ID   AL1B1_BOVIN             Reviewed;         511 AA.
AC   P52476;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 65.
DE   RecName: Full=Aldehyde dehydrogenase X, mitochondrial;
DE            EC=1.2.1.3;
DE   AltName: Full=Aldehyde dehydrogenase family 1 member B1;
DE   AltName: Full=ALDH class 2;
DE   AltName: Full=ALDHX;
DE   Flags: Precursor; Fragment;
GN   Name=ALDH1B1; Synonyms=ALDH1B2, ALDH5, ALDHX;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology
RT   and evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 284-409.
RC   TISSUE=Cornea;
RX   MEDLINE=93263009; PubMed=8493893;
RA   Algar E.M., Cheung B., Hayes J., Holmes R.S., Beacham I.R.;
RT   "Bovine corneal aldehyde dehydrogenases: evidence for multiple gene
RT   products (ALDH3 and ALDHX).";
RL   Adv. Exp. Med. Biol. 328:153-157(1993).
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. In the cornea, this enzyme may help in the
CC       absorption of the damaging UV-B, as well as in the detoxification
CC       of the UV-induced peroxidic aldehydes.
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; AAFC03050684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S61045; AAB26659.1; -; mRNA.
DR   IPI; IPI00908070; -.
DR   PIR; I46935; I46935.
DR   UniGene; Bt.13145; -.
DR   HSSP; P05091; 1O02.
DR   Ensembl; ENSBTAG00000020385; Bos taurus.
DR   HOVERGEN; P52476; -.
DR   OMA; P52476; EALFFNM.
DR   BRENDA; 1.2.1.3; 251.
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_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; FALSE_NEG.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Mitochondrion; NAD; Oxidoreductase; Transit peptide.
FT   TRANSIT      <1     11       Mitochondrion (Potential).
FT   CHAIN        12    511       Aldehyde dehydrogenase X, mitochondrial.
FT                                /FTId=PRO_0000056477.
FT   NP_BIND     256    261       NAD (By similarity).
FT   ACT_SITE    279    279       Proton acceptor (By similarity).
FT   ACT_SITE    313    313       Nucleophile (By similarity).
FT   SITE        180    180       Transition state stabilizer (By
FT                                similarity).
FT   CONFLICT    308    308       N -> S (in Ref. 2; AAB26659).
FT   NON_TER       1      1
SQ   SEQUENCE   511 AA;  56770 MW;  D032C6E84D9799B3 CRC64;
     PRLFALHHSA TQYFSAAALP SPIPNPDIPD NQLFISNKWH DAVSKKTFPT VSPATGEVIG
     HVAEGDWADV DLAAKAARAA FRLGSPWRWM DALKRGWLLN HLADLVERDC VYLASLESLD
     NGKPFQESYV LDLDEVIKVY RYFAGWADKW HGKTIPMDGE HFCFTRHEPV GVCCQIIPWN
     FPLVMQSWKL ALALAMGNTV VTKVAEQTPF SALYLASLIK EVGLPPGLVN IVTGYGPTAG
     AAIAHHMDIG KVAFTGSTKV GHLIQKAAGN SSLKRVTLEL GGKSLSIVLA DADMDHAVEQ
     RQEALFFNMG QCCCPGSWTF IEESIYDEFL ERTVEKAKQR RVGNPFDLDT QQGPQVDRER
     FERILGYIQL GQKEGAKLLC GGEHFRQQCF FIKPTVFGGV QDDMRIAREE IFGPVQPLFK
     FKKIEEVIER ADNTRYGLAA AVFTQDLDKA MYFTQALQTG TVWVNTYNVV TCHTPLGGFK
     EPGNGRELGE DGLKAYTEVK TVTIKVPQKN S
//