSK PLKFRVLTRP IKASGSETPD LTVATRTGSK DLPIRNIPGN
YGLPIVGPIK DRWDYFYDQG AEEFFKSRIR KYNSTVYRVN MPPGAFIAEN PQVVALLDGK
SFPVLFDVDK VEKKDLFTGT YMPSTELTGG YRILSYLDPS EPKHEKLKNL LFFLLKSSRN
RIFPEFQATY SELFDSLEKE LSLKGKADFG GSSDGTAFNF LARAFYGTNP ADTKLKADAP
GLITKWVLFN LHPLLSIGLP RVIEEPLIHT FSLPPALVKS DYQRLYEFFL ESAGEILVEA
DKLGISREEA THNLLFATCF NTWGGMKILF PNMVKRIGRA GHQVHNRLAE EIRSVIKSNG
GELTMGAIEK MELTKSVVYE CLRFEPPVTA QYGRAKKDLV IESHDAAFKV KAGEMLYGYQ
PLATRDPKIF DRADEFVPER FVGEEGEKLL RHVLWSNGPE TETPTVGNKQ CAGKDFVVLV
ARLFVIEIFR RYDSFDIEVG TSPLGSSVNF SSLRKASF
