ID B2A9F9_PODAN Unreviewed; 615 AA.
AC B2A9F9;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 1, supercontig 1 {ECO:0000313|EMBL:CAP59706.1};
GN ORFNames=PODANS_1_470 {ECO:0000313|EMBL:CAP59706.1};
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:CAP59706.1};
RN [1] {ECO:0000313|EMBL:CAP59706.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP59706.1};
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:CAP59706.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP59706.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; CU633438; CAP59706.1; -; Genomic_DNA.
DR RefSeq; XP_001912227.1; XM_001912192.1.
DR AlphaFoldDB; B2A9F9; -.
DR GeneID; 6196919; -.
DR KEGG; pan:PODANSg09273; -.
DR VEuPathDB; FungiDB:PODANS_1_470; -.
DR HOGENOM; CLU_002865_6_1_1; -.
DR OrthoDB; 858083at2759; -.
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; 4.10.450.10; Glucose Oxidase, domain 2; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027424; Glucose_Oxidase_domain_2.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552:SF115; DEHYDROGENASE XPTC-RELATED; 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.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 94..117
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 291..305
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 96
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 104..107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 615 AA; 67001 MW; 0D389391ABBE8615 CRC64;
MRLCGVIQVS CFAGLFPASI QAIKETYDYV IVGGGTAGLT VGDRLSESGK LGLYPCCVLT
LMTEPDGQRP GTLYNITSAP VAGLNNKTFP VSIGCVVGGS SAVNGMVFQR GNAKDYDVWG
ELGGGNPRVR WNWVDMLKYF KKSIQMTAPK PETAAFDLRY DTKYWGRNLT TNHTIFATFG
NQLNSSLLSD AFYEAAKRLS GMKVSPDAGS GQLGLQYYQT STNPYTGERS YSRTGHWDGL
NRANYDLLTA TRANKIVFDH HRAAGVQIYP RGESTKKTTI RARKEVILAA GAIHTPQILQ
LSGIGPADLL KRAGIPVKVD LPGVGYNFQD HTFIPAVSFS WLTSPLIPEH LNITVVDDGL
GKTSLGLSVE LPVVSPGSFK RIASKYESQD PATYLPKDTD RTIIRGYRKQ QQIYAREMRA
KDFSFLRATF SGDPSFVPII IHPVSRGTVL IDPAAGSDIE VEPIVNYRAA SNPIDVDVAV
EEIKFLRRFM TTGELSRYNA TEVVPGPGLE SDEALGAWVR ANTIPSVYHP VGTAAKMPRE
WGGVVGEDLM VYGVRGLSVV DASMMPTIVA GTTSMTVYAV AEKVRIDLDF FLLNLQADKR
EQAADLIKLR AGTIV
//
