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O16025

- AOSL_PLEHO

UniProt

O16025 - AOSL_PLEHO

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Protein
Allene oxide synthase-lipoxygenase protein
Gene
N/A
Organism
Plexaura homomalla (Black sea rod)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

(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.

Cofactori

Binds 2 calcium ions per subunit.
Binds 1 iron ion per subunit.
Binds 1 heme group per subunit.1 Publication

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi353 – 3531Iron (heme axial ligand); catalytic
Metal bindingi387 – 3871Calcium 1; via carbonyl oxygen; structural
Metal bindingi389 – 3891Calcium 1; via carbonyl oxygen; structural
Metal bindingi390 – 3901Calcium 2; via carbonyl oxygen; structural
Metal bindingi391 – 3911Calcium 2; structural
Metal bindingi416 – 4161Calcium 2; structural
Metal bindingi417 – 4171Calcium 2; via carbonyl oxygen; structural
Metal bindingi419 – 4191Calcium 2; structural
Metal bindingi452 – 4521Calcium 1; via carbonyl oxygen; structural
Metal bindingi454 – 4541Calcium 1; via carbonyl oxygen; structural
Metal bindingi757 – 7571Iron; catalytic
Metal bindingi762 – 7621Iron; catalytic
Metal bindingi943 – 9431Iron; catalytic
Metal bindingi947 – 9471Iron; catalytic
Metal bindingi1066 – 10661Iron; via carboxylate; catalytic

GO - Molecular functioni

  1. arachidonate 8(R)-lipoxygenase activity Source: UniProtKB-EC
  2. catalase activity Source: InterPro
  3. heme binding Source: InterPro
  4. hydroperoxide dehydratase activity Source: UniProtKB-EC
  5. iron ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. arachidonic acid metabolic process Source: UniProtKB-UniPathway
  2. oxylipin biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Lyase, Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00383.

Protein family/group databases

PeroxiBasei5626. PhoKatLox01.

Names & Taxonomyi

Protein namesi
Recommended name:
Allene oxide synthase-lipoxygenase protein
Including the following 2 domains:
Alternative name(s):
Hydroperoxidehydrase
Arachidonate 8-lipoxygenase (EC:1.13.11.40)
OrganismiPlexaura homomalla (Black sea rod)
Taxonomic identifieri47982 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaOctocoralliaAlcyonaceaHolaxoniaPlexauridaePlexaura

Subcellular locationi

Cytoplasm. Membrane; Peripheral membrane protein
Note: Calcium binding promotes binding to membranes.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi411 – 4111D → 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. 1 Publication
Mutagenesisi413 – 4131W → A: Reduces stimulation of LOX-activity by calcium and membrane binding. 1 Publication
Mutagenesisi419 – 4191E → 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. 1 Publication
Mutagenesisi449 – 4491W → A: Reduces LOX-activity in the absence of membranes and increases activity in the presence of liposomes. May alter protein structure. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10661066Allene oxide synthase-lipoxygenase protein
PRO_0000220724Add
BLAST

Interactioni

Subunit structurei

Dimer Inferred.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 159
Helixi17 – 2711
Turni35 – 373
Helixi38 – 5922
Turni60 – 623
Beta strandi65 – 673
Beta strandi69 – 7911
Beta strandi89 – 913
Beta strandi96 – 10712
Beta strandi113 – 1153
Beta strandi117 – 12812
Beta strandi133 – 1419
Helixi147 – 1537
Helixi160 – 1667
Helixi170 – 17910
Beta strandi181 – 1833
Helixi187 – 1893
Beta strandi198 – 2014
Beta strandi207 – 21913
Helixi223 – 2253
Helixi232 – 2354
Turni236 – 2394
Helixi253 – 26412
Beta strandi267 – 27711
Helixi284 – 2874
Turni295 – 2973
Beta strandi301 – 31111
Helixi314 – 3196
Beta strandi337 – 3415
Helixi344 – 36219
Turni363 – 3653
Beta strandi374 – 3829
Beta strandi394 – 4007
Beta strandi408 – 4103
Beta strandi423 – 4319
Beta strandi434 – 44310
Beta strandi455 – 46410
Beta strandi467 – 4693
Beta strandi471 – 48515
Helixi499 – 51517
Helixi534 – 5363
Helixi539 – 5413
Helixi545 – 56824
Turni569 – 5713
Helixi577 – 5848
Beta strandi590 – 5923
Turni594 – 6007
Helixi602 – 61110
Helixi632 – 6354
Helixi636 – 6383
Helixi645 – 6517
Beta strandi654 – 6585
Helixi660 – 6623
Beta strandi698 – 7036
Beta strandi709 – 71911
Beta strandi721 – 7244
Helixi734 – 75421
Helixi755 – 7617
Helixi762 – 77514
Helixi781 – 79010
Helixi793 – 80311
Helixi810 – 8145
Turni816 – 8205
Helixi821 – 83010
Helixi835 – 8384
Helixi840 – 8467
Turni852 – 8543
Helixi859 – 88224
Helixi886 – 8916
Helixi893 – 90513
Beta strandi911 – 9133
Helixi925 – 93915
Helixi941 – 9477
Helixi950 – 9545
Helixi957 – 9593
Beta strandi970 – 9734
Helixi977 – 9837
Helixi987 – 100014
Beta strandi1009 – 10113
Helixi1021 – 104626
Beta strandi1048 – 10503
Helixi1057 – 10593
Beta strandi1060 – 10634

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliO16025.
SMRiO16025. Positions 3-368, 374-1066.

