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Database: UniProt
Entry: G7XYM0_ASPKW
LinkDB: G7XYM0_ASPKW
Original site: G7XYM0_ASPKW 
ID   G7XYM0_ASPKW            Unreviewed;       477 AA.
AC   G7XYM0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:GAA92029.1};
GN   ORFNames=AKAW_10143 {ECO:0000313|EMBL:GAA92029.1};
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA92029.1};
RN   [1] {ECO:0000313|EMBL:GAA92029.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA92029.1};
RX   PubMed=22045919; DOI=10.1128/EC.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
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, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; DF126487; GAA92029.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7XYM0; -.
DR   STRING; 1033177.G7XYM0; -.
DR   VEuPathDB; FungiDB:AKAW_10143; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   InParanoid; G7XYM0; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd07106; ALDH_AldA-AAD23400; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR044086; LUC3-like.
DR   PANTHER; PTHR11699:SF263; ALDEHYDE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          26..470
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   477 AA;  52118 MW;  ACF384556F558CB6 CRC64;
     MGSLDKIDFT TFYNTINNEL TTTAATRHSL NPATRKPNPP VPVSTASDLN RAVDSARNAF
     KTWSKLSPSE RRSKVVALGE AIDLHAEELT ALLVQEQGKP HGQAAIEVSM SGTWCKQIPQ
     LELSDEVLQD TDDQRVIQRF TPMGVVAGIV PWNFPLLLAV GKIAPAVYTG NCIIIKPSPF
     TPYCALKIGE LAAKIFPPGV VQVLSDDGNI GPLMTAHPGI NKISFTGSTE TGKRIMRHCA
     DTLKSVTLEL GGNDPAIVCE DVDIEQVVPQ IATLSFLVSA QVCMMIKRLY VHEKIYDKFL
     EAFVNFTKNL KVGNGTEPDV FFGPVQNEMQ YGKLKDLFSS IQTENLKPAL GGSITESEGY
     FVTPTIIDNP PDNSRVVQEE PFGPILPLMK WSDEDEVIAR ANDTDTGLGA SVWSKDVDRA
     QRIGTQLESG SVWINSHFQV APNIPFGGMK ASGNGREWGL EGLKSYTQSQ MLWVKKA
//
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