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Database: UniProt
Entry: Q2U0U1_ASPOR
LinkDB: Q2U0U1_ASPOR
Original site: Q2U0U1_ASPOR 
ID   Q2U0U1_ASPOR            Unreviewed;       486 AA.
AC   Q2U0U1;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN   ORFNames=AO090011000306 {ECO:0000313|EMBL:BAE64824.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE64824.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE64824.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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|RuleBase:RU003345}.
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DR   EMBL; AP007171; BAE64824.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2U0U1; -.
DR   STRING; 510516.Q2U0U1; -.
DR   EnsemblFungi; BAE64824; BAE64824; AO090011000306.
DR   HOGENOM; CLU_005391_1_0_1; -.
DR   OMA; LCWTGCK; -.
DR   OrthoDB; 178592at2759; -.
DR   Proteomes; UP000006564; Chromosome 7.
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; cd07102; ALDH_EDX86601; 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   PANTHER; PTHR11699:SF275; ALDEHYDE DEHYDROGENASE (NAD) FAMILY PROTEIN (EUROFUNG); 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 2.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006564}.
FT   DOMAIN          4..293
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          311..478
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   486 AA;  53266 MW;  FD0EFD4B52566F22 CRC64;
     MVNQIRTLSP STNKVIFEHP GTSLDEARAI AQASENAFQS YKQLSLADRK AIMVKALNIV
     DANKETLANE LTAQMGRPIA YCTKEIDTMR KRADYLLSIA DDSLKNLPGQ AESGFRRFLK
     KEPLGVTLIS TAWNYPYLIT VNTLLPALLA GNTVLLRPSP QTPLLGERLV SYFHEAGLPT
     NVLQLLHVGS LDVLDEIVKL PQIKLVSFTG STAGGLRLRE ATARRVVPVN LELGGNDPAY
     VRPDADIAYV AAQIVDGAVF NSGQSCCSIE RVYVHADIYD NFITEVQKEL STLVELLLVY
     LKITSRRTNK SSYKLGDPTD KATTTGPVIS KQALKNIQSH IDDALSKGAI DATPENTTFT
     SLPAEGNYIA PKLLTNVTHD MVTMREETFG PVIPVMRVSS DEEAVALMND SDYGLTASVW
     TKDIKAGEAL IEKIDAGTVY INRCDYPSPD LAWIGWKNSG LGCTLGPHAF DGFYKLKSFH
     IKEEQT
//
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