ID A9ZSY8_9ASCO Unreviewed; 576 AA.
AC A9ZSY8;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Formate oxidase 1 {ECO:0000313|EMBL:BAF98891.1};
GN Name=FOD1 {ECO:0000313|EMBL:BAF98891.1};
OS Schwanniomyces vanrijiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Schwanniomyces.
OX NCBI_TaxID=27305 {ECO:0000313|EMBL:BAF98891.1};
RN [1] {ECO:0000313|EMBL:BAF98891.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18685206; DOI=10.1271/bbb.80121;
RA Maeda Y., Oki M., Fujii Y., Hatanaka A., Hojo M., Hirano K., Uchida H.;
RT "Cloning and expression of three formate oxidase genes from Debaryomyces
RT vanrijiae MH201.";
RL Biosci. Biotechnol. Biochem. 72:1999-2004(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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; AB371646; BAF98891.1; -; mRNA.
DR AlphaFoldDB; A9ZSY8; -.
DR UniPathway; UPA00147; -.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0047639; F:alcohol oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046188; P:methane catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
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:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 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; PS00623; GMC_OXRED_1; 1.
PE 2: Evidence at transcript level;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968}.
FT DOMAIN 86..109
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
SQ SEQUENCE 576 AA; 64144 MW; DB8F5581DA85615F CRC64;
MVQSHYDFVI VGGGTAGNTV AGRLAENPNV TVLVVEAGVA NSADLPEITT PSNAMNLRGS
KHDWAYKTTL VKRDDYERIE KPNTRGKALG GSSSLNYFTW IPGCKPTFDR WAEYGGEEWT
WDPLVPYLRK SATYHDDTGL YNPELKKLGA GGPIPISHSE LVEELEPFRE NLIKAWKSTG
KPFTENIYDG EMIGLNHCIS TIYHGKRSGS FLFVKNRPNI TIIPEVHSKN LIIDASNTAK
GVVVIDKEGN EHSFYATREV ILSQGVFESP KLLMLSGVGP RKELESNGIE VKVESRHVGQ
NLLDHPGVPF VLQVKDDICV DDILMRQNEK NKAAHVQYQK DGSGPVGSGL LELVGFPRID
EYFEKDPLYR ERKAANGGKD PFCPEGQPHF ELDFVGMYGT AFQWHFPTPK KGSHITIVVD
LVRPVSEGGE VTLNSADPLE QPKINLNFFA DELDIVGMRE GIRFTYDLLT KGDGFKDLVV
KEFPWEMPLD DDKEMRRAVL DRCQTAFHPC GTNRLSKNIE QGVVDPALKV HGVKNLRVID
ASIIPVIPDC RIQNSVYMIG EKGADLIKAA HKDLYN
//
