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Protein

Allene oxide synthase, chloroplastic

Gene

CYP74A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate = (9Z,15Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O.1 Publication

Cofactori

heme1 Publication

Pathwayi: oxylipin biosynthesis

This protein is involved in the pathway oxylipin biosynthesis, which is part of Lipid metabolism.Curated
View all proteins of this organism that are known to be involved in the pathway oxylipin biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei321 – 3211Substrate1 Publication
Binding sitei389 – 3891Substrate1 Publication
Metal bindingi471 – 4711Iron (heme axial ligand)1 Publication

GO - Molecular functioni

GO - Biological processi

  • defense response Source: TAIR
  • defense response to fungus Source: TAIR
  • epoxygenase P450 pathway Source: TAIR
  • jasmonic acid biosynthetic process Source: TAIR
  • oxylipin biosynthetic process Source: UniProtKB-UniPathway
  • oxylipin metabolic process Source: TAIR
  • response to fungus Source: TAIR
  • response to jasmonic acid Source: TAIR
  • response to wounding Source: TAIR
  • sterol metabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Oxylipin biosynthesis

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-1582.
BRENDAi4.2.1.92. 399.
SABIO-RKQ96242.
UniPathwayiUPA00382.

Names & Taxonomyi

Protein namesi
Recommended name:
Allene oxide synthase, chloroplastic (EC:4.2.1.921 Publication)
Alternative name(s):
Cytochrome P450 74A
Hydroperoxide dehydrase
Gene namesi
Name:CYP74A
Synonyms:AOS
Ordered Locus Names:At5g42650
ORF Names:MJB21.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G42650.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast thylakoid Source: TAIR
  • chloroplast thylakoid membrane Source: TAIR
  • membrane Source: TAIR
  • mitochondrion Source: TAIR
  • plastoglobule Source: TAIR
  • thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi137 – 1371F → L: Impaired allene oxide synthase (AOS) activity, but some hydroperoxide lyase (HPL) activity. Strong hydroperoxide lyase (HPL) activity; when associated with A-155. 1 Publication
Mutagenesisi155 – 1551S → A: Strong HPL activity; when associated with L-137. 1 Publication
Mutagenesisi321 – 3211N → Q: Abolished allene oxide synthase activity. 1 Publication

Chemistry

ChEMBLiCHEMBL2268010.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2121ChloroplastSequence analysisAdd
BLAST
Chaini22 – 518497Allene oxide synthase, chloroplasticPRO_0000003625Add
BLAST

Proteomic databases

PaxDbiQ96242.
PRIDEiQ96242.

PTM databases

iPTMnetiQ96242.

Expressioni

Inductioni

By wounding.1 Publication

Gene expression databases

GenevisibleiQ96242. AT.

Interactioni

Protein-protein interaction databases

BioGridi19523. 2 interactions.
IntActiQ96242. 1 interaction.
STRINGi3702.AT5G42650.1.

