ID G5AKU7_HETGA Unreviewed; 521 AA.
AC G5AKU7;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Aldehyde dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040706};
DE EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
DE AltName: Full=ALDH class 2 {ECO:0000256|ARBA:ARBA00041743};
DE AltName: Full=ALDH-E2 {ECO:0000256|ARBA:ARBA00042494};
GN Name=ALDH2 {ECO:0000313|EMBL:JAN96297.1};
GN ORFNames=GW7_10136 {ECO:0000313|EMBL:EHA97640.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHA97640.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHA97640.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
RN [2] {ECO:0000313|EMBL:JAN96297.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver {ECO:0000313|EMBL:JAN96297.1};
RA Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA Platzer M., Szafranski K.;
RT "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for clearance of cellular formaldehyde, a cytotoxic
CC and carcinogenic metabolite that induces DNA damage.
CC {ECO:0000256|ARBA:ARBA00037438}.
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 -!- 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|RuleBase:RU003345}.
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DR EMBL; JH165689; EHA97640.1; -; Genomic_DNA.
DR EMBL; GEBF01007335; JAN96297.1; -; Transcribed_RNA.
DR RefSeq; XP_004843838.1; XM_004843781.2.
DR AlphaFoldDB; G5AKU7; -.
DR STRING; 10181.G5AKU7; -.
DR GeneID; 101706449; -.
DR KEGG; hgl:101706449; -.
DR CTD; 217; -.
DR eggNOG; KOG2450; Eukaryota.
DR InParanoid; G5AKU7; -.
DR OMA; HGIGYYP; -.
DR OrthoDB; 2291791at2759; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR Bgee; ENSHGLG00000010830; Expressed in ovary and 10 other cell types or tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:Ensembl.
DR GO; GO:0106435; F:carboxylesterase activity; IEA:Ensembl.
DR GO; GO:0018547; F:nitroglycerin reductase activity; IEA:Ensembl.
DR GO; GO:0046185; P:aldehyde catabolic process; IEA:Ensembl.
DR GO; GO:1903179; P:regulation of dopamine biosynthetic process; IEA:Ensembl.
DR GO; GO:1905627; P:regulation of serotonin biosynthetic process; IEA:Ensembl.
DR CDD; cd07141; ALDH_F1AB_F2_RALDH1; 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:SF233; ALDEHYDE DEHYDROGENASE, 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.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813}.
FT DOMAIN 49..512
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 289
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 521 AA; 56503 MW; A8F928473DC44809 CRC64;
MLRAAAVAAA DLGPRLGCRL LSVGAAQAIP TPNQQPEVFY NQIFINNEWH DAVSKKTFPT
VNPSTGEVIC QVAEGNKEDV DKAVKAARAA FQLGSPWRRI NASERGRLLY RLADLIERDR
TYLAALETLD NGKPYVISYL VDLDMVLKCI RYYAGWADKY HGKTIPIDGD FFSYTRHEPV
GVCGQIIPWN FPLLMQAWKL GPALATGNVV VMKVAEQTPL TALYVASLIK EAGFPPGVVN
IVPGFGPTAG AAIASHEDVD KVAFTGSTEV GQLIQVAAGS SNLKKVTLEL GGKSPNIIMS
DADMDWAVEQ AHFALFFNQG QCCCAGSRTF VQENVYEEFV ERSVARAKAR VVGNPFDSQT
EQGPQVDETQ FKKILGYIKS GKEDGAKLLC GGGAAADRGY FIQPTVFGDV QDGMTIAKEE
IFGPVMQILK FKTIEEVVGR ANNSKYGLAA AVFTKDIDKA NYVSQALQAG TVWVNCYNVF
GAQSPFGGYK MSGSGRELGE YGLQAYTEVK TVTVKVPQKN S
//
