MNLOX_GAETR
ID MNLOX_GAETR Reviewed; 618 AA.
AC Q8X150;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Manganese lipoxygenase {ECO:0000303|PubMed:9582345};
DE Short=Mn-LO {ECO:0000303|PubMed:9582345};
DE Short=MnLOX {ECO:0000303|PubMed:12047377};
DE EC=1.13.11.- {ECO:0000269|PubMed:10751400, ECO:0000269|PubMed:9582345};
DE EC=1.13.11.45 {ECO:0000269|PubMed:10751400, ECO:0000269|PubMed:9582345};
DE AltName: Full=Linoleate 11S-lipoxygenase {ECO:0000305|PubMed:9582345};
DE AltName: Full=Linoleate 13R-lipoxygenase {ECO:0000305|PubMed:9582345};
DE AltName: Full=Manganese 13R-lipoxygenase {ECO:0000250|UniProtKB:Q8X151};
DE Short=13R-MnLOX {ECO:0000250|UniProtKB:Q8X151};
DE Flags: Precursor;
OS Gaeumannomyces tritici (Wheat and barley take-all root rot fungus)
OS (Gaeumannomyces graminis var. tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Gaeumannomyces.
OX NCBI_TaxID=36779;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-595, PROTEIN SEQUENCE OF 212-267; 312-320;
RP 382-391; 489-500; 528-538; 551-569 AND 585-617, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RC STRAIN=CBS 905.73;
RX PubMed=12047377; DOI=10.1046/j.1432-1033.2002.02936.x;
RA Hornsten L., Su C., Osbourn A.E., Hellman U., Oliw E.H.;
RT "Cloning of the manganese lipoxygenase gene reveals homology with the
RT lipoxygenase gene family.";
RL Eur. J. Biochem. 269:2690-2697(2002).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS.
RC STRAIN=CBS 905.73;
RA Sugio A., Takagi S., Christensen S.R., Oestergaard L., Oliw E.H.;
RT "Lipoxygenase.";
RL Patent number WO0220730, 14-MAR-2002.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND GLYCOSYLATION.
RX PubMed=9582345; DOI=10.1074/jbc.273.21.13072;
RA Su C., Oliw E.H.;
RT "Manganese lipoxygenase. Purification and characterization.";
RL J. Biol. Chem. 273:13072-13079(1998).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10751400; DOI=10.1074/jbc.m001408200;
RA Su C., Sahlin M., Oliw E.H.;
RT "Kinetics of manganese lipoxygenase with a catalytic mononuclear redox
RT center.";
RL J. Biol. Chem. 275:18830-18835(2000).
CC -!- FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-linolenic
CC acids to 11S- and 13R-hydroperoxy fatty acids. At the end of
CC lipoxygenation, the intermediate product 11S-HPODE from linoleic acid
CC is then transformed into 13R-HPODE as the final product. It also acts
CC on alpha-linolenic acid producing 11S-HPOTrE and 13R-HPOTrE with
CC subsequent transformation of 11S-HPOTrE to 13R-HPOTrE as the final
CC product. Gamma-linolenic acid is a poor substrate. Oleate and
CC arachidonate are not substrates. {ECO:0000269|PubMed:10751400,
CC ECO:0000269|PubMed:9582345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (11S)-hydroperoxy-(9Z,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:18993, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:57467; EC=1.13.11.45;
CC Evidence={ECO:0000269|PubMed:10751400, ECO:0000269|PubMed:9582345};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (13R)-hydroperoxy-(9Z,11E)-
CC octadecadienoate; Xref=Rhea:RHEA:51240, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:133985;
CC Evidence={ECO:0000269|PubMed:10751400, ECO:0000269|PubMed:9582345};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (11S)-hydroperoxy-
CC (9Z,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:51440,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:134110;
CC Evidence={ECO:0000250|UniProtKB:Q8X151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (13R)-hydroperoxy-
