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Protein

Allene oxide synthase-lipoxygenase protein

Gene
N/A
Organism
Plexaura homomalla (Black sea rod)
Status
Reviewed-Annotation score: 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: arachidonate metabolism

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi353Iron (heme axial ligand); catalytic1
Metal bindingi387Calcium 1; via carbonyl oxygen; structural1 Publication1
Metal bindingi389Calcium 1; via carbonyl oxygen; structural1 Publication1
Metal bindingi390Calcium 2; via carbonyl oxygen; structural1 Publication1
Metal bindingi391Calcium 2; structural1 Publication1
Metal bindingi416Calcium 2; structural1 Publication1
Metal bindingi417Calcium 2; via carbonyl oxygen; structural1 Publication1
Metal bindingi419Calcium 2; structural1 Publication1
Metal bindingi452Calcium 1; via carbonyl oxygen; structural1 Publication1
Metal bindingi454Calcium 1; via carbonyl oxygen; structural1 Publication1
Metal bindingi757Iron; catalytic1
Metal bindingi762Iron; catalytic1
Metal bindingi943Iron; catalytic1
Metal bindingi947Iron; catalytic1
Metal bindingi1066Iron; via carboxylate; catalytic1

GO - Molecular functioni

GO - Biological processi

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

BRENDAi1.13.11.40. 4917.
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 PROSITE-ProRule annotation1 Publication
  • Membrane 1 Publication; Peripheral membrane protein 1 Publication

  • Note: Calcium binding promotes binding to membranes.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi411D → 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 Publication1
Mutagenesisi413W → A: Reduces stimulation of LOX-activity by calcium and membrane binding. 1 Publication1
Mutagenesisi419E → 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 Publication1
Mutagenesisi449W → A: Reduces LOX-activity in the absence of membranes and increases activity in the presence of liposomes. May alter protein structure. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002207241 – 1066Allene oxide synthase-lipoxygenase proteinAdd BLAST1066

Proteomic databases

PRIDEiO16025.

Interactioni

Subunit structurei

Dimer.2 Publications

Structurei

Secondary structure

11066
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 15Combined sources9
Helixi17 – 27Combined sources11
Turni35 – 37Combined sources3
Helixi38 – 59Combined sources22
Turni60 – 62Combined sources3
Beta strandi65 – 67Combined sources3
Beta strandi69 – 79Combined sources11
Beta strandi89 – 91Combined sources3
Beta strandi96 – 107Combined sources12
Beta strandi113 – 115Combined sources3
Beta strandi117 – 128Combined sources12
Beta strandi133 – 141Combined sources9
Helixi147 – 153Combined sources7
Helixi160 – 166Combined sources7
Helixi170 – 179Combined sources10
Beta strandi181 – 183Combined sources3
Helixi187 – 189Combined sources3
Beta strandi198 – 201Combined sources4
Beta strandi207 – 219Combined sources13
Helixi223 – 225Combined sources3
Helixi232 – 235Combined sources4
Turni236 – 239Combined sources4
Helixi253 – 264Combined sources12
Beta strandi267 – 277Combined sources11
Helixi284 – 287Combined sources4
Turni295 – 297Combined sources3
Beta strandi301 – 311Combined sources11
Helixi314 – 319Combined sources6
Beta strandi337 – 341Combined sources5
Helixi344 – 362Combined sources19
Turni363 – 365Combined sources3
Beta strandi374 – 382Combined sources9
Beta strandi394 – 400Combined sources7
Beta strandi408 – 410Combined sources3
Beta strandi423 – 431Combined sources9
Beta strandi434 – 443Combined sources10
Beta strandi455 – 464Combined sources10
Beta strandi467 – 469Combined sources3
Beta strandi471 – 485Combined sources15
Helixi499 – 515Combined sources17
Helixi534 – 536Combined sources3
Helixi539 – 541Combined sources3
Helixi545 – 568Combined sources24
Turni569 – 571Combined sources3
Helixi577 – 584Combined sources8
Beta strandi590 – 592Combined sources3
Turni594 – 600Combined sources7
Helixi602 – 611Combined sources10
Helixi632 – 635Combined sources4
Helixi636 – 638Combined sources3
Helixi645 – 651Combined sources7
Beta strandi654 – 658Combined sources5
Helixi660 – 662Combined sources3
Beta strandi698 – 703Combined sources6
Beta strandi709 – 719Combined sources11
Beta strandi721 – 724Combined sources4
Helixi734 – 754Combined sources21
Helixi755 – 761Combined sources7
Helixi762 – 775Combined sources14
Helixi781 – 790Combined sources10
Helixi793 – 803Combined sources11
Helixi810 – 814Combined sources5
Turni816 – 820Combined sources5
Helixi821 – 830Combined sources10
Helixi835 – 838Combined sources4
Helixi840 – 846Combined sources7
Turni852 – 854Combined sources3
Helixi859 – 882Combined sources24
Helixi886 – 891Combined sources6
Helixi893 – 905Combined sources13
Beta strandi911 – 913Combined sources3
Helixi925 – 939Combined sources15
Helixi941 – 947Combined sources7
Helixi950 – 954Combined sources5
Helixi957 – 959Combined sources3
Beta strandi970 – 973Combined sources4
Helixi977 – 983Combined sources7
Helixi987 – 1000Combined sources14
Beta strandi1009 – 1011Combined sources3
Helixi1021 – 1046Combined sources26
Beta strandi1048 – 1050Combined sources3
Helixi1057 – 1059Combined sources3
Beta strandi1060 – 1063Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO16025.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini374 – 490PLATPROSITE-ProRule annotationAdd BLAST117
Domaini491 – 1066LipoxygenasePROSITE-ProRule annotationAdd BLAST576

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 371Allene oxide synthaseAdd BLAST371
Regioni372 – 1066Arachidonate 8-lipoxygenaseAdd BLAST695

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.
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.
PfamiPF00305. 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.
PIRiT30903.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei5626. PhoKatLox01.

Proteomic databases

PRIDEiO16025.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00383.
BRENDAi1.13.11.40. 4917.

Miscellaneous databases

EvolutionaryTraceiO16025.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
2.60.60.20. 1 hit.
InterProiIPR020835. Catalase-like_dom.
IPR011614. Catalase_core.
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.
PfamiPF00305. 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]
ProtoNetiSearch...

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 2, 2016
This is version 102 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

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.