ID G0S2U9_CHATD Unreviewed; 786 AA.
AC G0S2U9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=CTHT_0018560 {ECO:0000313|EMBL:EGS22332.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS22332.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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; GL988040; EGS22332.1; -; Genomic_DNA.
DR RefSeq; XP_006692351.1; XM_006692288.1.
DR AlphaFoldDB; G0S2U9; -.
DR GeneID; 18255894; -.
DR KEGG; cthr:CTHT_0018560; -.
DR eggNOG; ENOG502QSD8; Eukaryota.
DR HOGENOM; CLU_008878_3_1_1; -.
DR OMA; YGVIYET; -.
DR OrthoDB; 601859at2759; -.
DR Proteomes; UP000008066; 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; 3.
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:UP000008066};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 287..505
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 591..727
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 762..786
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 786 AA; 85905 MW; 29282BA1B2F2CA17 CRC64;
MRPLTPDASP AAAPLAVDLP PYTEFLNETQ WKVLMALMDA VIPAIRVQDT AQQQQGSRMQ
DDLSALHLSS AEYSDAASQL RNAVTPLDPT AELIEAYLAE RPSDNPLFAQ LMKCILSNIP
PSKQRELKIL LSVLSTRAGS LILTHRASPL PLLSIQDRTK ILRSWATSPL WSIRALFKSM
TTLGKLAWLR STPYFAPLTG FPRVPAAWVA GSKSYPYEFL QFSPGPDVKA PVEIATDVVI
VGSGCGAGVV AHKLATEFGK GLNVLVIEKG WHFDASHFPM SQTTGLANLF EAGGVIESDD
GSITVTAGAC FGGGGTVNWS ASLQPQDFVR KEWAQERKLE FFETEDFQKC LDRVWKHMGV
TGDKLTPSHG NKVLLEGAKR LGYTAKIVPQ NCGDNAHHDG YCTLGCWKGE KNGPVNGWFP
EAAEQGVKFV EGMKVDKVLF DVKKGKRVAV GVEGVWTPRG GAEQVKVVVK SKKVVVSCGT
LWSPVVLMNS GLKNPQIGKN LYLHPTNFVM GVFDENVQPW EGGCLTSVVS DFDNLDGKGH
GVKLEAIFLP WTTGQNYKLH AAKYPHLNAF IAICRDRDTG HIYRDPVSGC PRIAYTPSDF
DRAHNLRGII ELSRILFSSG AREIVPALPG LEPFVVSADK SADKTKDDFE KWIARLKQHG
NRPPSTPFAS AHQMGTCRMS AREKDGVVDP RGRVWGTEGL YVADASVFPS ASGVNPMITV
MAIAEHIARG IVEDLKGEGM QAKFLTTGAE INNTRKDHRL NLAAQERRYS FDGRRSTTSN
SRDLDS
//
