ID   AL1B1_RAT               Reviewed;         519 AA.
AC   Q66HF8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   04-NOV-2008, entry version 38.
DE   RecName: Full=Aldehyde dehydrogenase X, mitochondrial;
DE            EC=1.2.1.3;
DE   AltName: Full=Aldehyde dehydrogenase family 1 member B1;
DE   Flags: Precursor;
GN   Name=Aldh1b1; Synonyms=Aldhx;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 55-75; 162-174; 327-340 AND 444-453, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: ALDHs play a major role in the detoxification of
CC       alcohol-derived acetaldehyde. They are involved in the metabolism
CC       of corticosteroids, biogenic amines, neurotransmitters, and lipid
CC       peroxidation (By similarity).
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   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; BC081884; AAH81884.1; -; mRNA.
DR   RefSeq; NP_001011975.1; -.
DR   UniGene; Rn.12547; -.
DR   SMR; Q66HF8; 26-519.
DR   Ensembl; ENSRNOG00000011497; Rattus norvegicus.
DR   GeneID; 298079; -.
DR   KEGG; rno:298079; -.
DR   RGD; 1306737; Aldh1b1.
DR   HOVERGEN; Q66HF8; -.
DR   NextBio; 643122; -.
DR   ArrayExpress; Q66HF8; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016160; Ald_DHase_CS.
DR   InterPro; IPR016162; Ald_DHase_N.
DR   InterPro; IPR015590; Aldehyde_DHase.
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   Transit peptide.
FT   TRANSIT       1     19       Mitochondrion (Potential).
FT   CHAIN        20    519       Aldehyde dehydrogenase X, mitochondrial.
FT                                /FTId=PRO_0000271413.
FT   NP_BIND     264    269       NAD (By similarity).
FT   ACT_SITE    287    287       Proton acceptor (By similarity).
FT   ACT_SITE    321    321       Nucleophile (By similarity).
FT   SITE        188    188       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   519 AA;  57625 MW;  6D25E0E806F8EA50 CRC64;
     MLNARFLVPR LLCLQGRTTS YSTAAALPNP IPNPEIRYNQ LFINNEWHDA VSKKTFPTVN
     PTTGEVIGHV AEGDRADVDL AVRAAREAFR LGSPWRRMDA SERGRLLNRL ADLVERDRVY
     LASLETLDNG KPFQESYVLD LDEVIKVYRY LAGWADKWHG KTIPMDGEHF CFTRHEPVGV
     CGQIIPWNFP LVMQGWKLAP ALATGNTVVM KVAEQTPLSA LYLASLIKEA GFPPGVVNII
     TGYGPTAGAA IAQHMDVDKV AFTGSTEVGH LIQKAAGDSN LKRVTLELGG KSPSIVLADA
     DMDHAVDQCH EALFFNMGQC CCAGSRTFVE ESIYHEFLER TVEKAKKRKV GNPFELDTQQ
     GPQVDKEQFE KILGYIRLGQ KEGAKLLCGG ERFGERGFFI KPTVFGNVQD DMRIAREEIF
     GPVQPLFKFK KIEEVIQRAN NTRYGLAAAV FTRDLDKALY FSQALQAGTV WVNTYNIVTC
     HTPFGGFKES GNGRELGEDG LKAYTEVKTV TIKVSEKNS
//