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Manganese lipoxygenase (MnLOX) (EC 1.13.11.-) (EC 1.13.11.45)

 MNLOX_FUSOF             Reviewed;         610 AA.
F9FRH4;
11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
19-OCT-2011, sequence version 1.
28-MAR-2018, entry version 30.
RecName: Full=Manganese lipoxygenase {ECO:0000303|PubMed:26113537};
Short=MnLOX {ECO:0000303|PubMed:26113537};
EC=1.13.11.- {ECO:0000269|PubMed:26113537};
EC=1.13.11.45;
Flags: Precursor;
ORFNames=FOXB_09004;
Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
Fusarium; Fusarium oxysporum species complex.
NCBI_TaxID=660025;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Fo5176;
PubMed=21942452; DOI=10.1094/MPMI-08-11-0212;
Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
"A highly conserved effector in Fusarium oxysporum is required for
full virulence on Arabidopsis.";
Mol. Plant Microbe Interact. 25:180-190(2012).
[2]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
GLYCOSYLATION, AND MUTAGENESIS OF LEU-530.
PubMed=26113537; DOI=10.1194/jlr.M060178;
Wennman A., Magnuson A., Hamberg M., Oliw E.H.;
"Manganese lipoxygenase of F. oxysporum and the structural basis for
biosynthesis of distinct 11-hydroperoxy stereoisomers.";
J. Lipid Res. 56:1606-1615(2015).
-!- FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-
linolenic acids to 9-, 11- and 13-hydroperoxy fatty acids.
Oxidizes linoleic acid to mainly 11R-, 13S- and racemic 9-HPODE,
and alpha-linolenic acid to 11-HPOTrE.
{ECO:0000269|PubMed:26113537}.
-!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,12Z)-(11S)-11-
hydroperoxyoctadeca-9,12-dienoate. {ECO:0000250|UniProtKB:Q8X151}.
-!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,12Z)-(11R)-11-
hydroperoxyoctadeca-9,12-dienoate. {ECO:0000269|PubMed:26113537}.
-!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,11E)-(13S)-13-
hydroperoxyoctadeca-9,11-dienoate. {ECO:0000269|PubMed:26113537}.
-!- CATALYTIC ACTIVITY: Alpha-linolenate + O(2) = (9Z,12Z,15Z)-(11S)-
11-hydroperoxyoctadeca-9,12,15-trienoate.
{ECO:0000269|PubMed:26113537}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:26113537};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=29 uM for linoleate {ECO:0000269|PubMed:26113537};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8X151}.
-!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:26113537}.
-!- SIMILARITY: Belongs to the lipoxygenase family. Manganese
lipoxygenase subfamily. {ECO:0000305}.
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EMBL; AFQF01002523; EGU80482.1; -; Genomic_DNA.
SMR; F9FRH4; -.
OrthoDB; EOG092C18O5; -.
SABIO-RK; F9FRH4; -.
Proteomes; UP000002489; Unassembled WGS sequence.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0050584; F:linoleate 11-lipoxygenase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
InterPro; IPR000907; LipOase.
InterPro; IPR013819; LipOase_C.
InterPro; IPR036226; LipOase_C_sf.
PANTHER; PTHR11771; PTHR11771; 1.
Pfam; PF00305; Lipoxygenase; 1.
SUPFAM; SSF48484; SSF48484; 1.
PROSITE; PS51393; LIPOXYGENASE_3; 1.
1: Evidence at protein level;
Complete proteome; Dioxygenase; Glycoprotein; Iron; Manganese;
Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 610 Manganese lipoxygenase. {ECO:0000255}.
/FTId=PRO_5003383224.
DOMAIN 47 610 Lipoxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 290 290 Manganese; catalytic.
{ECO:0000250|UniProtKB:G4NAP4}.
METAL 295 295 Manganese; catalytic.
{ECO:0000250|UniProtKB:G4NAP4}.
METAL 475 475 Manganese; catalytic.
{ECO:0000250|UniProtKB:G4NAP4}.
METAL 479 479 Manganese; catalytic.
{ECO:0000250|UniProtKB:G4NAP4}.
METAL 610 610 Manganese; catalytic; via carboxylate.
{ECO:0000250|UniProtKB:G4NAP4}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 259 259 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 386 386 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 540 540 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 348 348 S->F: Changes the stereospecificity of
the enzyme from 11R-, 13S- and racemic 9-
HPODE to 11S-, 13R- and 9S-HPODE.
{ECO:0000269|PubMed:26113537}.
MUTAGEN 530 530 L->R: No effect.
{ECO:0000269|PubMed:26113537}.
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


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