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Database: UniProt
Entry: B9WMC7_CANDC
LinkDB: B9WMC7_CANDC
Original site: B9WMC7_CANDC 
ID   B9WMC7_CANDC            Unreviewed;       707 AA.
AC   B9WMC7;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Long-chain-alcohol oxidase {ECO:0000256|ARBA:ARBA00013125, ECO:0000256|PIRNR:PIRNR028937};
DE            EC=1.1.3.20 {ECO:0000256|ARBA:ARBA00013125, ECO:0000256|PIRNR:PIRNR028937};
GN   OrderedLocusNames=Cd36_32890 {ECO:0000313|CGD:CAL0000167182};
GN   ORFNames=CD36_32890 {ECO:0000313|EMBL:CAX40240.1};
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX40240.1, ECO:0000313|Proteomes:UP000002605};
RN   [1] {ECO:0000313|EMBL:CAX40240.1, ECO:0000313|Proteomes:UP000002605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC   {ECO:0000313|Proteomes:UP000002605};
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
CC   -!- FUNCTION: Long-chain fatty alcohol oxidase involved in the omega-
CC       oxidation pathway of lipid degradation.
CC       {ECO:0000256|ARBA:ARBA00003842}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain primary fatty alcohol + O2 = a long-chain fatty
CC         aldehyde + H2O2; Xref=Rhea:RHEA:22756, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17176, ChEBI:CHEBI:77396; EC=1.1.3.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00000920,
CC         ECO:0000256|PIRNR:PIRNR028937};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|PIRNR:PIRNR028937}.
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DR   EMBL; FM992695; CAX40240.1; -; Genomic_DNA.
DR   RefSeq; XP_002422236.1; XM_002422191.1.
DR   AlphaFoldDB; B9WMC7; -.
DR   SMR; B9WMC7; -.
DR   GeneID; 8049385; -.
DR   KEGG; cdu:CD36_32890; -.
DR   CGD; CAL0000167182; Cd36_32890.
DR   VEuPathDB; FungiDB:CD36_32890; -.
DR   eggNOG; ENOG502QSD8; Eukaryota.
DR   HOGENOM; CLU_008878_3_1_1; -.
DR   OrthoDB; 601859at2759; -.
DR   UniPathway; UPA00147; -.
DR   Proteomes; UP000002605; Chromosome R.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0047639; F:alcohol oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046577; F:long-chain-alcohol oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046188; P:methane catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   InterPro; IPR012400; Long_Oxdase.
DR   PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF028937; Lg_Ch_AO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR028937};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          245..458
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          543..692
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   ACT_SITE        637
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
SQ   SEQUENCE   707 AA;  77697 MW;  3DB2001EF7A7119E CRC64;
     MVTMDSIFPS KVEYKQVDTF IALCDGLIYD TTVDEIKDVI APDFPQEKLE EYVKTFTRPS
     QTPGFREAVY ETVNSNTTNA SRSFGILCNI LGSRILAPTL TNSLTPIKDM TLKEREALLA
     SWRDSPLATK RRLFRAVCAL AGTTIVRLAS ELHFKAIHFP QKDLRETAYE GQIIDPFRYE
     FMEKPTFEGA EIYLPDIDAI IIGSGAGSGV VAHTLANDGY KTLILEKGKY FSSSELQFDD
     YSGVKQLYQG GGAVVTLNQQ MLILAGSTFG GGTTVNWSAC IKTPFKVRKE WYDDFGVEFA
     ATDTYDKDQD YVFKQMGAST DGITHSLANE VIMEGGKKLG YASKEINQNS GGHPHHPCGF
     CHLGCKYGIK QGSVANWFRD AAANGSKFME QVRVVKILNK NGIAYGVLCQ DVATGVNFTI
     TGPKKYVVSA GSLNTPTVLT NSGFKNKHIG RNLTLHPVTT VFGDFGKDVQ ADHFHNSIMT
     AVCTQVDDLD GKAHGAKIET ILNAPFLQAA FLPWRGSNEF RRDLLRYNNM VAMLLITRDS
     TSGTVKGDPN RPDALYVDYT VNKFDRNALL QALLITADML YIEGAKRILS PQSWVPIFES
     NVPKDQRSID DKDYVEWRKK VAGIPFDQYG AAYGSAHQMS SCRMSGKGPA FGAVDTNGKL
     FECSNVYVAD ASVLPTASGA NPMISTMTVA RHIGLGLAKD LKTKAKL
//
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