ID   AL1B1_MOUSE             Reviewed;         519 AA.
AC   Q9CZS1; Q3UAH5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   04-NOV-2008, entry version 58.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Embryo, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon;
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).
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.
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; AK012213; BAB28101.1; -; mRNA.
DR   EMBL; AK088396; BAC40326.1; -; mRNA.
DR   EMBL; AK150992; BAE30016.1; -; mRNA.
DR   EMBL; AK151349; BAE30325.1; -; mRNA.
DR   EMBL; AK151364; BAE30339.1; -; mRNA.
DR   EMBL; AK153416; BAE31976.1; -; mRNA.
DR   EMBL; BC020001; AAH20001.1; -; mRNA.
DR   EMBL; BC086768; AAH86768.1; -; mRNA.
DR   RefSeq; NP_082546.1; -.
DR   UniGene; Mm.331583; -.
DR   HSSP; P05091; 1O04.
DR   SMR; Q9CZS1; 26-519.
DR   PhosphoSite; Q9CZS1; -.
DR   Ensembl; ENSMUSG00000035561; Mus musculus.
DR   GeneID; 72535; -.
DR   KEGG; mmu:72535; -.
DR   NMPDR; fig|10090.3.peg.9526; -.
DR   MGI; MGI:1919785; Aldh1b1.
DR   HOVERGEN; Q9CZS1; -.
DR   NextBio; 336439; -.
DR   ArrayExpress; Q9CZS1; -.
DR   CleanEx; MM_ALDH1B1; -.
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   2: Evidence at transcript level;
KW   Mitochondrion; NAD; Oxidoreductase; Transit peptide.
FT   TRANSIT       1     19       Mitochondrion (Potential).
FT   CHAIN        20    519       Aldehyde dehydrogenase X, mitochondrial.
FT                                /FTId=PRO_0000271411.
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).
FT   CONFLICT    146    146       K -> R (in Ref. 1; BAE30339).
FT   CONFLICT    261    261       A -> T (in Ref. 1; BAE30339).
SQ   SEQUENCE   519 AA;  57553 MW;  69222D7409BFEEF3 CRC64;
     MLTARLLLPR LLCLQGRTTS YSTAAALPNP IPNPEICYNK LFINNEWHDA VSKKTFPTVN
     PTTGEVIGHV AEGDRADVDL AVKAAREAFR LGSPWRRMDA SERGRLLNRL ADLVERDRVY
     LASLETLDNG KPFQESYVLD LDEVIKVYRY FAGWADKWHG KTIPMDGEHF CFTRHEPVGV
     CGQIIPWNFP LVMQGWKLAP ALATGNTVVM KVAEQTPLSA LYLASLIKEA GFPPGVVNII
     TGYGPTAGAA IAQHMDVDKV AFTGSTEVGH LIQKAAGESN LKRVTLELGG KSPSIVLADA
     DMEHAVDQCH EALFFNMGQC CCAGSRTFVE ESIYREFLER TVEKAKQRKV GNPFELDTQQ
     GPQVDKEQFE RILGYIRLGQ KEGAKLLCGG ERLGERGFFI KPTVFGDVQD GMRIAKEEIF
     GPVQPLFKFK KIEEVIQRAN NTRYGLAAAV FTRDLDKAIY FTQALQAGTV WVNTYNIVTC
     HTPFGGFKES GNGRELGEDG LRAYTEVKTV TIKVPEKNS
//