Structurei

Secondary structure

1
518
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi66 – 7611Combined sources
Helixi81 – 9212Combined sources
Beta strandi95 – 1006Combined sources
Turni105 – 1073Combined sources
Beta strandi112 – 1165Combined sources
Turni119 – 1213Combined sources
Helixi122 – 1265Combined sources
Turni128 – 1303Combined sources
Beta strandi139 – 1413Combined sources
Helixi145 – 1484Combined sources
Helixi154 – 1563Combined sources
Helixi162 – 17716Combined sources
Turni178 – 1814Combined sources
Helixi182 – 20423Combined sources
Beta strandi205 – 2095Combined sources
Helixi210 – 22617Combined sources
Helixi230 – 2323Combined sources
Turni234 – 2374Combined sources
Helixi239 – 25113Combined sources
Helixi252 – 2543Combined sources
Helixi261 – 2688Combined sources
Beta strandi269 – 2713Combined sources
Helixi275 – 2784Combined sources
Helixi279 – 29214Combined sources
Helixi294 – 3029Combined sources
Helixi307 – 31913Combined sources
Helixi322 – 34019Combined sources
Helixi342 – 35817Combined sources
Turni359 – 3613Combined sources
Helixi365 – 3695Combined sources
Helixi372 – 38413Combined sources
Beta strandi390 – 3978Combined sources
Beta strandi399 – 4024Combined sources
Beta strandi407 – 4104Combined sources
Beta strandi415 – 4195Combined sources
Helixi420 – 4245Combined sources
Turni427 – 4293Combined sources
Turni431 – 4344Combined sources
Turni438 – 4414Combined sources
Helixi443 – 4486Combined sources
Helixi449 – 4524Combined sources
Helixi474 – 49118Combined sources
Beta strandi492 – 50110Combined sources
Beta strandi503 – 51513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RCHX-ray1.85A/B34-518[»]
2RCLX-ray2.41A/B34-518[»]
2RCMX-ray1.73A/B34-518[»]
3CLIX-ray1.80A/B34-518[»]
3DSIX-ray1.60A/B34-518[»]
3DSJX-ray1.60A/B34-518[»]
3DSKX-ray1.55A/B34-518[»]
ProteinModelPortaliQ96242.
SMRiQ96242. Positions 51-516.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96242.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IF79. Eukaryota.
ENOG410ZAGU. LUCA.
HOGENOMiHOG000238722.
InParanoidiQ96242.
KOiK01723.
OMAiFNFLARA.
PhylomeDBiQ96242.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
SUPFAMiSSF48264. SSF48264. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96242-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASISTPFPI SLHPKTVRSK PLKFRVLTRP IKASGSETPD LTVATRTGSK
60 70 80 90 100
DLPIRNIPGN YGLPIVGPIK DRWDYFYDQG AEEFFKSRIR KYNSTVYRVN
110 120 130 140 150
MPPGAFIAEN PQVVALLDGK SFPVLFDVDK VEKKDLFTGT YMPSTELTGG
160 170 180 190 200
YRILSYLDPS EPKHEKLKNL LFFLLKSSRN RIFPEFQATY SELFDSLEKE
210 220 230 240 250
LSLKGKADFG GSSDGTAFNF LARAFYGTNP ADTKLKADAP GLITKWVLFN
260 270 280 290 300
LHPLLSIGLP RVIEEPLIHT FSLPPALVKS DYQRLYEFFL ESAGEILVEA
310 320 330 340 350
DKLGISREEA THNLLFATCF NTWGGMKILF PNMVKRIGRA GHQVHNRLAE
360 370 380 390 400
EIRSVIKSNG GELTMGAIEK MELTKSVVYE CLRFEPPVTA QYGRAKKDLV
410 420 430 440 450
IESHDAAFKV KAGEMLYGYQ PLATRDPKIF DRADEFVPER FVGEEGEKLL
460 470 480 490 500
RHVLWSNGPE TETPTVGNKQ CAGKDFVVLV ARLFVIEIFR RYDSFDIEVG
510
TSPLGSSVNF SSLRKASF
Length:518
Mass (Da):58,197
Last modified:April 27, 2001 - v3
Checksum:iDCC30E428B4A9132
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 23333LSLKG…NPADT → AFPLRESGFRRFQRRNRLLF LGSSFLRDESRRY in CAA63266 (PubMed:8756596).CuratedAdd
BLAST
Sequence conflicti289 – 2935FLESA → LRIR in CAA63266 (PubMed:8756596).Curated
Sequence conflicti319 – 3191C → S in CAA63266 (PubMed:8756596).Curated
Sequence conflicti339 – 3402RA → PG in CAA63266 (PubMed:8756596).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92510 mRNA. Translation: CAA63266.1.
Y12636 Genomic DNA. Translation: CAA73184.1.
AF172727 mRNA. Translation: AAF00225.1.
AB007647 Genomic DNA. Translation: BAB10621.1.
CP002688 Genomic DNA. Translation: AED94842.1.
AY062828 mRNA. Translation: AAL32906.1.
AY065089 mRNA. Translation: AAL38265.1.
AY128733 mRNA. Translation: AAM91133.1.
AY128755 mRNA. Translation: AAM91155.1.
RefSeqiNP_199079.1. NM_123629.3.
UniGeneiAt.211.

