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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

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 2 calcium ions per subunit.
  • Fe cationNote: Binds 1 Fe cation per subunit.
  • hemeNote: 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
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 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-KW
  2. membrane Source: UniProtKB-KW
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 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 – 159Combined sources
Helixi17 – 2711Combined sources
Turni35 – 373Combined sources
Helixi38 – 5922Combined sources
Turni60 – 623Combined sources
Beta strandi65 – 673Combined sources
Beta strandi69 – 7911Combined sources
Beta strandi89 – 913Combined sources
Beta strandi96 – 10712Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi117 – 12812Combined sources
Beta strandi133 – 1419Combined sources
Helixi147 – 1537Combined sources
Helixi160 – 1667Combined sources
Helixi170 – 17910Combined sources
Beta strandi181 – 1833Combined sources
Helixi187 – 1893Combined sources
Beta strandi198 – 2014Combined sources
Beta strandi207 – 21913Combined sources
Helixi223 – 2253Combined sources
Helixi232 – 2354Combined sources
Turni236 – 2394Combined sources
Helixi253 – 26412Combined sources
Beta strandi267 – 27711Combined sources
Helixi284 – 2874Combined sources
Turni295 – 2973Combined sources
Beta strandi301 – 31111Combined sources
Helixi314 – 3196Combined sources
Beta strandi337 – 3415Combined sources
Helixi344 – 36219Combined sources
Turni363 – 3653Combined sources
Beta strandi374 – 3829Combined sources
Beta strandi394 – 4007Combined sources
Beta strandi408 – 4103Combined sources
Beta strandi423 – 4319Combined sources
Beta strandi434 – 44310Combined sources
Beta strandi455 – 46410Combined sources
Beta strandi467 – 4693Combined sources
Beta strandi471 – 48515Combined sources
Helixi499 – 51517Combined sources
Helixi534 – 5363Combined sources
Helixi539 – 5413Combined sources
Helixi545 – 56824Combined sources
Turni569 – 5713Combined sources
Helixi577 – 5848Combined sources
Beta strandi590 – 5923Combined sources
Turni594 – 6007Combined sources
Helixi602 – 61110Combined sources
Helixi632 – 6354Combined sources
Helixi636 – 6383Combined sources
Helixi645 – 6517Combined sources
Beta strandi654 – 6585Combined sources
Helixi660 – 6623Combined sources
Beta strandi698 – 7036Combined sources
Beta strandi709 – 71911Combined sources
Beta strandi721 – 7244Combined sources
Helixi734 – 75421Combined sources
Helixi755 – 7617Combined sources
Helixi762 – 77514Combined sources
Helixi781 – 79010Combined sources
Helixi793 – 80311Combined sources
Helixi810 – 8145Combined sources
Turni816 – 8205Combined sources
Helixi821 – 83010Combined sources
Helixi835 – 8384Combined sources
Helixi840 – 8467Combined sources
Turni852 – 8543Combined sources
Helixi859 – 88224Combined sources
Helixi886 – 8916Combined sources
Helixi893 – 90513Combined sources
Beta strandi911 – 9133Combined sources
Helixi925 – 93915Combined sources
Helixi941 – 9477Combined sources
Helixi950 – 9545Combined sources
Helixi957 – 9593Combined sources
Beta strandi970 – 9734Combined sources
Helixi977 – 9837Combined sources
Helixi987 – 100014Combined sources
Beta strandi1009 – 10113Combined sources
Helixi1021 – 104626Combined sources
Beta strandi1048 – 10503Combined sources
Helixi1057 – 10593Combined sources
Beta strandi1060 – 10634Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4QWTX-ray2.00A/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

        10         20         30         40         50
MTWKNFGFEI FGEKYGQEEL EKRIKDEHTP PPDSPVFGGL KLKLKKEKFK
60 70 80 90 100
TLFTLGTTLK GFRRATHTVG TGGIGEITIV NDPKFPEHEF FTAGRTFPAR
110 120 130 140 150
LRHANLKYPD DAGADARSFS IKFADSDSDG PLDIVMNTGE ANIFWNSPSL
160 170 180 190 200
EDFVPVEEGD AAEEYVYKNP YYYYNLVEAL RRAPDTFAHL YYYSQVTMPF
210 220 230 240 250
KAKDGKVRYC RYRALPGDVD IKEEDESGRL TEEEQRKIWI FSRHENEKRP
260 270 280 290 300
DDYLRKEYVE RLQKGPVNYR LQIQIHEASP DDTATIFHAG ILWDKETHPW
310 320 330 340 350
FDLAKVSIKT PLSPDVLEKT AFNIANQPAS LGLLEAKSPE DYNSIGELRV
360 370 380 390 400
AVYTWVQHLR KLKIGSLVPA GQNAIYNVEV ETGDREHAGT DATITIRITG
410 420 430 440 450
AKGRTDYLKL DKWFHNDFEA GSKEQYTVQG FDVGDIQLIE LHSDGGGYWS
460 470 480 490 500
GDPDWFVNRV IIISSTQDRV YSFPCFRWVI KDMVLFPGEA TLPFNEVPAI
510 520 530 540 550
VSEQRQKELE QRKLTYQWDY VSDDMPGNIK AKTHDDLPRD VQFTDEKSRS
560 570 580 590 600
YQESRKAALV NLGIGSLFTM FENWDSYDDY HILYRNWILG GTPNMADRWH
610 620 630 640 650
EDRWFGYQFL NGANPVILTR CDALPSNFPV TNEHVNASLD RGKNLDEEIK
660 670 680 690 700
DGHIYIVDFK VLVGAKSYGG PVLEDIGYKV PDHLKHDEAD IRYCAAPLAL
710 720 730 740 750
FYVNKLGHLM PIAIQINQEP GPENPIWTPH EENEHDWMMA KFWLGVAESN
760 770 780 790 800
FHQLNTHLLR THLTTESFAL STWRNLASAH PVFKLLQPHI YGVLAIDTIG
810 820 830 840 850
RKELIGSGGI VDQSLSLGGG GHVTFMEKCF KEVNLQDYHL PNALKKRGVD
860 870 880 890 900
DPSKLPGFYY RDDGLALWEA IETFIGEIIA IFYKNDDDVK RDNEIQSWIY
910 920 930 940 950
DVHKNGWRVN PGHQDHGVPA SFESREQLKE VLTSLVFTFS CQHAAVNFSQ
960 970 980 990 1000
KDHYGFTPNA PAVLRHPPPK KKGEATLQSI LSTLPSKSQA AKAIATVYIL
1010 1020 1030 1040 1050
TKFSEDERYL GNYSATAWED KDALDAINRF QDKLEDISKK IKQRNENLEV
1060
PYIYLLPERI PNGTAI
Length:1,066
Mass (Da):121,783
Last modified:January 1, 1998 - v1
Checksum:iDD26886BD1EE95D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003692 mRNA. Translation: AAC47743.1.
PIRiT30903.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003692 mRNA. Translation: AAC47743.1 .
PIRi T30903.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 [» ]
4QWT X-ray 2.00 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: November 26, 2014
This is version 96 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