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   03-AUG-2022, entry version 97.
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) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=08-0203-Berlin;
RX   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 alternata and
RT   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:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC       step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X78227; CAA55071.2; -; mRNA.
DR   PIR; S43108; S43108.
DR   AlphaFoldDB; P42041; -.
DR   SMR; P42041; -.
DR   Allergome; 13; Alt a 10.
DR   Allergome; 3057; Alt a 10.0101.
DR   PRIDE; P42041; -.
DR   UniPathway; UPA00780; UER00768.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 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
FT                   /note="Aldehyde dehydrogenase"
FT                   /id="PRO_0000056434"
FT   ACT_SITE        264
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        298
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         241..246
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            148
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
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