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Manganese lipoxygenase (MnLOX) (EC 1.13.11.-) (EC 1.13.11.45) (EC 1.13.11.58) (Linoleate 9S-lipoxygenase) (Linoleate 9S-LOX) (Manganese 9S-lipoxygenase) (9S-MnLOX)

 MNLOX_NAKOS             Reviewed;         617 AA.
P0CT92;
11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
11-MAY-2016, sequence version 1.
18-JUL-2018, entry version 10.
RecName: Full=Manganese lipoxygenase;
Short=MnLOX;
EC=1.13.11.- {ECO:0000269|PubMed:23233731};
EC=1.13.11.45 {ECO:0000269|PubMed:23233731};
EC=1.13.11.58 {ECO:0000269|PubMed:23233731};
AltName: Full=Linoleate 9S-lipoxygenase {ECO:0000303|PubMed:23233731};
Short=Linoleate 9S-LOX {ECO:0000303|PubMed:23233731};
AltName: Full=Manganese 9S-lipoxygenase {ECO:0000303|PubMed:23233731};
Short=9S-MnLOX;
Flags: Precursor;
Nakataea oryzae (Rice stem rot fungus) (Magnaporthe salvinii).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Magnaporthales; Magnaporthaceae;
Nakataea.
NCBI_TaxID=165778;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NBRC 6642;
Sugio A., Takagi S.;
"Variants of lipoxygenase and their use.";
Patent number WO02086114, 31-OCT-2002.
[2]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF LEU-350.
STRAIN=CBS 253.34, and CBS 288.52;
PubMed=23233731; DOI=10.1194/jlr.M033787;
Wennman A., Oliw E.H.;
"Secretion of two novel enzymes, manganese 9S-lipoxygenase and epoxy
alcohol synthase, by the rice pathogen Magnaporthe salvinii.";
J. Lipid Res. 54:762-775(2013).
-!- FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-
linolenic acids to 9S-, 11- and 13R-hydroperoxy fatty acids. At
the end of lipoxygenation, the intermediate products 11S-HPODE and
13R-HPODE from linoleic acid are then transformed into 9S-HPODE as
the final product. The intermediate product 11R-HPOTrE from alpha-
linolenic acid is transformed into 9S-HPOTrE and 13R-HPOTrE as the
final products. 9S-HPOTrE is further oxidized by the enzyme to
9,16-DiHOTrE as the end product. Also acts on gamma-linolenic acid
producing 9-HOTrE(n-6) as the main metabolite.
{ECO:0000269|PubMed:23233731}.
-!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9S,10E,12Z)-9-hydroperoxy-
10,12-octadecadienoate. {ECO:0000269|PubMed:23233731}.
-!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,12Z)-(11S)-11-
hydroperoxyoctadeca-9,12-dienoate. {ECO:0000269|PubMed:23233731}.
-!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,11E)-(13R)-13-
hydroperoxyoctadeca-9,11-dienoate. {ECO:0000269|PubMed:23233731}.
-!- CATALYTIC ACTIVITY: Alpha-linolenate + O(2) = (10E,12Z,15Z)-(9S)-
9-hydroperoxyoctadeca-10,12,15-trienoate.
{ECO:0000269|PubMed:23233731}.
-!- CATALYTIC ACTIVITY: Alpha-linolenate + O(2) = (9Z,12Z,15Z)-(11R)-
11-hydroperoxyoctadeca-9,12,15-trienoate.
{ECO:0000269|PubMed:23233731}.
-!- CATALYTIC ACTIVITY: Alpha-linolenate + O(2) = (9Z,11E,15Z)-(13R)-
13-hydroperoxyoctadeca-9,11,15-trienoate.
{ECO:0000269|PubMed:23233731}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:23233731};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23233731}.
-!- SIMILARITY: Belongs to the lipoxygenase family. Manganese
lipoxygenase subfamily. {ECO:0000305}.
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EMBL; AX590415; CAD61974.1; -; Genomic_DNA.
SMR; P0CT92; -.
SwissLipids; SLP:000001655; -.
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;
Dioxygenase; Glycoprotein; Manganese; Metal-binding; Oxidoreductase;
Secreted; Signal.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 617 Manganese lipoxygenase. {ECO:0000255}.
/FTId=PRO_0000436134.
DOMAIN 122 617 Lipoxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 293 293 Manganese; catalytic.
{ECO:0000250|UniProtKB:G4NAP4}.
METAL 297 297 Manganese; catalytic.
{ECO:0000250|UniProtKB:G4NAP4}.
METAL 479 479 Manganese; catalytic.
{ECO:0000250|UniProtKB:G4NAP4}.
METAL 483 483 Manganese; catalytic.
{ECO:0000250|UniProtKB:G4NAP4}.
METAL 617 617 Manganese; catalytic; via carboxylate.
{ECO:0000250|UniProtKB:G4NAP4}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 547 547 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 350 350 L->F: Changes the stereospecificity of
the enzyme to almost 100% 9S-HPOTrE as
final product from the oxigenation of
alpha-linolenic acid.
{ECO:0000269|PubMed:23233731}.
MUTAGEN 350 350 L->M: Changes the stereospecificity of
the enzyme from 100% 9S-HPODE to 62%
13R- and 38% 9S-HPODE from the
oxigenation of linoleic acid.
{ECO:0000269|PubMed:23233731}.
SEQUENCE 617 AA; 67532 MW; C9896F37DD0A9D99 CRC64;
MRIGLLAFAV AARYVEALPV ASGEEVASSS APTTLPSTSS SSALPSPTKY TLPHEDPNPE
ARKAEIALKR GGFLYGPSTL GQTTFYPSGT LGTAMSQRDQ ALWLRDAENQ TITAYREANE
TLRDIQSHGG LKTLDDFALL YDGHWKASVP EGIEKGMLSN YTSDLLFSME RLSNNPYSLK
RLHPTKDKLP FSVEDKVVKQ LTATTLAALH KAGRLFFVDH SDQKKYTPQA GRYAAACQGL
FYVDARSNQF LPLAIKTNVG ADLTYTPLDD KNDWLLAKIM FNNNDLFYSQ MYHVLFHTVP
EIVHMAAIRT LSESHPVLAV LNRIMYQAYA IRPVGERILF NPGGFWDQNL GLPATAAVDF
LSSIYAHGEG GFRAGYVENN LRKRGLVGDT FGGPALPHFP FYEDAQRVLG AIRGFMQAFV
DSTYGGDDGA LARDFELQDW VAEANGPAQV RDFPTAPLRR REELVGILTH IAWNTGGAHH
VLNQGAPVRA SGVLPLHPAA LYAPVPAAKG AVASSDGLLA WLPDEVKSVE QVSLLARFNR
AQVRDRNQTV RNMFAAPELL AGNGEAYAAA NARFVEETGR ISREIEGRGF DSKGLSQGMP
FIWTALNPAV NPFFLSI


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