ID A0A165QCE5_9APHY Unreviewed; 218 AA.
AC A0A165QCE5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Semialdehyde dehydrogenase NAD-binding domain-containing protein {ECO:0000259|Pfam:PF01118};
GN ORFNames=DAEQUDRAFT_271030 {ECO:0000313|EMBL:KZT69272.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT69272.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT69272.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT69272.1,
RC ECO:0000313|Proteomes:UP000076727};
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 -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004450}.
CC -!- SIMILARITY: Belongs to the FMP52 family.
CC {ECO:0000256|ARBA:ARBA00006617}.
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DR EMBL; KV429059; KZT69272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165QCE5; -.
DR STRING; 1314783.A0A165QCE5; -.
DR OrthoDB; 1457777at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR PANTHER; PTHR14097; OXIDOREDUCTASE HTATIP2; 1.
DR PANTHER; PTHR14097:SF7; OXIDOREDUCTASE HTATIP2; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT DOMAIN 7..82
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01118"
SQ SEQUENCE 218 AA; 23362 MW; 1A1C0A7604FB559C CRC64;
MAGLSALILG ATGATGKVLL QELLASPKFS SVSEYGRHVT APEKVAAGKD KLEQKTIDFE
KLDDAGLKDK KWDVVFITLG TTRKNAGSAE AFEKIDRDGG ANANSPFLYM KSKGKTELAL
ADLGYSDTVI FRPAALGDAD RNEHRPLEVY VHAAAKAIST FIPSIYMPVP KLAKAMRVVG
EVGSQGVPPE RVRKMGSEKA PWSILDNNAI LAIADSFN
//
