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   22-FEB-2023, entry version 91.
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; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; 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   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 tarentolae.";
RL   Mol. Biochem. Parasitol. 71:65-79(1995).
CC   -!- FUNCTION: Could have an RNA-binding activity in addition of its
CC       catalytic role.
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   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; Z31698; CAA83503.1; -; Genomic_DNA.
DR   PIR; S43184; S43184.
DR   AlphaFoldDB; Q25417; -.
DR   SMR; Q25417; -.
DR   VEuPathDB; TriTrypDB:LtaPh_2511800; -.
DR   UniPathway; UPA00780; UER00768.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07091; ALDH_F1-2_Ald2-like; 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:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 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   Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; RNA-binding;
KW   Transit peptide.
FT   TRANSIT         1..9
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:7630384"
FT   CHAIN           10..498
FT                   /note="Aldehyde dehydrogenase, mitochondrial"
FT                   /id="PRO_0000007171"
FT   ACT_SITE        265
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        299
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         242..247
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            166
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P20000"
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
//