Reviewed, UniProtKB/Swiss-Prot Q8RNT4 (LOX_PSEAE)

Names and origin

Protein names

Recommended name:
    Oleic acid lipoxygenase
    EC=1.13.11.-

Gene names

Name:

lox

Organism

Pseudomonas aeruginosa

Taxonomic identifier

287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	685 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	In presence of oxygen, converts oleic acid into (S)-(E)-10-hydroperoxy-8-octadecenoic acid (HPOD), which spontaneously decomposes to the corresponding (E)-10-hydroxy-8-octadecenoic acid (HOD). In vivo, the reaction leads to the dihydroxy derivative (E)-7,10-dihydroxy-8-octadecenoic acid (DHOD), so that the three hydroxy-fatty acids can be isolated from the culture medium. Also active on linoleic acid and linolenic acid. Almost not active on arachidonic acid.
Cofactor	Binds 1 iron ion per subunit.
Enzyme regulation	Activated by Fe2+, Sn2+, Ag2+, Hg2+, Cd2+, Ca2+ and Cu2+. Inhibited by Ba2+, Zn2+ and Fe3+.
Subunit structure	Monomer.
Subcellular location	Periplasm.
Miscellaneous	In vitro, under anaerobic conditions, does not transform oleic acid into the corresponding hydroxy derivative HOD.
Sequence similarities	Belongs to the lipoxygenase family. Contains 1 lipoxygenase domain.
Biophysicochemical properties	Kinetic parameters: KM=0.74 mM for oleic acid KM=0.66 mM for linoleic acid KM=0.73 mM for linolenic acid Vmax=0.246 µmol/min/mg enzyme with oleic acid as substrate pH dependence: Optimum pH is 8.5-9.0. Temperature dependence: Optimum temperature is 25-30 degrees Celsius. Active up to 45 degrees Celsius, less active after 50 degrees Celsius and completely inactive at 70 degrees Celsius.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 685	666	Oleic acid lipoxygenase		PRO_0000018330
Regions
	Domain	122 – 685	564	Lipoxygenase
Sites
	Metal binding	377	1	Iron; catalytic By similarity
	Metal binding	382	1	Iron; catalytic By similarity
	Metal binding	555	1	Iron; catalytic By similarity
	Metal binding	559	1	Iron; catalytic By similarity
	Metal binding	685	1	Iron; via carboxylate; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8RNT4-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: DA863B58A47C4C29	FASTA	685	74,573
	10 20 30 40 50 60 MKRRSVLLSG VALSGTALAN DSIFFSPLKY LGAEQQRSID ASRSLLDNLI PPSLPQYDNL 70 80 90 100 110 120 AGKLARRAVL TSKKLAYVWT ENFANVKGVP MARSVPLGEL PNVDWLLKTA GVIVELIVNS 130 140 150 160 170 180 FASLPASAAA QFERIPAGLN GDLEAARQVH EALLEEAKND PAAAGSLLLR FTELQTRVIA 190 200 210 220 230 240 LLTRVGLLVD DILKSASNLV TQGGQGDGLN RFRAVFGTLR LPEVADSFRD DEAFAYWRVA 250 260 270 280 290 300 GPNPLLIRRV DALPANFPLG EEQFRRVMGA DDSLLEAAAS RRLYLLDYAE LGKLAPSGAV 310 320 330 340 350 360 DKLLTGTGFA YAPIALFALG KDRARLLPVA IQCGQDPATH PMFVRPAESE SDLYWGWQMA 370 380 390 400 410 420 KTVVLVAEEN YHEMFVHLAQ THLVSEAFCL ATQRTLAPSH PLHVLLAPHF EGTLFVNEGA 430 440 450 460 470 480 ARILLPSAGF IDVMFAAPIQ DTQATAGGNR LGFDFYRGML PESLKARNVD DPAALPDYPY 490 500 510 520 530 540 RDDGLLVWNA IRQWAADYVA VYYASDGDVT ADVELAAWVG EVIGSGKVAG FRPITGRSQL 550 560 570 580 590 600 VEVLTMVIFT ASAQHAAVNF PQPSMMTYAP AICAMSAAPA PDSPSGKSEA DWLKMMPPAL 610 620 630 640 650 660 VALEKVNIYH LLGSVYHGRL GDYRQTGFPY APVFSDRRVT ASGGPLERFQ ARLKEVEATI 670 680 RTRNQARRKP YEYLLPSRIP ASTNI

References

[1]

"Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-( E)-10-hydroxy-8-octadecenoic acid." Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A., Manresa A. Antonie Van Leeuwenhoek 85:129-139(2004) [PubMed: 15028873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: 42A2 / NCIMB 40045.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF479686 Genomic DNA. Translation: AAL85880.1.
3D structure databases
HSSP	HSSP built from PDB template 2SBL based on UniProtKB P08170.
ModBase	Search...
Family and domain databases
InterPro	IPR000907. LipOase. IPR013819. LipOase_C. [Graphical view]
PANTHER	PTHR11771. LipOase. 1 hit.
Pfam	PF00305. Lipoxygenase. 3 hits. [Graphical view]
PRINTS	PR00087. LIPOXYGENASE.
PROSITE	PS00711. LIPOXYGENASE_1. 1 hit. PS00081. LIPOXYGENASE_2. 1 hit. PS51393. LIPOXYGENASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LOX_PSEAE

Accession

Primary (citable) accession number: Q8RNT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	June 1, 2002
Last modified:	June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)