ID A2R2P1_ASPNC Unreviewed; 466 AA.
AC A2R2P1;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Contig An14c0070, genomic contig {ECO:0000313|EMBL:CAK41924.1};
DE EC=1.2.1.24 {ECO:0000313|EMBL:CAK41924.1};
GN ORFNames=An14g01440 {ECO:0000313|EMBL:CAK41924.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK41924.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK41924.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 Evidence={ECO:0000256|ARBA:ARBA00024149};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; AM270314; CAK41924.1; -; Genomic_DNA.
DR RefSeq; XP_001400771.1; XM_001400734.2.
DR AlphaFoldDB; A2R2P1; -.
DR SMR; A2R2P1; -.
DR EnsemblFungi; CAK41924; CAK41924; An14g01440.
DR GeneID; 4986999; -.
DR KEGG; ang:An14g01440; -.
DR VEuPathDB; FungiDB:An14g01440; -.
DR HOGENOM; CLU_005391_1_0_1; -.
DR OrthoDB; 178592at2759; -.
DR Proteomes; UP000006706; Chromosome 1R.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR CDD; cd07102; ALDH_EDX86601; 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 PANTHER; PTHR11699:SF275; ALDEHYDE DEHYDROGENASE (NAD) FAMILY PROTEIN (EUROFUNG); 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 Oxidoreductase {ECO:0000256|RuleBase:RU003345,
KW ECO:0000313|EMBL:CAK41924.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 4..458
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 466 AA; 50968 MW; BBC436E50D7EE72C CRC64;
MSNAIRTLSP STNKVIFEHP GLSLEEARQI AQASQDAFRT YKQTTLAQRK EIVLKALDLI
AANKDTLAEE LTTQMGRPIA FSAKEIETFR KRGDHILSIA EESLKSLPGT PENGFRRFLK
KEPVGPTLII TAWNFPYLVT INALVPALLA GNTVLLRPSP QTPIFGERLL TYFTQAGLPP
NVLQLVHVGS PDVLDQIVQL PQIQLISFTG STAGGFRIRE AVARRIVPVN LELGGNDPAY
VRPDADIPYV AAQLVDGAVF NSGQSCCAVE RVYVHADVHD KFVEEVQKEL ATYKLGSPHD
KSTTTGPVIS QAALKNIQSH IDDALSKGAV NATPKNPTFE NTPAEGNYQV PTVLTNVTHD
MVVMREETFG PVMPIMKVSS DEEAVALMND SDFGLTASVW TKDIAKGEDL IEQLDAGTVY
INRCDYPSPD LAWIGWKNSG LGCTLGPEGF NAFYKLKSFH IKEQQA
//
