Skip Header

Contribute Send feedback
Read comments (?) or add your own

O16025 (AOSL_PLEHO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Allene oxide synthase-lipoxygenase protein

Including the following 2 domains:

  1. Allene oxide synthase
    EC=4.2.1.92
    Alternative name(s):
    Hydroperoxidehydrase
  2. Arachidonate 8-lipoxygenase
    EC=1.13.11.40
OrganismPlexaura homomalla (Black sea rod)
Taxonomic identifier47982 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Cnidaria › Anthozoa › Octocorallia › Alcyonacea › Holaxonia › Plexauridae › Plexaura

Protein attributes

Sequence length1066 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme which is responsible for allene oxide biosynthesis via a two-step reaction which involves conversion of arachidonic acid to a 8R-hydroperoxide intermediate followed by conversion of the hydroperoxide to allene oxide. Ref.1 Ref.2

Catalytic activity

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

Arachidonate + O2 = (5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate.

Cofactor

Binds 2 calcium ions per subunit.

Binds 1 iron ion per subunit.

Binds 1 heme group per subunit. Ref.3

Enzyme regulation

Lipoxygenase activity is stimulated by calcium, sodium, lithium and potassium ions. Calcium binding promotes interaction with membranes and thus facilitates access to substrates. Ref.2 Ref.4

Pathway

Lipid metabolism; arachidonate metabolism.

Subunit structure

Dimer Probable. Ref.5

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Note: Calcium binding promotes binding to membranes. Ref.4

Sequence similarities

In the C-terminal section; belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10661066Allene oxide synthase-lipoxygenase protein
PRO_0000220724

Regions

Domain374 – 490117PLAT
Domain491 – 1066576Lipoxygenase
Region1 – 371371Allene oxide synthase
Region372 – 1066695Arachidonate 8-lipoxygenase

Sites

Metal binding3531Iron (heme axial ligand); catalytic
Metal binding3871Calcium 1; via carbonyl oxygen; structural
Metal binding3891Calcium 1; via carbonyl oxygen; structural
Metal binding3901Calcium 2; via carbonyl oxygen; structural
Metal binding3911Calcium 2; structural
Metal binding4161Calcium 2; structural
Metal binding4171Calcium 2; via carbonyl oxygen; structural
Metal binding4191Calcium 2; structural
Metal binding4521Calcium 1; via carbonyl oxygen; structural
Metal binding4541Calcium 1; via carbonyl oxygen; structural
Metal binding7571Iron; catalytic
Metal binding7621Iron; catalytic
Metal binding9431Iron; catalytic
Metal binding9471Iron; catalytic
Metal binding10661Iron; via carboxylate; catalytic

Experimental info

Mutagenesis4111D → A: Reduces stimulation of LOX-activity by calcium and membrane binding. Abolishes stimulation of LOX-activity by calcium and membrane binding; when associated with A-419. Ref.4
Mutagenesis4131W → A: Reduces stimulation of LOX-activity by calcium and membrane binding. Ref.4
Mutagenesis4191E → A: Reduces stimulation of LOX-activity by calcium and membrane binding. Abolishes stimulation of LOX-activity by calcium and membrane binding; when associated with A-411. Ref.4
Mutagenesis4491W → A: Reduces LOX-activity in the absence of membranes and increases activity in the presence of liposomes. May alter protein structure. Ref.4

Secondary structure

1 ............................................................................................................................................................. 1066
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O16025 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: DD26886BD1EE95D7

FASTA1,066121,783
        10         20         30         40         50         60 
MTWKNFGFEI FGEKYGQEEL EKRIKDEHTP PPDSPVFGGL KLKLKKEKFK TLFTLGTTLK 

        70         80         90        100        110        120 
GFRRATHTVG TGGIGEITIV NDPKFPEHEF FTAGRTFPAR LRHANLKYPD DAGADARSFS 

       130        140        150        160        170        180 
IKFADSDSDG PLDIVMNTGE ANIFWNSPSL EDFVPVEEGD AAEEYVYKNP YYYYNLVEAL 

       190        200        210        220        230        240 
RRAPDTFAHL YYYSQVTMPF KAKDGKVRYC RYRALPGDVD IKEEDESGRL TEEEQRKIWI 

       250        260        270        280        290        300 
FSRHENEKRP DDYLRKEYVE RLQKGPVNYR LQIQIHEASP DDTATIFHAG ILWDKETHPW 

       310        320        330        340        350        360 
FDLAKVSIKT PLSPDVLEKT AFNIANQPAS LGLLEAKSPE DYNSIGELRV AVYTWVQHLR 

       370        380        390        400        410        420 
KLKIGSLVPA GQNAIYNVEV ETGDREHAGT DATITIRITG AKGRTDYLKL DKWFHNDFEA 

