MNLOX_MAGO7
ID MNLOX_MAGO7 Reviewed; 619 AA.
AC G4NAP4; A0A0M4MCV3; Q52YI5; Q52ZN7;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Manganese lipoxygenase {ECO:0000303|PubMed:26264916};
DE Short=MnLOX {ECO:0000303|PubMed:26264916};
DE EC=1.13.11.- {ECO:0000269|PubMed:26264916};
DE EC=1.13.11.45 {ECO:0000269|PubMed:26264916};
DE EC=1.13.11.58 {ECO:0000269|PubMed:26264916};
DE AltName: Full=Manganese 9S/11S-lipoxygenase;
DE Short=9S/11S-MnLOX;
DE Flags: Precursor;
GN ORFNames=MGG_08499;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], REVISION OF GENE MODEL, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=Guyane 11;
RX PubMed=26264916; DOI=10.1016/j.abb.2015.07.014;
RA Wennman A., Jerneren F., Magnuson A., Oliw E.H.;
RT "Expression and characterization of manganese lipoxygenase of the rice
RT blast fungus reveals prominent sequential lipoxygenation of alpha-linolenic
RT acid.";
RL Arch. Biochem. Biophys. 583:87-95(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [3] {ECO:0007744|PDB:5FNO}
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 17-619 IN COMPLEX WITH MANGANESE,
RP GLYCOSYLATION AT ASN-86; ASN-164 AND ASN-549, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF ARG-539 AND PHE-540.
RX PubMed=26783260; DOI=10.1074/jbc.m115.707380;
RA Wennman A., Oliw E.H., Karkehabadi S., Chen Y.;
RT "Crystal structure of manganese lipoxygenase of the rice blast fungus
RT Magnaporthe oryzae.";
RL J. Biol. Chem. 291:8130-8139(2016).
CC -!- FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-linolenic
CC acids to 9S-, 11- and 13R-hydroperoxy fatty acids. At the end of
CC lipoxygenation, the intermediate product 11S-HPODE from linoleic acid
CC is then transformed into 9S-HPODE and 13R-HPODE as the final products.
CC The intermediate product 11R-HPOTrE from alpha-linolenic acid is
CC transformed into 9S-HPOTrE and 13R-HPOTrE as the final products. 9S-
CC HPOTrE is further oxidized by the enzyme to 9S,16S-DiHPOTrE as the end
CC product. {ECO:0000269|PubMed:26264916}.
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:26264916};
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:26264916};
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:26264916};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (9S)-hydroperoxy-
CC (10E,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:51248,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:60962;
CC Evidence={ECO:0000269|PubMed:26264916};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (11R)-hydroperoxy-
CC (9Z,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:51252,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:133989;
CC Evidence={ECO:0000269|PubMed:26264916, ECO:0000269|PubMed:26783260};
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:26264916};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9S)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoate + O2 =
CC (9S,16S)-dihydroperoxy-(10E,12Z,14E)-octadecatrienoate;
CC Xref=Rhea:RHEA:51256, ChEBI:CHEBI:15379, ChEBI:CHEBI:60962,
CC ChEBI:CHEBI:133991; Evidence={ECO:0000269|PubMed:26264916,
CC ECO:0000269|PubMed:26783260};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:26783260};
CC Note=Three His residues, the carboxyl oxygen of the C-terminal Ile or
CC Val residue, and a fifth residue, usually Asn, ligate the metal, which
CC binds water to form a catalytic base Mn(2+)OH(2) for hydrogen
CC abstraction. {ECO:0000250|UniProtKB:Q8X151};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8X151}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. Manganese lipoxygenase
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EHA49687.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KT734829; ALE27899.1; -; mRNA.
DR EMBL; AY829440; AAX48918.1; -; mRNA.
DR EMBL; AY858988; AAX52528.1; -; Genomic_DNA.
DR EMBL; CM001234; EHA49687.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003716006.1; XM_003715958.1.
DR PDB; 5FNO; X-ray; 2.04 A; A/B=17-588.
DR PDBsum; 5FNO; -.
DR AlphaFoldDB; G4NAP4; -.
DR SMR; G4NAP4; -.
DR STRING; 318829.MGG_08499T0; -.
DR SwissLipids; SLP:000001658; -.
DR iPTMnet; G4NAP4; -.
DR PRIDE; G4NAP4; -.
