Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O16025

- AOSL_PLEHO

UniProt

O16025 - AOSL_PLEHO

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    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; structural1 Publication
    Metal bindingi389 – 3891Calcium 1; via carbonyl oxygen; structural1 Publication
    Metal bindingi390 – 3901Calcium 2; via carbonyl oxygen; structural1 Publication
    Metal bindingi391 – 3911Calcium 2; structural1 Publication
    Metal bindingi416 – 4161Calcium 2; structural1 Publication
    Metal bindingi417 – 4171Calcium 2; via carbonyl oxygen; structural1 Publication
    Metal bindingi419 – 4191Calcium 2; structural1 Publication
    Metal bindingi452 – 4521Calcium 1; via carbonyl oxygen; structural1 Publication
    Metal bindingi454 – 4541Calcium 1; via carbonyl oxygen; structural1 Publication
    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

    GO - Biological processi

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

    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 1 PublicationPROSITE-ProRule annotation. Membrane 1 Publication; Peripheral membrane protein 1 Publication
    Note: Calcium binding promotes binding to membranes.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB-SubCell

    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 proteinPRO_0000220724Add
    BLAST

    Interactioni

    Subunit structurei

    Dimer.2 Publications

    Structurei

    Secondary structure

    1
    1066
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO16025.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini374 – 490117PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini491 – 1066576LipoxygenasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 371371Allene oxide synthaseAdd
    BLAST
    Regioni372 – 1066695Arachidonate 8-lipoxygenaseAdd
    BLAST

    Sequence similaritiesi

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

    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

    « Hide

    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...
    MobiDBi 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: October 1, 2014
    This is version 94 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