ID V5FXD6_BYSSN Unreviewed; 665 AA.
AC V5FXD6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=alcohol oxidase {ECO:0000256|ARBA:ARBA00013077};
DE EC=1.1.3.13 {ECO:0000256|ARBA:ARBA00013077};
GN ORFNames=PVAR5_1905 {ECO:0000313|EMBL:GAD93297.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD93297.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + O2 = an aldehyde + H2O2;
CC Xref=Rhea:RHEA:19829, ChEBI:CHEBI:15379, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478; EC=1.1.3.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001411};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- PATHWAY: Energy metabolism; methane degradation.
CC {ECO:0000256|ARBA:ARBA00005144}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix
CC {ECO:0000256|ARBA:ARBA00004253}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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:GAD93297.1}.
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DR EMBL; BAUL01000053; GAD93297.1; -; Genomic_DNA.
DR AlphaFoldDB; V5FXD6; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_5_1_1; -.
DR InParanoid; V5FXD6; -.
DR OrthoDB; 2392848at2759; -.
DR Proteomes; UP000018001; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF119; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Methanol utilization {ECO:0000256|ARBA:ARBA00023095};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000018001}.
FT DOMAIN 269..283
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 227
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 570..571
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 665 AA; 74462 MW; D8860418562A3D17 CRC64;
MTIPEEVDII ICGGGSSGCV PAGRLANLDH NLQVLLIEAG EDNLNNPWVY RPGIYPRNMK
LDSKTASFYY SRPSQYLDGR RAIVPCAHIL GGGSSINFMM YTRASASDYD DFQAKGWTTR
ELIPLMKKHE TYQRACNNRD LHGFEGPIKV SFGNYTYPIM QDFLRAAESQ GIPITDDLQD
LKTGHGAEHW LKWINRDTGR RSDAAHAYIH STRSKFDNLH LKTSTKVDKV IIENGRAVGV
ATVPTKPLNG TNPERKIYRA RKQIIVSGGT LSSPLILQRS GVGDPQKLRE AGIKPIVDLP
GVGRNFQDHY LTFAVYRAKP DVESFDDFIR GDPEVQKKVF DEWNIKGTGP LATNGIDAGV
KIRPTEEELA EMRNWPTPEF QSGWDSYFKN KPDKPVMHYS VISGWFGDHM LMPPGKFFTM
FHFLEYPFSR GWIHVKSPDP YEAPDFDAGF MNDKRDMAPM VWGYIKSRET ARRMAAYAGE
VTAMHPHFSY DSPARAFDMD LATTNAYAGP LHLSANIQHG SWSHPLEPGK SPAANFLNSN
RQETREALKY TKKDIEHIEK WVERHVETTW HCLGTNSMAP REGNSIVKHG VLDERLNVHG
VKGLKVSDLS ICPDNVGCNT FSTALLIGEK CAVLTAEDLG YSGSALDMKV PTYHAPGEVV
NLARL
//
