ID A0A091CNJ8_FUKDA Unreviewed; 257 AA.
AC A0A091CNJ8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 19.
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};
GN ORFNames=H920_19561 {ECO:0000313|EMBL:KFO19098.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO19098.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO19098.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO19098.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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; KN125198; KFO19098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091CNJ8; -.
DR eggNOG; KOG2450; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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; 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; 2.
DR SUPFAM; SSF53720; ALDH-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT DOMAIN 112..171
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 173..255
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 257 AA; 28413 MW; D4822E684993B728 CRC64;
MQGSSHGTSQ HLLLRCFDAK DLEDDSKRGY TSVAVILSSF FRSIKPVFHN SHLDCVLSKR
SSSWTLLWCY LAPGFNSWGL GARALVPHPL VQQLVSIRPD TSLCPPPASS IETGFPPGVG
NIITGYGPTT GRAIAWHMDV DEVAFTSSTE ESHLTQKVAG DSNLKRVTLE LDDVRIVKEE
IIRPVQLLFK FKKIEEVIER ANNTRYGLAA AVFMQDLDKA MYFTQALQAG TVWVNTYNTV
TCHTPFGALR NLAVGRS
//
