LOX_PSEAI
ID LOX_PSEAI Reviewed; 685 AA.
AC Q8RNT4;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Linoleate 9/13-lipoxygenase;
DE EC=1.13.11.12 {ECO:0000269|Ref.4};
DE EC=1.13.11.58 {ECO:0000269|PubMed:15028873, ECO:0000269|PubMed:15803390, ECO:0000269|Ref.4};
DE AltName: Full=Oleate 10S-lipoxygenase;
DE EC=1.13.11.77 {ECO:0000269|PubMed:15028873, ECO:0000269|PubMed:15803390, ECO:0000269|Ref.4};
DE Flags: Precursor;
GN Name=lox;
OS Pseudomonas aeruginosa.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=42A2 / NCIMB 40045;
RX PubMed=15803390; DOI=10.1007/s10482-004-4021-1;
RA Vidal-Mas J., Busquets M., Manresa A.;
RT "Cloning and expression of a lipoxygenase from Pseudomonas aeruginosa
RT 42A2.";
RL Antonie Van Leeuwenhoek 87:245-251(2005).
RN [2]
RP SEQUENCE REVISION.
RA Vidal-Mas J., Besumbes O., Manresa M., Busquets M.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=42A2 / NCIMB 40045;
RX PubMed=15028873; DOI=10.1023/b:anto.0000020152.15440.65;
RA Busquets M., Deroncele V., Vidal-Mas J., Rodriguez E., Guerrero A.,
RA Manresa A.;
RT "Isolation and characterization of a lipoxygenase from Pseudomonas 42A2
RT responsible for the biotransformation of oleic acid into (S)-(E)-10-
RT hydroxy-8-octadecenoic acid.";
RL Antonie Van Leeuwenhoek 85:129-139(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=42A2 / NCIMB 40045;
RA Vidal-Mas J.;
RT "Cloning, expression and characterization of the lipoxygenase of
RT Pseudomonas aeruginosa 42A2.";
RL Thesis (2005), University of Barcelona, Spain.
CC -!- FUNCTION: In presence of oxygen, converts linoleate into (9S)-
CC hydroperoxy-10,12-octadecenoate (9HPOD), which spontaneously decomposes
CC to the corresponding 9-hydroxy-10,12-octadecenoate (9HOD), and into 13-
CC hydroperoxy-9,11-octadecenoate (13HPOD) which spontaneously decomposes
CC to the corresponding 13-hydroxy-9,11-octadecenoate (13HOD). Also active
CC on linolenate. To a lesser extent, is also able to convert oleate into
CC (10S)-hydroperoxy-8E-octadecenoate, which spontaneously decomposes to
CC the corresponding 10-hydroxy-8E-octadecenoate. Is almost not active on
CC arachidonate. {ECO:0000269|PubMed:15028873,
CC ECO:0000269|PubMed:15803390, ECO:0000269|Ref.4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58;
CC Evidence={ECO:0000269|PubMed:15028873, ECO:0000269|PubMed:15803390,
CC ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + O2 = (8E,10S)-10-hydroperoxy-octadeca-8-
CC enoate; Xref=Rhea:RHEA:37907, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75341; EC=1.13.11.77;
CC Evidence={ECO:0000269|PubMed:15028873, ECO:0000269|PubMed:15803390,
CC ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (8E,10S,12Z)-10-
CC hydroperoxyoctadeca-8,12-dienoate; Xref=Rhea:RHEA:37919,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:75346;
CC EC=1.13.11.77; Evidence={ECO:0000269|PubMed:15028873,
CC ECO:0000269|PubMed:15803390, ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (8E,10S,12Z,15Z)-10-
CC hydroperoxyoctadeca-8,12,15-trienoate; Xref=Rhea:RHEA:37923,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:75348;
CC EC=1.13.11.77; Evidence={ECO:0000269|PubMed:15028873,
CC ECO:0000269|PubMed:15803390, ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-
CC octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12;
CC Evidence={ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (13S)-hydroperoxy-
CC (9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:34495,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:58757;
CC EC=1.13.11.12; Evidence={ECO:0000269|Ref.4};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000305|PubMed:15028873};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000305|PubMed:15028873};
CC -!- ACTIVITY REGULATION: Inhibited by Ba(2+), Zn(2+) and Fe(3+).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=78.9 uM for linoleate (Ref.4) {ECO:0000269|PubMed:15028873,
CC ECO:0000269|Ref.4};
CC KM=0.74 mM for oleate {ECO:0000269|PubMed:15028873,
CC ECO:0000269|Ref.4};
CC KM=0.66 mM for linoleate {ECO:0000269|PubMed:15028873,
CC ECO:0000269|Ref.4};
CC KM=0.73 mM for linolenate {ECO:0000269|PubMed:15028873,
CC ECO:0000269|Ref.4};
CC Vmax=0.246 umol/min/mg enzyme with oleate as substrate
CC {ECO:0000269|PubMed:15028873, ECO:0000269|Ref.4};
CC Vmax=81.75 umol/min/mg enzyme with linoleate as substrate (Ref.4)
CC {ECO:0000269|PubMed:15028873, ECO:0000269|Ref.4};
CC Note=kcat is 96 sec(-1) with linoleate as substrate (Ref.4).;
CC pH dependence:
CC Optimum pH is 7 with linoleate as substrate, and 8.5-9.0 with oleate
CC as substrate. {ECO:0000269|PubMed:15028873, ECO:0000269|Ref.4};
CC Temperature dependence:
CC Optimum temperature is 25-30 degrees Celsius. Active up to 45 degrees
CC Celsius, less active after 50 degrees Celsius and completely inactive
CC at 70 degrees Celsius. {ECO:0000269|PubMed:15028873,
CC ECO:0000269|Ref.4};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15028873}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|PROSITE-ProRule:PRU00726,
CC ECO:0000269|PubMed:15028873}.
