MNLOX_COLGC
ID MNLOX_COLGC Reviewed; 609 AA.
AC T0JRM4;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 34.
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 {ECO:0000269|PubMed:26113537};
DE EC=1.13.11.58 {ECO:0000269|PubMed:26113537};
DE AltName: Full=Manganese 9S/11S-lipoxygenase;
DE Short=9S/11S-MnLOX;
DE Flags: Precursor;
GN ORFNames=CGLO_15145;
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14;
RX PubMed=23902260; DOI=10.1094/mpmi-03-13-0080-r;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION, AND MUTAGENESIS OF.
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 9S- and 13R-HPODE and alpha-linolenic acid to 11R-HPOTrE.
CC {ECO:0000269|PubMed:26113537}.
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: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 = (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:26113537};
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:26113537};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8X151};
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: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; AMYD01003602; EQB45907.1; -; Genomic_DNA.
DR AlphaFoldDB; T0JRM4; -.
DR SMR; T0JRM4; -.
DR STRING; 1237896.T0JRM4; -.
DR EnsemblFungi; EQB45907; EQB45907; CGLO_15145.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_4_0_1; -.
DR OMA; LALPYPY; -.
DR OrthoDB; 385042at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
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 Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..609
FT /note="Manganese lipoxygenase"
FT /evidence="ECO:0000255"
FT /id="PRO_5004565294"
FT DOMAIN 117..609
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 289
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 294
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 474
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 478
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 609
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 609 AA; 67312 MW; C1B855BE6E8F9934 CRC64;
MRLLLSIAGL TTVVNALAVR ADGNVTSSTA VATPTAWTGF PVPTEYTLPQ DDHDFQERKE
EIKLKRDTIT YVPSIIGETS LFIGGSVGTQ IVRQEQAKWI QDLTPVQQDA FREGNASLKA
IQDHGGLKTL EDYKILYDGH WSGSVPGGIA QGQFNNFTSD LLFAMERLST NPYVVRRLNP
ESDKIPFSVD ANNVTHLTGT TLDTLFKSGS LFLADHSYQA EYTAQDGRYS AACQALFFLD
QRSGQFLPLA IKTNVGSDLV YTPLDDPNDW LLAKIMYNVN DFFHGQIYHL ANSHAVAEIV
NLAAIRTLSS RHPVFGLLQR LMFQAYAIRA TGEIALFNPG GLFDQSFAFS NVYARKFATD
FYPTVAGPFQ ANYFEEDLRA RGLLNASYGP ELPHLPFHED GHKIINAIRT FIGTFVDTVY
ESDKVLAEDS ELQAWIAEAN GPAKVINFPS APLNTRKQLA EILTHMAWLT GVSHHVLNQG
EPFTTSGVLP LHPASLYAPV PTAKGGIKDL LPWLPNEQKS VEQISLLARF NRPKIVENNE
TLLHMFDVKT LLSGTGEAVK AANEQFMIAM GTISKEISTR KFDDQGLSQG MPFIWTGMDP
GVIPFYLSV