Genome annotation databases

EnsemblPlantsiAT5G42650.1; AT5G42650.1; AT5G42650.
GeneIDi834273.
GrameneiAT5G42650.1; AT5G42650.1; AT5G42650.
KEGGiath:AT5G42650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92510 mRNA. Translation: CAA63266.1.
Y12636 Genomic DNA. Translation: CAA73184.1.
AF172727 mRNA. Translation: AAF00225.1.
AB007647 Genomic DNA. Translation: BAB10621.1.
CP002688 Genomic DNA. Translation: AED94842.1.
AY062828 mRNA. Translation: AAL32906.1.
AY065089 mRNA. Translation: AAL38265.1.
AY128733 mRNA. Translation: AAM91133.1.
AY128755 mRNA. Translation: AAM91155.1.
RefSeqiNP_199079.1. NM_123629.3.
UniGeneiAt.211.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RCHX-ray1.85A/B34-518[»]
2RCLX-ray2.41A/B34-518[»]
2RCMX-ray1.73A/B34-518[»]
3CLIX-ray1.80A/B34-518[»]
3DSIX-ray1.60A/B34-518[»]
3DSJX-ray1.60A/B34-518[»]
3DSKX-ray1.55A/B34-518[»]
ProteinModelPortaliQ96242.
SMRiQ96242. Positions 51-516.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19523. 2 interactions.
IntActiQ96242. 1 interaction.
STRINGi3702.AT5G42650.1.

Chemistry

ChEMBLiCHEMBL2268010.

PTM databases

iPTMnetiQ96242.

Proteomic databases

PaxDbiQ96242.
PRIDEiQ96242.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G42650.1; AT5G42650.1; AT5G42650.
GeneIDi834273.
GrameneiAT5G42650.1; AT5G42650.1; AT5G42650.
KEGGiath:AT5G42650.

Organism-specific databases

TAIRiAT5G42650.

Phylogenomic databases

eggNOGiENOG410IF79. Eukaryota.
ENOG410ZAGU. LUCA.
HOGENOMiHOG000238722.
InParanoidiQ96242.
KOiK01723.
OMAiFNFLARA.
PhylomeDBiQ96242.

Enzyme and pathway databases

UniPathwayiUPA00382.
BioCyciMetaCyc:MONOMER-1582.
BRENDAi4.2.1.92. 399.
SABIO-RKQ96242.

Miscellaneous databases

EvolutionaryTraceiQ96242.
PROiQ96242.

Gene expression databases

GenevisibleiQ96242. AT.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
SUPFAMiSSF48264. SSF48264. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, molecular and functional characterization of Arabidopsis thaliana allene oxide synthase (CYP 74), the first enzyme of the octadecanoid pathway to jasmonates."
    Laudert D., Pfannschmidt U., Lottspeich F., Hollanderczytko H., Weiler E.W.
    Plant Mol. Biol. 31:323-335(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, INDUCTION BY WOUNDING.
    Strain: cv. Columbia.
    Tissue: Leaf.
  2. "Structure and regulation of the Arabidopsis thaliana allene oxide synthase gene."
    Kubigsteltig I., Laudert D., Weiler E.W.
    Planta 208:463-471(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence of an allene oxide synthase cDNA from Arabidopsis thaliana."
    Staswick P.E.
    Plant Gene Register PGR99-130
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  4. "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
    Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 4:401-414(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
    Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
    Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Wassilewskija.
  8. "Tocopherol cyclase (VTE1) localization and vitamin E accumulation in chloroplast plastoglobule lipoprotein particles."
    Vidi P.-A., Kanwischer M., Baginsky S., Austin J.R., Csucs G., Doermann P., Kessler F., Brehelin C.
    J. Biol. Chem. 281:11225-11234(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Col-2.
  9. "Protein profiling of plastoglobules in chloroplasts and chromoplasts. A surprising site for differential accumulation of metabolic enzymes."
    Ytterberg A.J., Peltier J.-B., van Wijk K.J.
    Plant Physiol. 140:984-997(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  10. "Structural insights into the evolutionary paths of oxylipin biosynthetic enzymes."
    Lee D.-S., Nioche P., Hamberg M., Raman C.S.
    Nature 455:363-368(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 34-518 IN COMPLEX WITH HEME AND SUBSTRATE ANALOGS, MUTAGENESIS OF PHE-137; SER-155 AND ASN-321.

Entry informationi

Entry nameiCP74A_ARATH
AccessioniPrimary (citable) accession number: Q96242
Secondary accession number(s): P93720, Q9ZR51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 27, 2001
Last modified: May 11, 2016
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.