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Manganese lipoxygenase (MnLOX) (EC 1.13.11.-) (EC 1.13.11.45) (EC 1.13.11.58)

 MNLOX_MAGO7             Reviewed;         619 AA.
G4NAP4; A0A0M4MCV3; Q52YI5; Q52ZN7;
11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
11-MAY-2016, sequence version 2.
20-DEC-2017, entry version 35.
RecName: Full=Manganese lipoxygenase {ECO:0000303|PubMed:26264916};
Short=MnLOX {ECO:0000303|PubMed:26264916};
EC=1.13.11.- {ECO:0000269|PubMed:26264916};
EC=1.13.11.45 {ECO:0000269|PubMed:26264916};
EC=1.13.11.58 {ECO:0000269|PubMed:26264916};
Flags: Precursor;
ORFNames=MGG_08499;
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice
blast fungus) (Pyricularia oryzae).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Magnaporthales; Magnaporthaceae;
Magnaporthe.
NCBI_TaxID=242507;
[1]
NUCLEOTIDE SEQUENCE [MRNA], REVISION OF GENE MODEL, FUNCTION, AND
CATALYTIC ACTIVITY.
STRAIN=Guyane 11;
PubMed=26264916; DOI=10.1016/j.abb.2015.07.014;
Wennman A., Jerneren F., Magnuson A., Oliw E.H.;
"Expression and characterization of manganese lipoxygenase of the rice
blast fungus reveals prominent sequential lipoxygenation of alpha-
linolenic acid.";
Arch. Biochem. Biophys. 583:87-95(2015).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
PubMed=15846337; DOI=10.1038/nature03449;
Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W.,
Harding M., Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J.,
Calvo S.E., Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E.,
Birren B.W.;
"The genome sequence of the rice blast fungus Magnaporthe grisea.";
Nature 434:980-986(2005).
[3] {ECO:0000244|PDB:5FNO}
X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 17-619 IN COMPLEX WITH
MANGANESE, GLYCOSYLATION AT ASN-86; ASN-164 AND ASN-549, CATALYTIC
ACTIVITY, AND MUTAGENESIS OF ARG-539 AND PHE-540.
PubMed=26783260; DOI=10.1074/jbc.M115.707380;
Wennman A., Oliw E.H., Karkehabadi S., Chen Y.;
"Crystal structure of manganese lipoxygenase of the rice blast fungus
Magnaporthe oryzae.";
J. Biol. Chem. 291:8130-8139(2016).
-!- FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-
linolenic acids to 9S-, 11- and 13R-hydroperoxy fatty acids. At
the end of lipoxygenation, the intermediate product 11S-HPODE from
linoleic acid is then transformed into 9S-HPODE and 13R-HPODE as
the final products. 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 9S,16S-DiHPOTrE as the end product.
{ECO:0000269|PubMed:26264916}.
-!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9S,10E,12Z)-9-hydroperoxy-
10,12-octadecadienoate. {ECO:0000269|PubMed:26264916}.
-!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,12Z)-(11S)-11-
hydroperoxyoctadeca-9,12-dienoate. {ECO:0000269|PubMed:26264916}.
-!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,11E)-(13R)-13-
hydroperoxyoctadeca-9,11-dienoate. {ECO:0000269|PubMed:26264916}.
-!- CATALYTIC ACTIVITY: Alpha-linolenate + O(2) = (10E,12Z,15Z)-(9S)-
9-hydroperoxyoctadeca-10,12,15-trienoate.
{ECO:0000269|PubMed:26264916}.
-!- CATALYTIC ACTIVITY: Alpha-linolenate + O(2) = (9Z,12Z,15Z)-(11R)-
11-hydroperoxyoctadeca-9,12,15-trienoate.
{ECO:0000269|PubMed:26264916, ECO:0000269|PubMed:26783260}.
-!- CATALYTIC ACTIVITY: Alpha-linolenate + O(2) = (9Z,11E,15Z)-(13R)-
13-hydroperoxyoctadeca-9,11,15-trienoate.
{ECO:0000269|PubMed:26264916}.
-!- CATALYTIC ACTIVITY: (10E,12Z,15Z)-(9S)-9-hydroperoxyoctadeca-
10,12,15-trienoate + O(2) = (10E,12Z,14E)-(9S,16S)-9,16-
dihydroperoxyoctadeca-10,12,14-trienoate.
{ECO:0000269|PubMed:26264916, ECO:0000269|PubMed:26783260}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:26783260};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8X151}.
-!- SIMILARITY: Belongs to the lipoxygenase family. Manganese
lipoxygenase subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EHA49687.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; KT734829; ALE27899.1; -; mRNA.
EMBL; AY829440; AAX48918.1; -; mRNA.
EMBL; AY858988; AAX52528.1; -; Genomic_DNA.
EMBL; CM001234; EHA49687.1; ALT_SEQ; Genomic_DNA.
RefSeq; XP_003716006.1; XM_003715958.1.
PDB; 5FNO; X-ray; 2.04 A; A/B=17-588.
PDBsum; 5FNO; -.
SMR; G4NAP4; -.
STRING; 318829.MGG_08499T0; -.
SwissLipids; SLP:000001658; -.
iPTMnet; G4NAP4; -.
EnsemblFungi; MGG_08499T0; MGG_08499T0; MGG_08499.
GeneID; 2678734; -.
KEGG; mgr:MGG_08499; -.