CC (9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:51244,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:133987;
CC Evidence={ECO:0000269|PubMed:10751400, ECO:0000269|PubMed:9582345};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10751400};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 uM for linoleate {ECO:0000269|PubMed:9582345};
CC KM=2.4 uM for alpha-linoleate {ECO:0000269|PubMed:9582345};
CC KM=31 uM for oxygen {ECO:0000269|PubMed:9582345};
CC KM=8.1 uM for 11S-HPODE (for isomerization to 13R-HPODE reaction)
CC {ECO:0000269|PubMed:10751400};
CC Vmax=8.2 umol/min/mg enzyme for linoleate
CC {ECO:0000269|PubMed:9582345};
CC Vmax=17.6 umol/min/mg enzyme for alpha-linoleate
CC {ECO:0000269|PubMed:9582345};
CC Vmax=10.4 umol/min/mg enzyme towards oxygen
CC {ECO:0000269|PubMed:9582345};
CC Vmax=7.5 umol/min/mg enzyme for 11S-HPODE (for isomerization to 13R-
CC HPODE reaction) {ECO:0000269|PubMed:10751400};
CC pH dependence:
CC Optimum pH is 7. Active from pH 5 to pH 11.
CC {ECO:0000269|PubMed:9582345};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Enzyme activity decreases
CC sharply above 63 degrees Celsius. {ECO:0000269|PubMed:9582345};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12047377,
CC ECO:0000269|PubMed:9582345}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:12047377,
CC ECO:0000269|PubMed:9582345}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; AY040825; AAK81883.1; -; mRNA.
DR AlphaFoldDB; Q8X150; -.
DR SMR; Q8X150; -.
DR SABIO-RK; Q8X150; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050584; F:linoleate 11-lipoxygenase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043651; P:linoleic acid metabolic process; IC:UniProtKB.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR PANTHER; PTHR11771; PTHR11771; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR SUPFAM; SSF48484; SSF48484; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Direct protein sequencing; Glycoprotein; Manganese;
KW Metal-binding; Oxidoreductase; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 17..618
FT /note="Manganese lipoxygenase"
FT /evidence="ECO:0000255"
FT /id="PRO_5004316175"
FT DOMAIN 47..617
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 36..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 290
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 294
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 478
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 482
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 618
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 222
FT /note="K -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="V -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="A -> W (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="R -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="Y -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 618 AA; 67620 MW; ABC5229CA8F86F37 CRC64;
MRSRILAIVF AARHVAALPL AAEDAAATLS LTSSASSTTV LPSPTQYTLP NNDPNQGARN
ASIARKRELF LYGPSTLGQT TFYPTGELGN NISARDVLLW RQDAANQTAT AYREANETFA
DITSRGGFKT LDDFALLYNG HWKESVPEGI SKGMLSNYTS DLLFSMERLS SNPYVLKRLH
PTKDKLPFSV ESKVVKKLTA TTLEALHKGG RLFLVDHSYQ KKYTPQPGRY AAACQGLFYL
DARSNQFLPL AIKTNVGADL TYTPLDDKND WLLAKIMFNN NDLFYSQMYH VLFHTIPEIV
HEAAFRTLSD RHPVMGVLNR LMYQAYAIRP VGGAVLFNPG GFWDQNFGLP ASAAIDFPGS
VYAQGGGGFQ AGYLEKDLRS RGLVGEDSGP RLPHFPFYED AHRLIGAIRR FMQAFVDSTY
GADDGDDGAL LRDYELQNWI AEANGPAQVR DFPAAPLRRR AQLVDVLTHV AWVTGGAHHV
MNQGSPVKFS GVVPLHPAAL YAPIPTTKGA TGNGTRAGLL AWLPNERQAV EQVSLLARFN
RAQVGDRKQT VRDAFAAPDL LAGNGPGYAA ANARFVEDTG RISREMAGRG FDGKGLSQGM
PFVWTALNPA VNPFFLSV