CC -!- MISCELLANEOUS: In vitro, under anaerobic conditions, does not transform
CC linoleate or oleate into the corresponding hydroxy derivative.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
CC -!- CAUTION: The biochemical characterization done in PubMed:15028873 is
CC devoted to oleic acid, however, the preferred substrate of the enzyme
CC is linoleic acid. {ECO:0000305}.
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DR EMBL; AF479686; AAL85880.2; -; Genomic_DNA.
DR PDB; 4G32; X-ray; 1.75 A; A=19-685.
DR PDB; 4G33; X-ray; 2.03 A; A=19-685.
DR PDB; 4RPE; X-ray; 1.60 A; A=19-685.
DR PDB; 5LC8; X-ray; 1.80 A; A=19-685.
DR PDBsum; 4G32; -.
DR PDBsum; 4G33; -.
DR PDBsum; 4RPE; -.
DR PDBsum; 5LC8; -.
DR AlphaFoldDB; Q8RNT4; -.
DR SMR; Q8RNT4; -.
DR KEGG; ag:AAL85880; -.
DR eggNOG; COG0753; Bacteria.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR PANTHER; PTHR11771; PTHR11771; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR SUPFAM; SSF48484; SSF48484; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Periplasm;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..685
FT /note="Linoleate 9/13-lipoxygenase"
FT /id="PRO_0000018330"
FT DOMAIN 122..685
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 377
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 382
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 555
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 559
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 685
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 33..47
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 60..76
FT /evidence="ECO:0007829|PDB:4RPE"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4RPE"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 103..122
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:4RPE"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 133..159
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 168..199
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:4RPE"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:4RPE"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:4RPE"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:4RPE"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:4RPE"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:4RPE"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:4RPE"
FT STRAND 326..335
FT /evidence="ECO:0007829|PDB:4RPE"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:4RPE"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 351..374
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 375..381
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 382..395
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 401..406
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 413..423
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 430..434
FT /evidence="ECO:0007829|PDB:4RPE"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 439..452
FT /evidence="ECO:0007829|PDB:4RPE"
FT TURN 455..458
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 460..466
FT /evidence="ECO:0007829|PDB:4RPE"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 479..502
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 506..510
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 513..524
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 537..551
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 553..559
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 562..565
FT /evidence="ECO:0007829|PDB:4RPE"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:4RPE"
FT TURN 569..571
FT /evidence="ECO:0007829|PDB:4RPE"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:4RPE"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 589..593
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 599..612
FT /evidence="ECO:0007829|PDB:4RPE"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 637..640
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 645..666
FT /evidence="ECO:0007829|PDB:4RPE"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:4RPE"
FT HELIX 676..678
FT /evidence="ECO:0007829|PDB:4RPE"
SQ SEQUENCE 685 AA; 74519 MW; 4F56EFE0780295FA CRC64;
MKRRSVLLSG VALSGTALAN DSIFFSPLKY LGAEQQRSID ASRSLLDNLI PPSLPQYDNL
AGKLARRAVL TSKKLVYVWT ENFANVKGVP MARSVPLGEL PNVDWLLKTA GVIVELIVNF
VASLPASAAA QFERIAAGLS GDLEAARQVH EALLEEAKND PAAAGSLLLR FTELQTRVIA
LLTRVGLLVD DILKSASNLV TQGGQGDGLN RFRAVFGTLR LPEVADSFRD DEAFAYWRVA
GPNPLLIRRV DALPANFPLG EEQFRRVMGA DDSLLEAAAS RRLYLLDYAE LGKLAPSGAV
DKLLTGTGFA YAPIALFALG KDRAGLLPVA IQCGQDPATH PMFVRPAESE SDLYWGWQMA
KTVVQVAEEN YHEMFVHLAQ THLVSEAFCL ATQRTLAPSH PLHVLLAPHF EGTLFINEGA
ARILLPSAGF IDVMFAAPIQ DTQATAGGNR LGFDFYRGML PESLKARNVD DPAALPDYPY
RDDGLLVWNA IRQWAADYVA VYYASDGDVT ADVELAAWVG EVIGSGKVAG FRPITGRSQL
VEVLTMVIFT ASAQHAAVNF PQPSMMTYAP AICAMSAAPA PDSPSGKSEA DWLKMMPPTL
VALEKVNIYH LLGSVYHGRL GDYRQTGFPY APVFSDRRVT ASGGPLERFQ ARLKEVEATI
RTRNQARRKP YEYLLPSRIP ASTNI