EuPathDB; FungiDB:MGG_08499; -.
InParanoid; G4NAP4; -.
OrthoDB; EOG092C18O5; -.
Proteomes; UP000009058; Chromosome 4.
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;
3D-structure; Complete proteome; Dioxygenase; Glycoprotein; Iron;
Manganese; Metal-binding; Oxidoreductase; Reference proteome;
Secreted; Signal.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 619 Manganese lipoxygenase.
/FTId=PRO_5003466387.
DOMAIN 55 619 Lipoxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 298 298 Manganese; catalytic.
{ECO:0000269|PubMed:26783260}.
METAL 303 303 Manganese; catalytic.
{ECO:0000269|PubMed:26783260}.
METAL 483 483 Manganese; catalytic.
{ECO:0000269|PubMed:26783260}.
METAL 487 487 Manganese; catalytic.
{ECO:0000269|PubMed:26783260}.
METAL 619 619 Manganese; catalytic; via carboxylate.
{ECO:0000269|PubMed:26783260}.
CARBOHYD 32 32 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:26783260}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:26783260}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 515 515 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 549 549 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:26783260}.
MUTAGEN 539 539 R->A: Reduces catalytic activity towards
alpha-linoleate, but retains oxidation
activity on 9S-HPOTrE.
{ECO:0000269|PubMed:26783260}.
MUTAGEN 540 540 F->L: Loss of oxidation activity on
alpha-linoleate, but retains oxidation
activity on 9S-HPOTrE.
{ECO:0000269|PubMed:26783260}.
HELIX 57 59 {ECO:0000244|PDB:5FNO}.
HELIX 63 76 {ECO:0000244|PDB:5FNO}.
STRAND 77 80 {ECO:0000244|PDB:5FNO}.
STRAND 83 88 {ECO:0000244|PDB:5FNO}.
STRAND 90 92 {ECO:0000244|PDB:5FNO}.
HELIX 93 131 {ECO:0000244|PDB:5FNO}.
HELIX 139 144 {ECO:0000244|PDB:5FNO}.
TURN 145 147 {ECO:0000244|PDB:5FNO}.
TURN 150 152 {ECO:0000244|PDB:5FNO}.
TURN 159 166 {ECO:0000244|PDB:5FNO}.
HELIX 168 173 {ECO:0000244|PDB:5FNO}.
HELIX 174 176 {ECO:0000244|PDB:5FNO}.
TURN 188 190 {ECO:0000244|PDB:5FNO}.
HELIX 199 206 {ECO:0000244|PDB:5FNO}.
HELIX 210 215 {ECO:0000244|PDB:5FNO}.
STRAND 219 223 {ECO:0000244|PDB:5FNO}.
HELIX 225 227 {ECO:0000244|PDB:5FNO}.
STRAND 242 247 {ECO:0000244|PDB:5FNO}.
TURN 249 251 {ECO:0000244|PDB:5FNO}.
STRAND 254 260 {ECO:0000244|PDB:5FNO}.
HELIX 275 277 {ECO:0000244|PDB:5FNO}.
HELIX 278 300 {ECO:0000244|PDB:5FNO}.
HELIX 303 316 {ECO:0000244|PDB:5FNO}.
HELIX 322 330 {ECO:0000244|PDB:5FNO}.
TURN 331 333 {ECO:0000244|PDB:5FNO}.
HELIX 334 336 {ECO:0000244|PDB:5FNO}.
HELIX 337 343 {ECO:0000244|PDB:5FNO}.
STRAND 346 349 {ECO:0000244|PDB:5FNO}.
HELIX 351 355 {ECO:0000244|PDB:5FNO}.
STRAND 356 358 {ECO:0000244|PDB:5FNO}.
HELIX 360 374 {ECO:0000244|PDB:5FNO}.
HELIX 378 380 {ECO:0000244|PDB:5FNO}.
HELIX 382 388 {ECO:0000244|PDB:5FNO}.
STRAND 391 393 {ECO:0000244|PDB:5FNO}.
HELIX 404 427 {ECO:0000244|PDB:5FNO}.
TURN 428 430 {ECO:0000244|PDB:5FNO}.
HELIX 432 436 {ECO:0000244|PDB:5FNO}.
HELIX 439 449 {ECO:0000244|PDB:5FNO}.
TURN 450 452 {ECO:0000244|PDB:5FNO}.
HELIX 465 480 {ECO:0000244|PDB:5FNO}.
HELIX 482 486 {ECO:0000244|PDB:5FNO}.
HELIX 490 493 {ECO:0000244|PDB:5FNO}.
TURN 494 496 {ECO:0000244|PDB:5FNO}.
TURN 498 500 {ECO:0000244|PDB:5FNO}.
STRAND 503 507 {ECO:0000244|PDB:5FNO}.
STRAND 513 516 {ECO:0000244|PDB:5FNO}.
HELIX 520 522 {ECO:0000244|PDB:5FNO}.
HELIX 527 538 {ECO:0000244|PDB:5FNO}.
HELIX 543 545 {ECO:0000244|PDB:5FNO}.
TURN 546 549 {ECO:0000244|PDB:5FNO}.
HELIX 552 554 {ECO:0000244|PDB:5FNO}.
HELIX 559 564 {ECO:0000244|PDB:5FNO}.
HELIX 567 588 {ECO:0000244|PDB:5FNO}.
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


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