Miscellaneous databases

EvolutionaryTraceiO16025.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini374 – 490117PLAT
Add
BLAST
Domaini491 – 1066576Lipoxygenase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 371371Allene oxide synthase
Add
BLAST
Regioni372 – 1066695Arachidonate 8-lipoxygenase
Add
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the lipoxygenase family.
Contains 1 PLAT domain.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
2.60.60.20. 1 hit.
InterProiIPR020835. Catalase-like_dom.
IPR011614. Catalase_core.
IPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
SSF56634. SSF56634. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O16025-1 [UniParc]FASTAAdd to Basket

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MTWKNFGFEI FGEKYGQEEL EKRIKDEHTP PPDSPVFGGL KLKLKKEKFK     50
TLFTLGTTLK GFRRATHTVG TGGIGEITIV NDPKFPEHEF FTAGRTFPAR 100
LRHANLKYPD DAGADARSFS IKFADSDSDG PLDIVMNTGE ANIFWNSPSL 150
EDFVPVEEGD AAEEYVYKNP YYYYNLVEAL RRAPDTFAHL YYYSQVTMPF 200
KAKDGKVRYC RYRALPGDVD IKEEDESGRL TEEEQRKIWI FSRHENEKRP 250
DDYLRKEYVE RLQKGPVNYR LQIQIHEASP DDTATIFHAG ILWDKETHPW 300
FDLAKVSIKT PLSPDVLEKT AFNIANQPAS LGLLEAKSPE DYNSIGELRV 350
AVYTWVQHLR KLKIGSLVPA GQNAIYNVEV ETGDREHAGT DATITIRITG 400
AKGRTDYLKL DKWFHNDFEA GSKEQYTVQG FDVGDIQLIE LHSDGGGYWS 450
GDPDWFVNRV IIISSTQDRV YSFPCFRWVI KDMVLFPGEA TLPFNEVPAI 500
VSEQRQKELE QRKLTYQWDY VSDDMPGNIK AKTHDDLPRD VQFTDEKSRS 550
YQESRKAALV NLGIGSLFTM FENWDSYDDY HILYRNWILG GTPNMADRWH 600
EDRWFGYQFL NGANPVILTR CDALPSNFPV TNEHVNASLD RGKNLDEEIK 650
DGHIYIVDFK VLVGAKSYGG PVLEDIGYKV PDHLKHDEAD IRYCAAPLAL 700
FYVNKLGHLM PIAIQINQEP GPENPIWTPH EENEHDWMMA KFWLGVAESN 750
FHQLNTHLLR THLTTESFAL STWRNLASAH PVFKLLQPHI YGVLAIDTIG 800
RKELIGSGGI VDQSLSLGGG GHVTFMEKCF KEVNLQDYHL PNALKKRGVD 850
DPSKLPGFYY RDDGLALWEA IETFIGEIIA IFYKNDDDVK RDNEIQSWIY 900
DVHKNGWRVN PGHQDHGVPA SFESREQLKE VLTSLVFTFS CQHAAVNFSQ 950
KDHYGFTPNA PAVLRHPPPK KKGEATLQSI LSTLPSKSQA AKAIATVYIL 1000
TKFSEDERYL GNYSATAWED KDALDAINRF QDKLEDISKK IKQRNENLEV 1050
PYIYLLPERI PNGTAI 1066
Length:1,066
Mass (Da):121,783
Last modified:January 1, 1998 - v1
Checksum:iDD26886BD1EE95D7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF003692 mRNA. Translation: AAC47743.1.
PIRiT30903.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF003692 mRNA. Translation: AAC47743.1 .
PIRi T30903.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U5U X-ray 2.00 A/B 1-374 [» ]
2FNQ X-ray 3.20 A/B 374-1066 [» ]
3DY5 X-ray 3.51 A/C 1-1066 [» ]
3FG1 X-ray 1.85 A/B/C/D 374-1066 [» ]
3FG3 X-ray 1.90 A/B/C/D 374-1066 [» ]
3FG4 X-ray 2.31 A/B/C/D 374-1066 [» ]
ProteinModelPortali O16025.
SMRi O16025. Positions 3-368, 374-1066.
ModBasei Search...

Protein family/group databases

PeroxiBasei 5626. PhoKatLox01.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00383 .

Miscellaneous databases

EvolutionaryTracei O16025.

Family and domain databases

Gene3Di 2.40.180.10. 1 hit.
2.60.60.20. 1 hit.
InterProi IPR020835. Catalase-like_dom.
IPR011614. Catalase_core.
IPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11771. PTHR11771. 1 hit.
Pfami PF00199. Catalase. 1 hit.
PF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view ]
PRINTSi PR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTi SM00308. LH2. 1 hit.
[Graphical view ]
SUPFAMi SSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
SSF56634. SSF56634. 1 hit.
PROSITEi PS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiAOSL_PLEHO
AccessioniPrimary (citable) accession number: O16025
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: January 1, 1998
Last modified: November 13, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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