ID ALDH2_LEITA Reviewed; 498 AA. AC Q25417; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 50. DE RecName: Full=Aldehyde dehydrogenase, mitochondrial; DE EC=1.2.1.3; DE AltName: Full=ALDH class 2; DE AltName: Full=P51; DE Flags: Precursor; GN Name=ALDH2; OS Leishmania tarentolae (Sauroleishmania tarentolae). OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmania; OC lizard Leishmania. OX NCBI_TaxID=5689; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 10-31. RC STRAIN=UC; RX MEDLINE=95356798; PubMed=7630384; DOI=10.1016/0166-6851(95)00023-T; RA Bringaud F., Peris M., Zen K.H., Simpson L.; RT "Characterization of two nuclear-encoded protein components of RT mitochondrial ribonucleoprotein complexes from Leishmania RT tarentolae."; RL Mol. Biochem. Parasitol. 71:65-79(1995). CC -!- FUNCTION: Could have a RNA-binding activity in addition of its CC catalytic role. CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = an acid + NADH. CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from CC ethanol: step 2/2. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z31698; CAA83503.1; -; Genomic_DNA. DR PIR; S43184; S43184. DR HSSP; P05091; 1O01. DR BRENDA; 1.2.1.3; 1138. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:EC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH. DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1. DR PANTHER; PTHR11699; Aldehyde_dehyd; 1. DR Pfam; PF00171; Aldedh; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; KW RNA-binding; Transit peptide. FT TRANSIT 1 9 Mitochondrion. FT CHAIN 10 498 Aldehyde dehydrogenase, mitochondrial. FT /FTId=PRO_0000007171. FT NP_BIND 242 247 NAD (By similarity). FT ACT_SITE 265 265 Proton acceptor (By similarity). FT ACT_SITE 299 299 Nucleophile (By similarity). FT SITE 166 166 Transition state stabilizer (By FT similarity). SQ SEQUENCE 498 AA; 54252 MW; 618D55F6ED5547EC CRC64; MLRATLARLE MAPKVTHIQE KLLINGKFVP AVSGKTFEVV NPADEKVIAN VAEAEKADVD LAVKAARHAF ESFRMTDCQW RRNLMLRLAD ILEKNSKEMA ALESLDNGKP YEVALNVDVA LSVECFRYCA GLADKVNGTV PPRSGNFLGI VKRQPIGVCG QIIPWNFPLL MAAFKLSPAL AMGNTVVLKP AEQTPLTAVR LGEMVMEAGY PDGVLNILPG FGATAGSEIA RHMDVDKIAF TGSTAVGHQV MQMAAETNLK KVSLELGGKS ALIVCEDADL EEAAEVATTR VYFNTGQVCT ASSRIYVHES VYDEFVSRLR KNAEARKVGP GNDTGNNMGP LVSKKQHERV LGYIEDGVKA GATVVTGGKK IGDKGYFVQP TIFSDVKEDM RICKEEIFGP VTCVMKYKDM DEVVKRANDS IYGLAAGICT RSMDTALRYS TYLNAGTVWV NTWNNFCPSM PFGGFKQSGI GRELGKEVVD MYTEPKAIHF ASRSIVKP //