ID   ALDH_ALTAL              Reviewed;         497 AA.
AC   P42041;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   04-NOV-2008, entry version 54.
DE   RecName: Full=Aldehyde dehydrogenase;
DE            Short=ALDDH;
DE            Short=ALDH;
DE            EC=1.2.1.3;
DE   AltName: Full=Allergen Alt a X;
DE   AltName: Allergen=Alt a 10;
GN   Name=ALTA10;
OS   Alternaria alternata (Alternaria rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporaceae;
OC   mitosporic Pleosporaceae; Alternaria; Alternaria alternata group.
OX   NCBI_TaxID=5599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=08-0203-Berlin;
RX   MEDLINE=95206305; PubMed=7898496; DOI=10.1016/0161-5890(94)00108-D;
RA   Achatz G., Oberkofler H., Lechenauer E., Simon-Nobbe B., Unger A.,
RA   Kandler D., Ebner C., Prillinger H., Kraft D., Breitenbach M.;
RT   "Molecular cloning of major and minor allergens of Alternaria
RT   alternata and Cladosporium herbarum.";
RL   Mol. Immunol. 32:213-227(1995).
RN   [2]
RP   SEQUENCE REVISION TO 73; 153-166; 334-336 AND 424.
RA   Simon-Nobbe B.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   REVIEW.
RX   PubMed=17709917; DOI=10.1159/000107578;
RA   Simon-Nobbe B., Denk U., Poell V., Rid R., Breitenbach M.;
RT   "The spectrum of fungal allergy.";
RL   Int. Arch. Allergy Immunol. 145:58-86(2008).
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   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; X78227; CAA55071.2; -; mRNA.
DR   PIR; S43108; S43108.
DR   HSSP; P05091; 1O04.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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   Allergen; Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN         1    497       Aldehyde dehydrogenase.
FT                                /FTId=PRO_0000056434.
FT   NP_BIND     241    246       NAD (By similarity).
FT   ACT_SITE    264    264       Proton acceptor (By similarity).
FT   ACT_SITE    298    298       Nucleophile (By similarity).
FT   SITE        148    148       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   497 AA;  53916 MW;  75DB63C621DFFB5C CRC64;
     MTSVKLSTPQ TGEFEQPTGL FINNEFVKAV DGKTFDVINP STEEVICSVQ EATEKDVDIA
     VAAARKAFNG PWRKETPENR GKLLNKLADL FEKNADLIAA VEALDNGKAF SMAKNVDVPA
     AAGCLRYYGG WADKIEGKVV DTAPDSFNYI RKEPIGVCGQ IIPWNFPILM WSWKIGPAIA
     TGNTVVLKTA EQTPLSAYIA CKLIQEAGFP PGVINVITGF GKIAGAAMSA HMDIDKIAFT
     GSTVVGRQIM KSAAGSNLKK VTLELGGKSP NIVFADADLD EAIHWVNFGI YFNHGQACCA
     GSRIYVQEEI YDKFIQRFKE RAAQNAVGDP FAADTFQGPQ VSQLQFDRIM GYIEEGKKSG
     ATIETGGNRK GDKGYFIEPT IFSNVTEDMK IQQEEIFGPV CTISKFKTKA DVIKIGNNTT
     YGLAAAVHTS NLTTAIEVAN ALRAGTVWVN SYNTLHWQLP FGGYKESGIG RELGEAALDN
     YIQTKTVSIR LGDVLFG
//