ID   B4DDF8_HUMAN            Unreviewed;       422 AA.
AC   B4DDF8;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   04-NOV-2026, entry version 73.
DE   SubName: Full=cDNA FLJ51786, highly similar to Retinal dehydrogenase 1 {ECO:0000313|EMBL:BAG56719.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG56719.1};
RN   [1] {ECO:0000313|EMBL:BAG56719.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adrenal gland {ECO:0000313|EMBL:BAG56719.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-hydroxynon-2-enal + NAD(+) + H2O = (E)-4-hydroxynon-2-
CC         enoate + NADH + 2 H(+); Xref=Rhea:RHEA:67248, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58968, ChEBI:CHEBI:142920;
CC         Evidence={ECO:0000256|ARBA:ARBA00050931};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67249;
CC         Evidence={ECO:0000256|ARBA:ARBA00050931};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetaldehyde + NAD(+) + H2O = acetate + NADH + 2 H(+);
CC         Xref=Rhea:RHEA:25294, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00050562};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25295;
CC         Evidence={ECO:0000256|ARBA:ARBA00050562};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + NAD(+) + H2O = a carboxylate + NADH + 2 H(+);
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:ARBA00051641};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186;
CC         Evidence={ECO:0000256|ARBA:ARBA00051641};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=malonaldehyde + NAD(+) + H2O = 3-oxopropanoate + NADH + 2
CC         H(+); Xref=Rhea:RHEA:67252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33190, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:566274; Evidence={ECO:0000256|ARBA:ARBA00052044};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67253;
CC         Evidence={ECO:0000256|ARBA:ARBA00052044};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=propanal + NAD(+) + H2O = propanoate + NADH + 2 H(+);
CC         Xref=Rhea:RHEA:67256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17153, ChEBI:CHEBI:17272, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00050831};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67257;
CC         Evidence={ECO:0000256|ARBA:ARBA00050831};
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; AK293176; BAG56719.1; -; mRNA.
DR   AlphaFoldDB; B4DDF8; -.
DR   PeptideAtlas; B4DDF8; -.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   CDD; cd07141; ALDH_F1AB_F2_RALDH1; 1.
DR   FunFam; 3.40.605.10:FF:000029; Aldehyde dehydrogenase, mitochondrial; 1.
DR   FunFam; 3.40.605.10:FF:000026; Aldehyde dehydrogenase, putative; 1.
DR   FunFam; 3.40.309.10:FF:000001; Mitochondrial aldehyde dehydrogenase 2; 1.
DR   Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1.
DR   Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   2: Evidence at transcript level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          1..413
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        224
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10008"
SQ   SEQUENCE   422 AA;  45997 MW;  F8CF0A555F2368AE CRC64;
     MDASERGRLL YKLADLIERD RLLLATMESM NGGKLYSNAY LNDLAGCIKT LRYCAGWADK
     IQGRTIPIDG NFFTYTRHEP IGVCGQIIPW NFPLVMLIWK IGPALSCGNT VVVKPAEQTP
     LTALHVASLI KEAGFPPGVV NIVPGYGPTA GAAISSHMDI DKVAFTGSTE VGKLIKEAAG
     KSNLKRVTLE LGGKSPCIVL ADADLDNAVE FAHHGVFYHQ GQCCIAASRI FVEESIYDEF
     VRRSVERAKK YILGNPLTPG VTQGPQIDKE QYDKILDLIE SGKKEGAKLE CGGGPWGNKG
     YFVQPTVFSN VTDEMRIAKE EIFGPVQQIM KFKSLDDVIK RANNTFYGLS AGVFTKDIDK
     AITISSALQA GTVWVNCYGV VSAQCPFGGF KMSGNGRELG EYGFHEYTEV KTVTVKISQK
     NS
//