ID   ALDH5_YEAS7             Reviewed;         520 AA.
AC   A6ZR27;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   04-NOV-2008, entry version 16.
DE   RecName: Full=Aldehyde dehydrogenase 5, mitochondrial;
DE            EC=1.2.1.3;
DE            EC=1.2.1.4;
DE   Flags: Precursor;
GN   Name=ALD5; ORFNames=SCY_1574;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R.,
RA   Wang X., Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S.,
RA   Li Y., Davis R.W., Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces
RT   cerevisiae strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Minor mitochondrial aldehyde dehydrogenase isoform.
CC       Plays a role in regulation or biosynthesis of electron transport
CC       chain components. Involved in the biosynthesis of acetate during
CC       anaerobic growth on glucose (By similarity).
CC   -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = an acid + NADH.
CC   -!- CATALYTIC ACTIVITY: An aldehyde + NADP(+) + H(2)O = an acid +
CC       NADPH.
CC   -!- ENZYME REGULATION: Induced by potassium ions (By similarity).
CC   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from
CC       ethanol: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; AAFW02000048; EDN63047.1; -; Genomic_DNA.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:EC.
DR   GO; GO:0033721; F:aldehyde dehydrogenase (NADP+) activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016163; Ald_DHase_C.
DR   InterPro; IPR016160; Ald_DHase_CS.
DR   InterPro; IPR016162; Ald_DHase_N.
DR   InterPro; IPR015590; Aldehyde_DHase.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
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   3: Inferred from homology;
KW   Complete proteome; Mitochondrion; NAD; NADP; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1     23       Mitochondrion (Potential).
FT   CHAIN        24    520       Aldehyde dehydrogenase 5, mitochondrial.
FT                                /FTId=PRO_0000330043.
FT   NP_BIND     266    271       NAD (By similarity).
FT   ACT_SITE    288    288       Proton acceptor (By similarity).
FT   ACT_SITE    322    322       Nucleophile (By similarity).
FT   SITE        190    190       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   520 AA;  56693 MW;  DCD382A1157F800A CRC64;
     MLSRTRAAAP NSRIFTRSLL RLYSQAPLRV PITLPNGFTY EQPTGLFING EFVASKQKKT
     FDVINPSNEE KITTVYKAME DDVDEAVAAA KKAFETKWSI VEPEVRAKAL FNLADLVEKH
     QETLAAIESM DNGKSLFCAR GDVALVSKYL RSCGGWADKI YGNVIDTGKN HFTYSIKEPL
     GVCGQIIPWN FPLLMWSWKI GPALATGNTV VLKPAETTPL SALFASQLCQ EAGIPAGVVN
     ILPGSGRVVG ERLSAHPDVK KIAFTGSTAT GRHIMKVAAD TVKKVTLELG GKSPNIVFAD
     ADLDKAVKNI AFGIFYNSGE VCCAGSRIYI QDTVYEEVLQ KLKDYTESLK VGDPFDEEVF
     QGAQTSDKQL HKILDYVDVA KSEGARLVTG GARHGSKGYF VKPTVFADVK EDMRIVKEEV
     FGPIVTVSKF STVDEVIAMA NDSQYGLAAG IHTNDINKAV DVSKRVKAGT VWINTYNNFH
     QNVPFGGFGQ SGIGREMGEA ALSNYTQTKS VRIAIDKPIR
//