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Database: UniProt
Entry: F7VSA1_SORMK
LinkDB: F7VSA1_SORMK
Original site: F7VSA1_SORMK 
ID   F7VSA1_SORMK            Unreviewed;       739 AA.
AC   F7VSA1;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=SMAC_01933 {ECO:0000313|EMBL:CCC08387.1};
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC08387.1, ECO:0000313|Proteomes:UP000001881};
RN   [1] {ECO:0000313|EMBL:CCC08387.1, ECO:0000313|Proteomes:UP000001881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC   {ECO:0000313|Proteomes:UP000001881};
RC   TISSUE=Mycelium {ECO:0000313|EMBL:CCC08387.1};
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA   Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCC08387.1}.
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DR   EMBL; CABT02000005; CCC08387.1; -; Genomic_DNA.
DR   RefSeq; XP_003348911.1; XM_003348863.1.
DR   AlphaFoldDB; F7VSA1; -.
DR   GeneID; 10806370; -.
DR   KEGG; smp:SMAC_01933; -.
DR   VEuPathDB; FungiDB:SMAC_01933; -.
DR   eggNOG; ENOG502QSD8; Eukaryota.
DR   HOGENOM; CLU_008878_3_1_1; -.
DR   InParanoid; F7VSA1; -.
DR   OMA; GCPTNAK; -.
DR   OrthoDB; 601859at2759; -.
DR   Proteomes; UP000001881; Unassembled WGS sequence.
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; 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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000001881};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          271..509
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          591..724
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        672
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
SQ   SEQUENCE   739 AA;  80170 MW;  D422F6AD1566047C CRC64;
     MASSVSGPTP PGLPPLPPGH GDYYTETQWT VLMSLLDATI PSITAVSNKK DDKTQLGLAD
     AEFKEIVTNA QASVVKKPAV EDITAYLAER ASDDPAFCCA MRRTLSTVPA SARNQLGAVL
     YALSTRPGSL LLTGYATPIQ DQPLHIRESI LRSWATSWFG TPRVLFKTFT VIAKVIWLQT
     SPLFRTVTGF PDVPVNWNPG RTEGFGFLQF DTSVNEPATV ETDVVIIGSG CGGGVCAKVL
     AEAGHRVLVV EKGYYFDPSQ LPMPRDQGGF HLFENNGFVN SVDSSINVVA GSCWGGGGSI
     NWSVSLQTQG YVRKEWSEQH GLPFFESGEY QTCLDRVCEF MGVVGGDDVR QSYRGQKLLD
     GSRKLGYAAQ VCPQNSGGKE HWCGHCHLGC ASAEKQGPAV SWLPAAAKRG ATFMEGFSAD
     RILWDESESS LSWFGFGGNN NKRRAVGVEG TWTARDTKGG VTGEQKTRKV IIKAKKVIVA
     AGTLNSPLIL QKSGLNSRHI GRNLYLHPVN FLGAYYEDDV KPWEGGIITS VCTAFENLDG
     QGHGVKLEGT CMLPYAILTQ LPWRGALAYK LACLRYRHLN AWISLARDRD TGRVYADPIT
     GKPSIEYTVS PFDAAHILEG LIALAKIAYV SEQPASEEDY DKGVKDPLFE SWLKTLRERG
     NAPPYPPYTS AHQMGTCRMS STPENGVVDP KGKVWGTEGL YVADASVFPS ASGVNPMITN
     MAIADWIARG VVGEFGKKI
//
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