ID A0A166J3N5_9AGAM Unreviewed; 371 AA.
AC A0A166J3N5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=NAD-P-binding protein {ECO:0000313|EMBL:KZV74135.1};
GN ORFNames=PENSPDRAFT_237064 {ECO:0000313|EMBL:KZV74135.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV74135.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV74135.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV74135.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the HIBADH-related family. NP60 subfamily.
CC {ECO:0000256|ARBA:ARBA00007598}.
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; KV424483; KZV74135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166J3N5; -.
DR STRING; 1314672.A0A166J3N5; -.
DR InParanoid; A0A166J3N5; -.
DR OrthoDB; 1332762at2759; -.
DR Proteomes; UP000077086; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR029154; HIBADH-like_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43580; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR PANTHER; PTHR43580:SF2; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077086}.
FT DOMAIN 41..212
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 222..327
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 371 AA; 39661 MW; 9F3DB22CE8A559A6 CRC64;
MALRNTLHSF TTLNAPPTGH SADNIPYSRP VTPGASEQPL KIGWVGLGAM GYPMARNLAA
TPPTHPAVGL PIKVWNRSDG KSHELVKELG EGKVSIAQSP GELAVECDII FTSLASDEVV
EIVYGQFAEA LKTHPPSKAK IFVETSTIYP TVAGKLDKLI SSIPHCRLIT SPVFGPPAAA
KEGHLVAYLA GDYQSKKLIA HLLVPAVARK VTDLGGNLEK APTMKLIGNS MILGCLELLA
ESFTLGAKSG IDQQIIHDWV KEMFPVPLFA HYGDKMLNNK FDGSIGFGID GGIKDASHIR
RLTSQVNSPM PVTDVAHQHL LAARAIHTTQ ARTGAQDFEV LDWSALIAGT RVAAGLDPFH
KDEPSGVVKD D
//
