LOXA_PSEAE
ID LOXA_PSEAE Reviewed; 685 AA.
AC Q9I4G8;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Lipoxygenase LoxA {ECO:0000303|PubMed:27500637};
DE EC=1.13.11.- {ECO:0000269|PubMed:27500637};
DE AltName: Full=Arachidonate 15-lipoxygenase;
DE Short=15-LOX;
DE EC=1.13.11.33 {ECO:0000269|PubMed:14766977, ECO:0000269|PubMed:27500637};
DE Flags: Precursor;
GN Name=loxA; OrderedLocusNames=PA1169;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=14766977; DOI=10.1073/pnas.0307308101;
RA Vance R.E., Hong S., Gronert K., Serhan C.N., Mekalanos J.J.;
RT "The opportunistic pathogen Pseudomonas aeruginosa carries a secretable
RT arachidonate 15-lipoxygenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2135-2139(2004).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31474948; DOI=10.3389/fmicb.2019.01826;
RA Morello E., Perez-Berezo T., Boisseau C., Baranek T., Guillon A., Brea D.,
RA Lanotte P., Carpena X., Pietrancosta N., Herve V., Ramphal R., Cenac N.,
RA Si-Tahar M.;
RT "Pseudomonas aeruginosa Lipoxygenase LoxA contributes to lung infection by
RT altering the host immune lipid signaling.";
RL Front. Microbiol. 10:1826-1826(2019).
RN [4] {ECO:0007744|PDB:5IR4, ECO:0007744|PDB:5IR5}
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 9-685 IN COMPLEX WITH IRON AND
RP MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY,
RP AND COFACTOR.
RX PubMed=27500637; DOI=10.1016/j.bbalip.2016.08.002;
RA Banthiya S., Kalms J., Galemou Yoga E., Ivanov I., Carpena X., Hamberg M.,
RA Kuhn H., Scheerer P.;
RT "Structural and functional basis of phospholipid oxygenase activity of
RT bacterial lipoxygenase from Pseudomonas aeruginosa.";
RL Biochim. Biophys. Acta 1861:1681-1692(2016).
CC -!- FUNCTION: Exhibits lipoxin synthase activity as part of a bacterial
CC evasion strategy to suppress the host immune defense (PubMed:31474948).
CC Oxygenates polyenoic fatty acids including eicosatrienoate and
CC docosahexaenoate to the corresponding (n-6)S-hydroperoxy derivatives
CC (PubMed:14766977, PubMed:27500637). In turn, this production of
CC bioactive lipid mediators promotes bacterial persistence in host lung
CC tissues by inhibiting the expression of major chemokines and
CC recruitment of leukocytes (PubMed:31474948).
CC {ECO:0000269|PubMed:14766977, ECO:0000269|PubMed:27500637,
CC ECO:0000269|PubMed:31474948}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = (15S)-hydroperoxy-
CC (8Z,11Z,13E)-eicosatrienoate; Xref=Rhea:RHEA:61524,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:144787;
CC Evidence={ECO:0000269|PubMed:27500637};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61525;
CC Evidence={ECO:0000305|PubMed:27500637};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (17S)-
CC hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate;
CC Xref=Rhea:RHEA:50840, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:133795; Evidence={ECO:0000269|PubMed:27500637};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50841;
CC Evidence={ECO:0000305|PubMed:27500637};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15S)-hydroperoxy-
CC (5Z,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:16869,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57446;
CC EC=1.13.11.33; Evidence={ECO:0000269|PubMed:14766977,
CC ECO:0000269|PubMed:27500637};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16870;
CC Evidence={ECO:0000305|PubMed:27500637};
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;
CC Evidence={ECO:0000269|PubMed:27500637};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22781;
CC Evidence={ECO:0000305|PubMed:27500637};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z,14Z)-eicosadienoate + O2 = (15S)-hydroperoxy-(11Z,13E)-
CC eicosadienoate; Xref=Rhea:RHEA:61572, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:77220, ChEBI:CHEBI:144832;
CC Evidence={ECO:0000269|PubMed:27500637};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61573;
CC Evidence={ECO:0000305|PubMed:27500637};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00726,
CC ECO:0000269|PubMed:27500637};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00726, ECO:0000269|PubMed:27500637};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:27500637}.
CC -!- SUBCELLULAR LOCATION: Periplasm. Secreted
CC {ECO:0000269|PubMed:31474948}. Note=Periplasmic with some activity
CC further secreted to the extracellular milieu.
CC {ECO:0000269|PubMed:31474948}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG04558.1; -; Genomic_DNA.
DR PIR; A83499; A83499.
DR RefSeq; NP_249860.1; NC_002516.2.
DR RefSeq; WP_010895542.1; NZ_QZGE01000006.1.
DR PDB; 5IR4; X-ray; 1.48 A; A=9-685.
