MNLOX_ASPFU
ID MNLOX_ASPFU Reviewed; 608 AA.
AC Q4WA38;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Manganese lipoxygenase {ECO:0000305|PubMed:24276623};
DE Short=MnLOX {ECO:0000305|PubMed:24276623};
DE EC=1.13.11.- {ECO:0000269|PubMed:24276623};
DE AltName: Full=Manganese 13-lipoxygenase;
DE Short=13-MnLOX;
DE Flags: Precursor;
GN ORFNames=AFUA_4G02770;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=24276623; DOI=10.1007/s00253-013-5392-x;
RA Heshof R., Jylhae S., Haarmann T., Joergensen A.L., Dalsgaard T.K.,
RA de Graaff L.H.;
RT "A novel class of fungal lipoxygenases.";
RL Appl. Microbiol. Biotechnol. 98:1261-1270(2014).
CC -!- FUNCTION: Lipoxygenase that metabolizes linoleic acid to 9- and 13-
CC hydroperoxy fatty acids. Specific towards 13-HPODE yielding 89% of the
CC total HPODE. {ECO:0000269|PubMed:24276623}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = 13-hydroperoxy-(9Z,11E)-
CC octadecadienoate; Xref=Rhea:RHEA:48848, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:90823;
CC Evidence={ECO:0000269|PubMed:24276623};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:24276623};
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 -!- SIMILARITY: Belongs to the lipoxygenase family. Manganese lipoxygenase
CC subfamily. {ECO:0000305}.
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DR EMBL; AAHF01000016; EAL84425.1; -; Genomic_DNA.
DR RefSeq; XP_746463.1; XM_741370.1.
DR AlphaFoldDB; Q4WA38; -.
DR SMR; Q4WA38; -.
DR STRING; 330879.Q4WA38; -.
DR EnsemblFungi; EAL84425; EAL84425; AFUA_4G02770.
DR GeneID; 3503886; -.
DR KEGG; afm:AFUA_4G02770; -.
DR VEuPathDB; FungiDB:Afu4g02770; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_4_0_1; -.
DR InParanoid; Q4WA38; -.
DR OMA; LALPYPY; -.
DR OrthoDB; 385042at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050584; F:linoleate 11-lipoxygenase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0043651; P:linoleic acid metabolic process; IEA:UniProt.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..608
FT /note="Manganese lipoxygenase"
FT /evidence="ECO:0000255"
FT /id="PRO_5004245467"
FT DOMAIN 29..608
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
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 473
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 477
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 608
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 608 AA; 68749 MW; B245FE7EDDDD55C7 CRC64;
MMVFSDCLIF SSLIISYALG LPVVPGQTVM EPSAALPDDG DHLYTLPMFD IRPWERVSEV
RLAREGYLYG PPLLGNTSFF PTGVLGDAMV ARDKAAWFRD VEYVTNNVYP EWDKAAIALA
KAGGIQSLSS YAVIYENQWA TTLPDGVASG MLTNWTQDLL FSMERLSINP YVVRRLHPRK
DRLPFAVDDR VVQHLAAGST LEALHCDGRL FFANHSYQAP YPKTPGRWTA ACTAYFFIHP
RSGAFLPLAI KTNMGSDLTY TPMDETNDWL FAKMAFEMND LFHSQLYHLA NTHDVAEPVH
QAALRTMSAR HPVRGYLDRL MYQAYAVRPI GEEFLFNEGG FYDSSFALPN WAGKKYATDA
YWEHAGHFKA TNFYQDLFDR GLVDCTYGPP LTSFPFYETV APMVEAIEEF TRAFVEAYYP
DKTLMDVDNE LQDWIIEATE AAKVIDFVPA PMREPEQLIS VLSHMAFLAG IAHHALNGAT
VSEASGVLPL HPSSFNRPLP EAKGSIDSLL PWLHNETEAL KQASLLVRFN RPLLDEQEGS
LPYMFSGSSF LARTGAPIHD AERRFREKMW AISDEIRMRQ FDERGLSQGM PFLWRSIDPR
KIPYYLCV
