MNLOX_FUSOF
ID MNLOX_FUSOF Reviewed; 610 AA.
AC F9FRH4;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Manganese lipoxygenase {ECO:0000303|PubMed:26113537};
DE Short=MnLOX {ECO:0000303|PubMed:26113537};
DE EC=1.13.11.- {ECO:0000269|PubMed:26113537};
DE EC=1.13.11.45;
DE AltName: Full=Manganese 11R/13S-lipoxygenase;
DE Short=11R/13S-MnLOX;
DE Flags: Precursor;
GN ORFNames=FOXB_09004;
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176;
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP GLYCOSYLATION, AND MUTAGENESIS OF SER-348 AND LEU-530.
RX PubMed=26113537; DOI=10.1194/jlr.m060178;
RA Wennman A., Magnuson A., Hamberg M., Oliw E.H.;
RT "Manganese lipoxygenase of F. oxysporum and the structural basis for
RT biosynthesis of distinct 11-hydroperoxy stereoisomers.";
RL J. Lipid Res. 56:1606-1615(2015).
CC -!- FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-linolenic
CC acids to 9-, 11- and 13-hydroperoxy fatty acids. Oxidizes linoleic acid
CC to mainly 11R-, 13S- and racemic 9-HPODE, and alpha-linolenic acid to
CC 11-HPOTrE. {ECO:0000269|PubMed:26113537}.
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:0000250|UniProtKB:Q8X151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (11R)-hydroperoxy-(9Z,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:51640, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:134248;
CC Evidence={ECO:0000269|PubMed:26113537};
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:26113537};
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:0000269|PubMed:26113537};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:26113537};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29 uM for linoleate {ECO:0000269|PubMed:26113537};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8X151}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:26113537}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. Manganese lipoxygenase
CC subfamily. {ECO:0000305}.
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DR EMBL; AFQF01002523; EGU80482.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FRH4; -.
DR SMR; F9FRH4; -.
DR STRING; 660025.F9FRH4; -.
DR SABIO-RK; F9FRH4; -.
DR Proteomes; UP000002489; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050584; F:linoleate 11-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:0043651; P:linoleic acid metabolic process; IEA:UniProt.
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; Glycoprotein; Manganese; Metal-binding; Oxidoreductase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..610
FT /note="Manganese lipoxygenase"
FT /evidence="ECO:0000255"
FT /id="PRO_5003383224"
FT DOMAIN 47..610
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
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 295
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 475
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 479
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 610
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 348
FT /note="S->F: Changes the stereospecificity of the enzyme
FT from 11R-, 13S- and racemic 9-HPODE to 11S-, 13R- and 9S-
FT HPODE."
FT /evidence="ECO:0000269|PubMed:26113537"
FT MUTAGEN 530
FT /note="L->R: No effect."
FT /evidence="ECO:0000269|PubMed:26113537"
SQ SEQUENCE 610 AA; 67941 MW; C872D677D76E552A CRC64;
MVALLIFLGI FTCVETLPLS DSPSSYIPEE VPSSQTADIG LPPPTEFTLP NEDDEILIRK
LNIQKTRKEI LYGPSLIGKT SFFISGPLGD QISQRDQTLW SRDAAPVVQA VSHDAAAALH
DIQIHGGLQN LDDYKILYQG HWSSSVPGGI AKGQFSNFTS DLLFSMERLS TNPYILRRLH
PHADELPFAV DSKIVQKLTG STLPSLHKAG RLFLADHSYQ KDYVAQEGRY AAACQALFYL
DDRCHQFLPL AIKTNVGSNL TYTPLDEPND WLLAKVMFNV NDLFHGQMYH LASTHAVAEI
VHLAALRTMS SRHPVLALLQ RLMYQAYAIR PIGNNILFNP GGLIDQNSVF SNVAVRKFAT
DFYPTVAGPV RSNYFEANLR SRGLLNATHG PDLPHFPFYE DGARIIKVIR TFIQSFVKSI
YKSDKVLAKD WELQAWIAEA NGAAEVIDFP PTPLKKRKHL VDILTHMAWL TGVSHHVLNQ
GEPVTTSGVL PLHPGSLYAP VPGEKGVVDS LLPWLPNEQK SVDQISFLAL FNRPQIVENN
RTLRYMFNSE SLLAGTVRAV AAANERFMEE MGHISQEISN RKFDDDGLSQ GMPFIWTGMD
PGVIPFYLSV
