ALDH_DAVTA
ID ALDH_DAVTA Reviewed; 496 AA.
AC P40108;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Aldehyde dehydrogenase;
DE Short=ALDDH;
DE Short=ALDH;
DE EC=1.2.1.3;
DE AltName: Full=Allergen Cla h 3;
DE AltName: Full=Allergen Cla h III;
DE AltName: Allergen=Cla h 10;
GN Name=CLAH10; Synonyms=CLAH3;
OS Davidiella tassiana (Mycosphaerella tassiana) (Cladosporium herbarum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Cladosporium.
OX NCBI_TaxID=29918;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC STRAIN=280202-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 66; 74; 95; 110; 114-121; 158-165 AND 367.
RA Simon-Nobbe B.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000269|PubMed:7898496}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X78228; CAA55072.2; -; mRNA.
DR PIR; S43114; S43114.
DR PDB; 7KQV; X-ray; 3.18 A; A/B/C/D=1-496.
DR PDBsum; 7KQV; -.
DR AlphaFoldDB; P40108; -.
DR SMR; P40108; -.
DR Allergome; 218; Cla h 10.
DR Allergome; 3201; Cla h 10.0101.
DR PRIDE; P40108; -.
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 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 3D-structure; Allergen; Cytoplasm; NAD; Oxidoreductase.
FT CHAIN 1..496
FT /note="Aldehyde dehydrogenase"
FT /id="PRO_0000056437"
FT ACT_SITE 263
FT /evidence="ECO:0000250"
FT ACT_SITE 296
FT /evidence="ECO:0000250"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:7KQV"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 54..68
FT /evidence="ECO:0007829|PDB:7KQV"
FT TURN 69..74
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 77..93
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 115..130
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 194..205
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:7KQV"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 242..255
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 278..290
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:7KQV"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 342..357
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 397..405
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 408..415
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 431..440
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 443..449
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 463..469
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:7KQV"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:7KQV"
FT STRAND 481..488
FT /evidence="ECO:0007829|PDB:7KQV"
SQ SEQUENCE 496 AA; 53554 MW; D938B5D0D9B26999 CRC64;
MTSVQLETPH SGKYEQPTGL FINNEFVKGQ EGKTFDVINP SDESVITQVH EATEKDVDIA
VAAARKAFEG SWRQETPENR GKLLNNLANL FEKNIDLLAA VESLDNGKAI SMAKGDISMC
VGCLRYYGGW ADKITGKVID TTPDTFNYVK KEPIGVCGQI IPWNFPLLMW AWKIGPAIAC
GNTVVLKTAE QTPLGGLVAA SLVKEAGFPP GVINVISGFG KVAGAALSSH MDVDKVAFTG
STVVGRTILK AAASSNLKKV TLELGGKSPN IVFEDADIDN AISWVNFGIF FNHGQCCCAG
SRVYVQESIY DKFVQKFKER AQKNVVGDPF AADTFQGPQV SKVQFDRIME YIQAGKDAGA
TVETGGKRKG DKGYFIEPTI FSNVTEDMKI VKEEIFGPVC SIAKFKTKED AIKLGNASTY
GLAAAVHTKN LNTAIEVSNA LKAGTVWVNT YNTLHHQMPF GGYKESGIGR ELGEDALANY
TQTKTVSIRL GDALFG
