ID B2ASX2_PODAN Unreviewed; 671 AA.
AC B2ASX2;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 6, supercontig 1 {ECO:0000313|EMBL:CAP67495.1};
GN ORFNames=PODANS_6_11490 {ECO:0000313|EMBL:CAP67495.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP67495.1};
RN [1] {ECO:0000313|EMBL:CAP67495.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP67495.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP67495.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP67495.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; CU633898; CAP67495.1; -; Genomic_DNA.
DR RefSeq; XP_001906824.1; XM_001906789.1.
DR AlphaFoldDB; B2ASX2; -.
DR GeneID; 6191130; -.
DR KEGG; pan:PODANSg3857; -.
DR VEuPathDB; FungiDB:PODANS_6_11490; -.
DR HOGENOM; CLU_002865_4_1_1; -.
DR OrthoDB; 3382025at2759; -.
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; 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:SF80; -; 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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..671
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002773890"
FT DOMAIN 366..380
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 671 AA; 71671 MW; F431272455242565 CRC64;
MLRLTTTILT GLTIFAIPAF AGGGGGGHGG YTKPEDNVYD YVIVGSGPGG GPLATNLAKA
GHSVLLVEAG DDQSNNPTSE IGALFFLPYQ DASMRWDFFV RNYANESRLL QHNHRVYRAT
EGTFYVGTSP PAGATLLGIH YPRGGTLGGS SAVNAMSSVL PSDSDWQIIA DLTGDTSWNP
TAMRSIFARI ENNHYLPSGT PGHGFNGYFD TSMSDESVWV GQDDMTTVMA EAADDLGQDR
LNIVDHLTAD VNALDPARDQ SVGVFGSAVH SDENARRFSS RDLVLETASA LTAAGKKKYP
LWIQLNTLAT KVTFKDINHP HRKPKATGIE YLQGQSVYRA DPRNTASNNG TWGRAFARKE
VIVSGGTFNS PQLLKLSGIG PAEELASFGI PLVKNLPGVG TNLQDNYEVP IVGHAASNFT
TPPPDPADPA CWFGAPGDPC VTLWQSQQGP YMKGATLNAV FRKSISPAYN ERDMFLVGGL
FALRGFWPPT DSIVPDPPNM FGFSTVKIGP QSRGGKVLLT STDPRDVPSI NFHLFEEGDA
GTAMDLAAEL DTVKFVRRLF ASVPAPLGPI SPVEPPCSGG MSADGTCDDA ADIEWLKNQI
FGHHPTSTCA IGADSDPNAV LDSKFRVRGV RGLRVVDASA FPRVPGPFPV LPTFMLSEKA
SESVLADAHT W
//
