ID   ALDH_EMENI              Reviewed;         497 AA.
AC   P08157; C8VSL3; Q5BFX6; Q9C1Q6;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   24-JAN-2024, entry version 141.
DE   RecName: Full=Aldehyde dehydrogenase;
DE            Short=ALDDH;
DE            Short=ALDH;
DE            EC=1.2.1.3;
GN   Name=aldA; Synonyms=aspA; ORFNames=AN0554;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3036652; DOI=10.1016/0378-1119(87)90310-6;
RA   Pickett M., Gwynne D.I., Buxton F.P., Elliott R., Davies R.W.,
RA   Lockington R.A., Scazzocchio C., Sealy-Lewis H.M.;
RT   "Cloning and characterization of the aldA gene of Aspergillus nidulans.";
RL   Gene 51:217-226(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11102439; DOI=10.1074/jbc.m005769200;
RA   Flipphi M., Mathieu M., Cirpus I., Panozzo C., Felenbok B.;
RT   "Regulation of the aldehyde dehydrogenase gene (aldA) and its role in the
RT   control of the coinducer level necessary for induction of the ethanol
RT   utilization pathway in Aspergillus nidulans.";
RL   J. Biol. Chem. 276:6950-6958(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; M16197; AAA33293.1; -; Genomic_DNA.
DR   EMBL; AF260123; AAK18072.1; -; Genomic_DNA.
DR   EMBL; AACD01000007; EAA66653.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF89245.1; -; Genomic_DNA.
DR   PIR; A29055; A29055.
DR   RefSeq; XP_658158.1; XM_653066.1.
DR   AlphaFoldDB; P08157; -.
DR   SMR; P08157; -.
DR   BioGRID; 1957104; 1.
DR   STRING; 227321.P08157; -.
DR   EnsemblFungi; CBF89245; CBF89245; ANIA_00554.
DR   GeneID; 2876330; -.
DR   KEGG; ani:AN0554.2; -.
DR   VEuPathDB; FungiDB:AN0554; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   HOGENOM; CLU_005391_0_0_1; -.
DR   InParanoid; P08157; -.
DR   OMA; WSNTFNK; -.
DR   OrthoDB; 216092at2759; -.
DR   UniPathway; UPA00780; UER00768.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IMP:AspGD.
DR   GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IMP:AspGD.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046187; P:acetaldehyde catabolic process; IMP:AspGD.
DR   GO; GO:0019413; P:acetate biosynthetic process; IMP:AspGD.
DR   GO; GO:0045991; P:carbon catabolite activation of transcription; IMP:AspGD.
DR   GO; GO:0071470; P:cellular response to osmotic stress; IEP:AspGD.
DR   GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006067; P:ethanol metabolic process; IMP:AspGD.
DR   GO; GO:0006567; P:threonine catabolic process; IMP:AspGD.
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   PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..497
FT                   /note="Aldehyde dehydrogenase"
FT                   /id="PRO_0000056438"
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            165
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        191
FT                   /note="E -> Q (in Ref. 1; AAA33293)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        208
FT                   /note="G -> P (in Ref. 1; AAA33293)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        247
FT                   /note="R -> P (in Ref. 1; AAA33293)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        409
FT                   /note="E -> V (in Ref. 1; AAA33293)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   497 AA;  54139 MW;  9C6CFC62731A25BD CRC64;
     MSDLFTTIET PVIKYEQPLG LFINNEFVKG VEGKTFQVIN PSNEKVITSV HEATEKDVDV
     AVAAARAAFE GPWRQVTPSE RGILINKLAD LMERDIDTLA AIESLDNGKA FTMAKVDLAN
     SIGCLRYYAG WADKIHGQTI DTNPETLTYT RHEPVGVCGQ IIPWNFPLLM WSWKIGPAVA
     AGNTVVLKTA EQTPLSALYA AKLIKEAGFP AGVINVISGF GRTAGAAISS HMDIDKVAFT
     GSTLVGRTIL QAAAKSNLKK VTLELGGKSP NIVFDDADID NAISWANFGI FFNHGQCCCA
     GSRILVQEGI YDKFVARFKE RAQKNKVGNP FEQDTFQGPQ VSQLQFDRIM EYINHGKKAG
     ATVATGGDRH GNEGYFIQPT VFTDVTSDMK IAQEEIFGPV VTIQKFKDEA EAIKIGNSTD
     YGLAAAVHTK NVNTAIRVSN ALKAGTVWIN NYNMISYQAP FGGFKQSGLG RELGSYALEN
     YTQIKTVHYR LGDALFA
//