ID A0A0F4YQW8_TALEM Unreviewed; 489 AA.
AC A0A0F4YQW8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Aldehyde dehydrogenase (NAD(+)) {ECO:0000313|EMBL:KKA20033.1};
DE EC=1.2.1.3 {ECO:0000313|EMBL:KKA20033.1};
GN ORFNames=T310_5976 {ECO:0000313|EMBL:KKA20033.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA20033.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA20033.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA20033.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024149};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKA20033.1}.
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DR EMBL; LASV01000297; KKA20033.1; -; Genomic_DNA.
DR RefSeq; XP_013326645.1; XM_013471191.1.
DR AlphaFoldDB; A0A0F4YQW8; -.
DR STRING; 1408163.A0A0F4YQW8; -.
DR GeneID; 25318296; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699:SF204; ALDEHYDE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:KKA20033.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958}.
FT DOMAIN 19..480
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 489 AA; 53243 MW; C3F66A22B3C68326 CRC64;
MTPEGIEPRL LINGKLVEAS DKKTFPLYNP TTREKIADVP EASEEDTNAA VAAAKAAFPS
WSALSPIQRG QCFKKLADLI REAHDELAYL EAISMGQPVS RYHDSYWAAA EFDYYSEAWL
RPQGTTSLHT PGFVNMTFRQ PYGVVAAIIP WNFPLGFFAK KTAPALMAGN TVVLKSSEKA
PLTLHDQSAK VATLVEKAGF PPGVLNIISG HGPLSGAILS SHMDVRVVTF TGSVRTGRQI
QMAAAKSNLK NVLLELGGKT PAVIFEDADL KKASEETRFS IQYNSGQVCM ANSRIYVQES
IADRFISLFK EKFAAVRAGD PTNKDTNHGP LADEAQYTTV TNYIEEGKKT GTLLHGGNGG
LQHLNGYFVE PTIFTNTPEN ARIVKEEIFG PVVVINTFKS EEEVIQKAND SEYGLYASVY
TKNLDRAMRM AKAFEAGTVS INCASPSLAP DMPFGGYKAS GIGREGWICG LDNYLETKTV
LMKVDSASQ
//