DR EnsemblFungi; MGG_08499T0; MGG_08499T0; MGG_08499.
DR GeneID; 2678734; -.
DR KEGG; mgr:MGG_08499; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_4_0_1; -.
DR InParanoid; G4NAP4; -.
DR OrthoDB; 385042at2759; -.
DR BRENDA; 1.13.11.45; 5238.
DR SABIO-RK; G4NAP4; -.
DR Proteomes; UP000009058; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050584; F:linoleate 11-lipoxygenase activity; IDA:UniProtKB.
DR GO; GO:1990136; F:linoleate 9S-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 3D-structure; Dioxygenase; Glycoprotein; Manganese; Metal-binding;
KW Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..619
FT /note="Manganese lipoxygenase"
FT /id="PRO_5003466387"
FT DOMAIN 55..619
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 298
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26783260"
FT BINDING 303
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26783260"
FT BINDING 483
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26783260"
FT BINDING 487
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26783260"
FT BINDING 619
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26783260"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:26783260"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:26783260"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:26783260"
FT MUTAGEN 539
FT /note="R->A: Reduces catalytic activity towards alpha-
FT linoleate, but retains oxidation activity on 9S-HPOTrE."
FT /evidence="ECO:0000269|PubMed:26783260"
FT MUTAGEN 540
FT /note="F->L: Loss of oxidation activity on alpha-linoleate,
FT but retains oxidation activity on 9S-HPOTrE."
FT /evidence="ECO:0000269|PubMed:26783260"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:5FNO"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5FNO"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:5FNO"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 93..131
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:5FNO"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:5FNO"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:5FNO"
FT TURN 159..166
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 168..173
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:5FNO"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:5FNO"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:5FNO"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:5FNO"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:5FNO"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 278..300
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 303..316
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 322..330
FT /evidence="ECO:0007829|PDB:5FNO"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 337..343
FT /evidence="ECO:0007829|PDB:5FNO"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 351..355
FT /evidence="ECO:0007829|PDB:5FNO"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 360..374
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 382..388
FT /evidence="ECO:0007829|PDB:5FNO"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 404..427
FT /evidence="ECO:0007829|PDB:5FNO"
FT TURN 428..430
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 432..436
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 439..449
FT /evidence="ECO:0007829|PDB:5FNO"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 465..480
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 482..486
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 490..493
FT /evidence="ECO:0007829|PDB:5FNO"
FT TURN 494..496
FT /evidence="ECO:0007829|PDB:5FNO"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:5FNO"
FT STRAND 503..507
FT /evidence="ECO:0007829|PDB:5FNO"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 527..538
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:5FNO"
FT TURN 546..549
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 559..564
FT /evidence="ECO:0007829|PDB:5FNO"
FT HELIX 567..588
FT /evidence="ECO:0007829|PDB:5FNO"
SQ SEQUENCE 619 AA; 68374 MW; 944A7654BE3DB894 CRC64;
MRVLVWIAGL APLAVAVPSS SYRVAVAARA DNTSASVAPS QNVSGAAPPE LVVYTLPCED
GNSTARTAEI RLKQATLLYG PSLLGNASYF PGGPLGDAIS LRDQTVWEGA AVVQSLRAFT
DAAKVAANIK QNGGLNSLDD FKVLYQDGWK GSVPQGIARG QSENYTSDLL FSMERLSVNP
YILKRLHPTE DALPFQVDRA TVKQLTKTSL KALHAAGRLF VADHSYQRNY TRLANRYSAA
CTALFYLDPR SNQFLPLAIK TNVGADLTYT PLDTDNNNWL LAKIMFNNND LFHGQIFHVA
YPHAIAEIVH LAALRTMSAR HPVLALMERL MYQAYAVRPL GERVLFNKGG LFEQNFAYPQ
DMVYKFVGDS YPTTGRWRAG YLDTDVRARG LVDADYGPEL PHFPFYEDGS RLVEVIRRFV
RSFVDATYHE SDEMVAKDAE LQAWVAEANG PAGVEDFEPG PLDTRERLVE VLTHMAWLTG
CAHHVLNQGE PVTASGVLPM HPTALYAPVP TSKANTTADL LGYLPSAQKS VDQVTLLARF
NRPDVVPTNQ TLRYMFAAPQ LLLGNGEAYR RANQRFVRAM GRISDEVKAR RFDDRGLSQG
MPFIWQALDP GNIPFYLSV
