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Database: UniProt
Entry: B2AMP8_PODAN
LinkDB: B2AMP8_PODAN
Original site: B2AMP8_PODAN 
ID   B2AMP8_PODAN            Unreviewed;       333 AA.
AC   B2AMP8;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 5, supercontig 5 {ECO:0000313|EMBL:CAP65238.1};
GN   ORFNames=PODANS_5_4740 {ECO:0000313|EMBL:CAP65238.1};
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:CAP65238.1};
RN   [1] {ECO:0000313|EMBL:CAP65238.1, 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}, and S mat+
RC   {ECO:0000313|EMBL:CAP65238.1};
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:CAP65238.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP65238.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {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).
RN   [4] {ECO:0000313|EMBL:CDP29450.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA   Ait Benkhali J., 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   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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DR   EMBL; CU633871; CAP65238.1; -; Genomic_DNA.
DR   EMBL; FO904940; CDP29450.1; -; Genomic_DNA.
DR   RefSeq; XP_001905329.1; XM_001905294.1.
DR   AlphaFoldDB; B2AMP8; -.
DR   STRING; 515849.B2AMP8; -.
DR   GeneID; 6189562; -.
DR   KEGG; pan:PODANSg2353; -.
DR   VEuPathDB; FungiDB:PODANS_5_4740; -.
DR   eggNOG; KOG1205; Eukaryota.
DR   HOGENOM; CLU_010194_8_1_1; -.
DR   OrthoDB; 1767556at2759; -.
DR   Proteomes; UP000001197; Chromosome 5.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd05233; SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR44196; DEHYDROGENASE/REDUCTASE SDR FAMILY MEMBER 7B; 1.
DR   PANTHER; PTHR44196:SF5; POSSIBLE MULTI-FUNCTIONAL ENZYME WITH ACYL-COA-REDUCTASE ACTIVITY ACRA1; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197}.
SQ   SEQUENCE   333 AA;  36241 MW;  F5E087D07496D89B CRC64;
     MTDQTAQFTP RFRTDIYPFI EPSKYRGSLR NKVTIITGAA GAIGRGLAES FAVAGTKLVL
     TYNRTPPPPE LEERCLRFGA ADVSFVKCDV AELGGCEALV KETLELHGRA DILINNAGAN
     GLGPLHDQAP QDFIKEIAVN FHGPYYLMRL LLTHFRQQRS GCVLNIASRA GTVAIPYSTG
     YCSSKAALIN LTACAQKELD IDGLGEEVHM YSLHPGGIKS AMTLKKYSPE SVSTLPPQAQ
     SKFVNALDIY DDSPYLNGMV CVALATGMGK EVLRGKYFDV GQDLEDVLAQ REALRQNPDL
     YGLHTSFLGG LKNGGVPEGG YRKEEWGKEF PGF
//
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