ID A0A090CV87_PODAN Unreviewed; 422 AA.
AC A0A090CV87;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:CDP30859.1};
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:CDP30859.1, ECO:0000313|Proteomes:UP000001197};
RN [1] {ECO:0000313|EMBL:CDP30859.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
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|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 2 subfamily. {ECO:0000256|ARBA:ARBA00038157}.
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DR EMBL; FO904941; CDP30859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090CV87; -.
DR eggNOG; KOG1575; Eukaryota.
DR InParanoid; A0A090CV87; -.
DR Proteomes; UP000001197; Chromosome 6.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43364; NADH-SPECIFIC METHYLGLYOXAL REDUCTASE-RELATED; 1.
DR PANTHER; PTHR43364:SF7; NADP-DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT DOMAIN 39..344
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
SQ SEQUENCE 422 AA; 46456 MW; 4EBA2AE3D0DDDAD2 CRC64;
MAPTFEEALT STFTLAPPPK SPLARYRLLS PTAGVRVSPL CLGGLNIGDE WKALMGEMTQ
PQAFSLLDYF YSAGGNFIDT ANAYQKEQSE QWIGEWMARR GVRDQMFIST KYSNNFRAGH
GETEIMASYI GNGTKSLHTS VHASLKKLQT GYIDLLFVHW YDYATSIPEL MQSLNVLVNQ
GKVLYLGISD APAWVVTKAN QYARDHALRG FSVYQGEWSA VARDFERDVI PMCREEGMGI
MPWGALGGGN FKSEGGQRRA EGVGGEGGRV HAPVGERHVK VAKALGRVAE RRGTGLTSVA
LAYVMQKAPY VFPVVGGRKI EHLRENIEAL KVRLEREDFE EIEGTVEFDL GWPNKLQFGG
RLPENMQDFW LMGTAGWFDN VPVVKAIVPA KEEEAGDLSS DHADGAKVVS LVSGGWKGVK
GE
//