       430        440        450        460        470        480 
GSKEQYTVQG FDVGDIQLIE LHSDGGGYWS GDPDWFVNRV IIISSTQDRV YSFPCFRWVI 

       490        500        510        520        530        540 
KDMVLFPGEA TLPFNEVPAI VSEQRQKELE QRKLTYQWDY VSDDMPGNIK AKTHDDLPRD 

       550        560        570        580        590        600 
VQFTDEKSRS YQESRKAALV NLGIGSLFTM FENWDSYDDY HILYRNWILG GTPNMADRWH 

       610        620        630        640        650        660 
EDRWFGYQFL NGANPVILTR CDALPSNFPV TNEHVNASLD RGKNLDEEIK DGHIYIVDFK 

       670        680        690        700        710        720 
VLVGAKSYGG PVLEDIGYKV PDHLKHDEAD IRYCAAPLAL FYVNKLGHLM PIAIQINQEP 

       730        740        750        760        770        780 
GPENPIWTPH EENEHDWMMA KFWLGVAESN FHQLNTHLLR THLTTESFAL STWRNLASAH 

       790        800        810        820        830        840 
PVFKLLQPHI YGVLAIDTIG RKELIGSGGI VDQSLSLGGG GHVTFMEKCF KEVNLQDYHL 

       850        860        870        880        890        900 
PNALKKRGVD DPSKLPGFYY RDDGLALWEA IETFIGEIIA IFYKNDDDVK RDNEIQSWIY 

       910        920        930        940        950        960 
DVHKNGWRVN PGHQDHGVPA SFESREQLKE VLTSLVFTFS CQHAAVNFSQ KDHYGFTPNA 

       970        980        990       1000       1010       1020 
PAVLRHPPPK KKGEATLQSI LSTLPSKSQA AKAIATVYIL TKFSEDERYL GNYSATAWED 

      1030       1040       1050       1060 
KDALDAINRF QDKLEDISKK IKQRNENLEV PYIYLLPERI PNGTAI

« Hide

References

[1]"Identification of a naturally occurring peroxidase-lipoxygenase fusion protein."
Koljak R., Boutaud O., Shieh B.-H., Samel N., Brash A.R.
Science 277:1994-1996(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"Purification and catalytic activities of the two domains of the allene oxide synthase-lipoxygenase fusion protein of the coral Plexaura homomalla."
Boutaud O., Brash A.R.
J. Biol. Chem. 274:33764-33770(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[3]"Characterization of the coral allene oxide synthase active site with UV-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopy: evidence for tyrosinate ligation to the ferric enzyme heme iron."
Abraham B.D., Sono M., Boutaud O., Shriner A., Dawson J.H., Brash A.R., Gaffney B.J.
Biochemistry 40:2251-2259(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: HEME-BINDING.
[4]"Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via a C2-like domain and a structural basis of product chirality."
Oldham M.L., Brash A.R., Newcomer M.E.
J. Biol. Chem. 280:39545-39552(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 373-1066 IN COMPLEX WITH CALCIUM AND IRON IONS, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF ASP-411; TRP-413; GLU-419 AND TRP-449.
[5]"The structure of coral allene oxide synthase reveals a catalase adapted for metabolism of a fatty acid hydroperoxide."
Oldham M.L., Brash A.R., Newcomer M.E.
Proc. Natl. Acad. Sci. U.S.A. 102:297-302(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-374 IN COMPLEX WITH HEME, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF003692 mRNA. Translation: AAC47743.1.
PIRT30903.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U5UX-ray2.00A/B1-374[»]
2FNQX-ray3.20A/B374-1066[»]
3DY5X-ray3.51A/C1-1066[»]
3FG1X-ray1.85A/B/C/D374-1066[»]
3FG3X-ray1.90A/B/C/D374-1066[»]
3FG4X-ray2.31A/B/C/D374-1066[»]
ProteinModelPortalO16025.
SMRO16025. Positions 3-368, 374-1066.
ModBaseSearch...

Protein family/group databases

PeroxiBase5626. PhoKatLox01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00383.

Family and domain databases

Gene3D2.40.180.10. 1 hit.
2.60.60.20. 1 hit.
InterProIPR020835. Catalase-like_dom.
IPR011614. Catalase_core.
IPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001024. LipOase_LH2.
IPR001885. LipOase_mml.
[Graphical view]
PANTHERPTHR11771. PTHR11771. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF56634. Catalase_N. 1 hit.
SSF49723. Lipase_LipOase. 1 hit.
SSF48484. Lipoxygenase. 1 hit.
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO16025.

Entry information

Entry nameAOSL_PLEHO
AccessionPrimary (citable) accession number: O16025
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: January 1, 1998
Last modified: April 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents