GenomeNet

Database: UniProt
Entry: B6HJ58_PENRW
LinkDB: B6HJ58_PENRW
Original site: B6HJ58_PENRW 
ID   B6HJ58_PENRW            Unreviewed;       750 AA.
AC   B6HJ58;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 66.
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   ORFNames=Pc21g23700 {ECO:0000313|EMBL:CAP97267.1}, PCH_Pc21g23700
GN   {ECO:0000313|EMBL:CAP97267.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP97267.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP97267.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM920436; CAP97267.1; -; Genomic_DNA.
DR   RefSeq; XP_002569337.1; XM_002569291.1.
DR   AlphaFoldDB; B6HJ58; -.
DR   GeneID; 8310242; -.
DR   KEGG; pcs:Pc21g23700; -.
DR   VEuPathDB; FungiDB:PCH_Pc21g23700; -.
DR   eggNOG; ENOG502QSD8; Eukaryota.
DR   HOGENOM; CLU_008878_3_1_1; -.
DR   OMA; GCPTNAK; -.
DR   OrthoDB; 601859at2759; -.
DR   BioCyc; PCHR:PC21G23700-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c21.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR003953; FAD-binding_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; PF00890; FAD_binding_2; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF028937; Lg_Ch_AO; 2.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR028937};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          221..258
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          269..494
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          565..727
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   ACT_SITE        674
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
SQ   SEQUENCE   750 AA;  81269 MW;  08414D0D68F3FA2F CRC64;
     MPAVSTYTPR DVPLPPAPSA TYFSELQWKT LYALADALVP SIHTAATAKS SNDRVISDAE
     WNSAVFSLST VISGPDAVNI ATQYLHENVS SNPQFRAIVE RLLGDYVHDE GRNGFGFILT
     ALNTRAGSLI ITGSTTPIQD QPVEFREKVV RGWDTSRLPP LRAIYRGLTA IVKKCWIITS
     PTIGPVLGFP RLPAHGKHAD GFQYEFLQFP PGDQPETIET DVVIVGSGCG GSVTAKNLAE
     AGHRVLVVEK SYSYPSNTFP MGPNEGFVNM FENGGAISSD DGSMAVLAGS TWGGGGTVNW
     SASLQTQGYV RQEWADAGLP FFTSLDFQKS LDRVCHRMGV NEEHVEHNHQ NRVILEGARK
     LGYAAKTVPQ NTGHGEHYCG YCTLGCASGG KKGPTESFLV DAAQAGASFM EGFCVEKVLF
     TNVNGRKVAS GVQGTWKSRD SHLGLGGIAA VERKVIIKAK KVVISAGTLQ SPLLLLRSGL
     NNPQIGRNLY LHPVMGAGAV FNEETHPWEG SALTTVVNEF EDLDGNGHGV KIESVSMMPS
     VFIPIFPWRD SLEYKLWAAK MRRSTSFITL TKDRDTGRVY PDPVDGRCRI DYTVSAFDRK
     HIVEAMIACA KIAYITGATE FHTVYRDLPP FIRPETSDPE APDGTNDAAL QNWIDELRRK
     SPLNPGRGLF ASAHQMGTCR MSKSPKLGVV DPNCQVWGTD GLYVVDASVF PSASGVNPMV
     TNMAIADWAS RNLARAMGTV RGEGSLIARL
//
DBGET integrated database retrieval system