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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//