DR PDB; 5IR5; X-ray; 1.90 A; A=9-685.
DR PDBsum; 5IR4; -.
DR PDBsum; 5IR5; -.
DR AlphaFoldDB; Q9I4G8; -.
DR SMR; Q9I4G8; -.
DR STRING; 287.DR97_765; -.
DR PaxDb; Q9I4G8; -.
DR PRIDE; Q9I4G8; -.
DR EnsemblBacteria; AAG04558; AAG04558; PA1169.
DR GeneID; 879547; -.
DR KEGG; pae:PA1169; -.
DR PATRIC; fig|208964.12.peg.1214; -.
DR PseudoCAP; PA1169; -.
DR HOGENOM; CLU_004282_3_2_6; -.
DR InParanoid; Q9I4G8; -.
DR OMA; CMDHWKE; -.
DR BioCyc; PAER208964:G1FZ6-1194-MON; -.
DR BRENDA; 1.13.11.33; 5087.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0050473; F:arachidonate 15-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
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; Fatty acid metabolism; Iron; Lipid metabolism;
KW Metal-binding; Oxidoreductase; Periplasm; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..685
FT /note="Lipoxygenase LoxA"
FT /id="PRO_0000018329"
FT DOMAIN 122..685
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:27500637,
FT ECO:0007744|PDB:5IR4"
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 ECO:0000269|PubMed:27500637, ECO:0007744|PDB:5IR4"
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 ECO:0000269|PubMed:27500637, ECO:0007744|PDB:5IR4"
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 ECO:0000269|PubMed:27500637, ECO:0007744|PDB:5IR4"
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 ECO:0000269|PubMed:27500637, ECO:0007744|PDB:5IR4"
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 ECO:0000269|PubMed:27500637, ECO:0007744|PDB:5IR4"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 33..47
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 60..76
FT /evidence="ECO:0007829|PDB:5IR4"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5IR4"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 103..123
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 126..159
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 164..199
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:5IR4"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:5IR4"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:5IR4"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:5IR4"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:5IR4"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:5IR4"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:5IR4"
FT STRAND 326..335
FT /evidence="ECO:0007829|PDB:5IR4"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:5IR4"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 351..374
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 375..381
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 382..395
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 401..406
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 413..423
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 430..434
FT /evidence="ECO:0007829|PDB:5IR4"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 439..452
FT /evidence="ECO:0007829|PDB:5IR4"
FT TURN 455..458
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 460..466
FT /evidence="ECO:0007829|PDB:5IR4"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 479..502
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 506..510
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 513..523
FT /evidence="ECO:0007829|PDB:5IR4"
FT TURN 524..526
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 537..551
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 553..559
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 562..565
FT /evidence="ECO:0007829|PDB:5IR4"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:5IR4"
FT TURN 569..571
FT /evidence="ECO:0007829|PDB:5IR4"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:5IR4"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 589..593
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 599..612
FT /evidence="ECO:0007829|PDB:5IR4"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 637..640
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 645..666
FT /evidence="ECO:0007829|PDB:5IR4"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:5IR4"
FT HELIX 676..678
FT /evidence="ECO:0007829|PDB:5IR4"
SQ SEQUENCE 685 AA; 74804 MW; B6A307595AE16A5E CRC64;
MKRRSVLLSG VALSGTALAN DSIFFSPLKY LGAEQQRSID ASRSLLDNLI PPSLPQYDNL
AGKLARRAVL TSKKLVYVWT ENFGNVKGVP MARSVPLGEL PNVDWLLKTA GVIVELIVNF
VASLPASAAA QFERIATGLS GDLEAARQVH EALLEEAKND PAAAGSLLLR FTELQTRVIA
ILTRVGLLVD DILKSASNLV TQRGQGDGLN RFRAVFGTLR LPEVADSFRD DEAFAYWRVA
GPNPLLIRRV DALPANFPLG EEQFRRVMGA DDSLLEAAAS RRLYLLDYAE LGKLAPSGAV
DKLLTGTGFA YAPIALFALG KDRARLLPVA IQCGQDPATH PMFVRPAESE SDLYWGWQMA
KTVVQVAEEN YHEMFVHLAQ THLVSEAFCL ATQRTLAPSH PLHVLLAPHF EGTLFINEGA
ARILLPSAGF IDVMFAAPIQ DTQATAGGNR LGFDFYRGML PESLKARNVD DPLALPDYPY
RDDGLLVWNA IRQWAADYVA VYYASDGDVT ADVELAAWVG EVIGSGKVAG FRPITGRSQL
VEVLTMVIFT ASAQHAAVNF PQPSMMTYAP AICAMSAAPA PDSPSGKSEA DWLKMMPPTL
VALEKVNIYH LLGSVYHGRL GDYRQTGFPY APVFSDRRVT ASGGPLERFQ ARLKEVEATI
RTRNQARRRP YEYLLPSRIP ASTNI
