ID ALDH2_MESAU Reviewed; 500 AA. AC P81178; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 24-JAN-2024, entry version 103. DE RecName: Full=Aldehyde dehydrogenase, mitochondrial; DE EC=1.2.1.3; DE AltName: Full=ALDH class 2; DE AltName: Full=ALDH-E2; DE AltName: Full=ALDH1; GN Name=ALDH2; OS Mesocricetus auratus (Golden hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; OC Cricetidae; Cricetinae; Mesocricetus. OX NCBI_TaxID=10036; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Liver; RX PubMed=9369242; DOI=10.1016/s0014-5793(97)01176-9; RA Hjelmqvist L., Lundgren R., Norin A., Joernvall H., Vallee B., Klyosov A., RA Keung W.M.; RT "Class 2 aldehyde dehydrogenase. Characterization of the hamster enzyme, RT sensitive to daidzin and conserved within the family of multiple forms."; RL FEBS Lett. 416:99-102(1997). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=20400973; DOI=10.1038/aja.2010.19; RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.; RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen RT (GP96) are unique to hamster caput epididymal spermatozoa."; RL Asian J. Androl. 12:344-355(2010). CC -!- FUNCTION: Required for clearance of cellular formaldehyde, a cytotoxic CC and carcinogenic metabolite that induces DNA damage. CC {ECO:0000250|UniProtKB:P05091}. 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 -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: CC step 2/2. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; P81178; -. DR SMR; P81178; -. DR STRING; 10036.ENSMAUP00000007329; -. DR eggNOG; KOG2450; Eukaryota. DR SABIO-RK; P81178; -. DR UniPathway; UPA00780; UER00768. DR Proteomes; UP000189706; Unplaced. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0106435; F:carboxylesterase activity; ISS:UniProtKB. DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; ISS:CAFA. DR GO; GO:0018547; F:nitroglycerin reductase activity; ISS:UniProtKB. DR GO; GO:0008957; F:phenylacetaldehyde dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0046185; P:aldehyde catabolic process; ISS:UniProtKB. DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:1903179; P:regulation of dopamine biosynthetic process; ISS:UniProtKB. DR GO; GO:1905627; P:regulation of serotonin biosynthetic process; ISS:UniProtKB. 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 1: Evidence at protein level; KW Acetylation; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; KW Reference proteome. FT CHAIN 1..500 FT /note="Aldehyde dehydrogenase, mitochondrial" FT /id="PRO_0000056468" FT ACT_SITE 268 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, FT ECO:0000255|PROSITE-ProRule:PRU10008" FT ACT_SITE 302 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, FT ECO:0000255|PROSITE-ProRule:PRU10008" FT BINDING 245..250 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT SITE 169 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P20000" FT MOD_RES 35 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 56 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 61 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 142 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 351 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 358 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 366 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 390 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 409 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 411 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 424 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 434 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" SQ SEQUENCE 500 AA; 54334 MW; 8B81886AB04F493F CRC64; SAAATSAVPA PNQQPEVFCN QIFINNEWHD AVSKKTFPTV NPSTGEVICQ VAEGSKEDVD KAVKAARAAF QLGSPWRRMD ASDRGRLLNR LADLIERDRT YLAALETLDN GKPYVISYLV DLDMVLKCLR YYAGWADKYH GKTIPIDGDF FSYTRHEPVG VCGQIIPWNF PLLMQAWKLG PALATGNVVV MKVAEQTPLT ALYVANLIKE AGFPPGVVNI VPGFGPTAGA AIASHEDVDK VAFTGSTEVG HLIQVAAGSS NLKRVTLELG GKSPNIIMSD ADMDWAVEQA HFALFFNQGQ CCCAGSRTFV QEDVYDEFVE RSVARAKSRV VGNPFDSRTE QGPQVDETQF KKILGYIKSG QQEGAKLLCG GGAAADRGYF IQPTVFGDVK DGMTIAKEEI FGPVMQILKF KTIEEVVGRA NNSKYGLAAA VFTKDLDKAN YLSQALQAGT VWINCYDVFG AQSPFGGYKM SGSGRELGEY GLQAYTEVKT VTIKVPQKNS //