ID F8P623_SERL9 Unreviewed; 458 AA.
AC F8P623;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=NAD binding dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SERLADRAFT_475225 {ECO:0000313|EMBL:EGO20890.1};
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1] {ECO:0000313|EMBL:EGO20890.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO20890.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "Evolution of plant cell wall degrading machinery underlies the functional
RT diversity of forest fungi.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL945439; EGO20890.1; -; Genomic_DNA.
DR RefSeq; XP_007321847.1; XM_007321785.1.
DR AlphaFoldDB; F8P623; -.
DR GeneID; 18820612; -.
DR KEGG; sla:SERLADRAFT_475225; -.
DR HOGENOM; CLU_039338_0_0_1; -.
DR OrthoDB; 5486868at2759; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR013944; OxRdtase_put_C.
DR PANTHER; PTHR43249:SF1; D-GLUCOSIDE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43249; UDP-N-ACETYL-2-AMINO-2-DEOXY-D-GLUCURONATE OXIDASE; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF08635; ox_reductase_C; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
FT DOMAIN 61..214
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 217..358
FT /note="Oxidoreductase putative C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08635"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 51134 MW; 005AD57D362BC3FE CRC64;
MASRRPSSNL EMTSTIPNRR GSERRGSDRR GSGFSSRRPS IDPSRLIPMD KASHVGGTDD
FNVVFIGAGN IMFGSDEGPW NHSFRFEHKL GLRLKVVALI DPAIERARAV LQKKCDSFVV
SAYQGTRVFK TLDDFVKNMS SKDRPRAVIV GSPPMFRGTI QPGRDVEMQI LKYFPGVAMF
IEKPIATGPK AEIEQAFTIA KRISDSKAVC SVGYMLRYLK AVQMMKRIIE ENDLTVMATI
ARYACAYEAI AKLDWWDKSK SAGPIVEQGT HFCDLSRYFG GEVDISSVTA HSLEWDENAG
HLSKMSVDES QIAPENRIPR VTAATWKYDS GAVGSFTHVA TLQGHNYSCE LEVHADGYSL
KLVNPYVQPM LYVRKPGDDH EQMITFPDDD PFFSEISNLI DIIEDIEEDP EAAQILSTYE
DACKTYELTW AIREASERSR DAKLARSKAA AEAVKEST
//