(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 90.
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.
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}.
DR   EMBL; AAHF01000016; EAL84425.1; -; Genomic_DNA.
DR   RefSeq; XP_746463.1; XM_741370.1.
DR   SMR; Q4WA38; -.
DR   EnsemblFungi; EAL84425; EAL84425; AFUA_4G02770.
DR   GeneID; 3503886; -.
DR   KEGG; afm:AFUA_4G02770; -.
DR   EuPathDB; FungiDB:Afu4g02770; -.
DR   HOGENOM; HOG000217303; -.
DR   InParanoid; Q4WA38; -.
DR   OMA; NPYAVRR; -.
DR   OrthoDB; 385042at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
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;
DR   PRODOM; Q4WA38.
DR   SWISS-2DPAGE; Q4WA38.
KW   Dioxygenase; Glycoprotein; Iron; 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   METAL           288
FT                   /note="Manganese; catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT   METAL           293
FT                   /note="Manganese; catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT   METAL           473
FT                   /note="Manganese; catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT   METAL           477
FT                   /note="Manganese; catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT   METAL           608
FT                   /note="Manganese; catalytic; via carboxylate"
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
//

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