ID   B4DLJ0_HUMAN            Unreviewed;       218 AA.
AC   B4DLJ0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Aldehyde dehydrogenase X, mitochondrial {ECO:0000256|ARBA:ARBA00040048};
DE            EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
DE   AltName: Full=Aldehyde dehydrogenase family 1 member B1 {ECO:0000256|ARBA:ARBA00041645};
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:BAG59552.1};
RN   [1] {ECO:0000313|EMBL:BAG59552.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Cord blood {ECO:0000313|EMBL:BAG59552.1};
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=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   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC       step 2/2. {ECO:0000256|ARBA:ARBA00037885}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986}.
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DR   EMBL; AK297020; BAG59552.1; -; mRNA.
DR   AlphaFoldDB; B4DLJ0; -.
DR   SMR; B4DLJ0; -.
DR   MaxQB; B4DLJ0; -.
DR   PeptideAtlas; B4DLJ0; -.
DR   ProteomicsDB; 4538; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR11699:SF207; ALDEHYDE DEHYDROGENASE X, MITOCHONDRIAL; 1.
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.
PE   2: Evidence at transcript level;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          2..209
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   218 AA;  24588 MW;  B6A4D1B6DF55CB85 CRC64;
     MEHAVEQCHE ALFFNMGQCC CAGSRTFVEE SIYNEFLERT VEKAKQRKVG NPFELDTQQG
     PQVDKEQFER VLGYIQLGQK EGAKLLCGGE RFGERGFFIK PTVFGGVQDD MRIAKEEIFG
     PVQPLFKFKK IEEVVERANN TRYGLAAAVF TRDLDKAMYF TQALQAGTVW VNTYNIVTCH
     TPFGGFKESG NGRELGEDGL KAYTEVKTVT IKVPQKNS
//