ID A0A1Y2XGE2_9PEZI Unreviewed; 756 AA.
AC A0A1Y2XGE2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=K445DRAFT_312709 {ECO:0000313|EMBL:OTB20276.1};
OS Daldinia sp. EC12.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB20276.1, ECO:0000313|Proteomes:UP000243732};
RN [1] {ECO:0000313|EMBL:OTB20276.1, ECO:0000313|Proteomes:UP000243732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC12 {ECO:0000313|EMBL:OTB20276.1,
RC ECO:0000313|Proteomes:UP000243732};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ112927; OTB20276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2XGE2; -.
DR STRING; 1001832.A0A1Y2XGE2; -.
DR OrthoDB; 601859at2759; -.
DR Proteomes; UP000243732; 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; 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:UP000243732};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 222..254
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 269..497
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 579..735
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT ACT_SITE 683
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
SQ SEQUENCE 756 AA; 83257 MW; 3BA680363FFA49AE CRC64;
MATPGQLIAP IPTQLPELKP DTYFSQAQWQ ILLALVDATV PSIVSDSTTT DKKDHLQIPM
SQLEDSYMRI KSSMRHPPDY KKFQQYLQSR PLDNPRFLQA VKRILEGVPD SNRKQLGAIL
NILATRLGSL AATGYYTPLH EQPIHIRESI LQAWNHSWMT VWPLIGNSIT RIAKVCFAQT
DPLLRELSGY TEVSDDYKPG PSFDFDFMQF EAGSETETID TDVVIVGSGC GGAVCAKVLS
EAGHKVIVVD KGYHFPPSQL PMTAEAGVKF LYEGNGTLQS VDGSVTILAG SCWGGGGTVN
WSVSLHPQGF LRQEWADQGL DFFTTQEFQH CIDRVCDFMG VSDAHIRHNH GANVILNGAK
KLGWAAKPCP QNTGGAEHYC GHCATGCGSS EKEGPSVSWL PAAARAGAKF IEGFNVSKVL
FDETRGMKTA VGILGTWTSR DKDGNAHTPE SERVQRQIQI RAKKVIVACG TLNSPLLLMR
SGLRNPHIGK HLYIHPVGQM NAFFNEDIKG WEGGILTSVC TSFENLDGKG HGVKLEPTSM
IPHMFLHGHP WRSALQWKLD ALRSRQMNSY IAIARDRDTG RVYPDPHDGR PTVEYSPSAL
DRKHILAGII ALAKMCYIEG ATEIWPFVKS IPSFVRRSKP TISTLDEGDD IDQGINDPDF
VAWLKNLERT GLNHPDATFS SAHQMGSCRM SAHPARGVVD PQGRVWEARN LYVADASVFP
TASGVNPMIT TMAIADWIAR RVSKDLIRGE QIRAAL
//
