MNLOX_NAKOS
ID MNLOX_NAKOS Reviewed; 617 AA.
AC P0CT92;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Manganese lipoxygenase;
DE Short=MnLOX;
DE EC=1.13.11.- {ECO:0000269|PubMed:23233731};
DE EC=1.13.11.45 {ECO:0000269|PubMed:23233731};
DE EC=1.13.11.58 {ECO:0000269|PubMed:23233731};
DE AltName: Full=Linoleate 9S-lipoxygenase {ECO:0000303|PubMed:23233731};
DE Short=Linoleate 9S-LOX {ECO:0000303|PubMed:23233731};
DE AltName: Full=Manganese 9S-lipoxygenase {ECO:0000303|PubMed:23233731};
DE Short=9S-MnLOX;
DE Flags: Precursor;
OS Nakataea oryzae (Rice stem rot fungus) (Magnaporthe salvinii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Nakataea.
OX NCBI_TaxID=165778;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 6642;
RA Sugio A., Takagi S.;
RT "Variants of lipoxygenase and their use.";
RL Patent number WO02086114, 31-OCT-2002.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LEU-350.
RC STRAIN=CBS 253.34, and CBS 288.52;
RX PubMed=23233731; DOI=10.1194/jlr.m033787;
RA Wennman A., Oliw E.H.;
RT "Secretion of two novel enzymes, manganese 9S-lipoxygenase and epoxy
RT alcohol synthase, by the rice pathogen Magnaporthe salvinii.";
RL J. Lipid Res. 54:762-775(2013).
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 products 11S-HPODE and 13R-HPODE from
CC linoleic acid are then transformed into 9S-HPODE as the final product.
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 9,16-DiHOTrE as the end
CC product. Also acts on gamma-linolenic acid producing 9-HOTrE(n-6) as
CC the main metabolite. {ECO:0000269|PubMed:23233731}.
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:23233731};
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:23233731};
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:23233731};
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:23233731};
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:23233731};
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:23233731};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23233731};
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:0000269|PubMed:23233731}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. Manganese lipoxygenase
CC subfamily. {ECO:0000305}.
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DR EMBL; AX590415; CAD61974.1; -; Genomic_DNA.
DR AlphaFoldDB; P0CT92; -.
DR SMR; P0CT92; -.
DR SwissLipids; SLP:000001655; -.
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 Dioxygenase; Glycoprotein; Manganese; Metal-binding; Oxidoreductase;
KW Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..617
FT /note="Manganese lipoxygenase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436134"
FT DOMAIN 122..617
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 23..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 293
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 297
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 483
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 617
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 350
FT /note="L->F: Changes the stereospecificity of the enzyme to
FT almost 100% 9S-HPOTrE as final product from the oxigenation
FT of alpha-linolenic acid."
FT /evidence="ECO:0000269|PubMed:23233731"
FT MUTAGEN 350
FT /note="L->M: Changes the stereospecificity of the enzyme
FT from 100% 9S-HPODE to 62% 13R- and 38% 9S-HPODE from the
FT oxigenation of linoleic acid."
FT /evidence="ECO:0000269|PubMed:23233731"
SQ 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
