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Database: UniProt
Entry: S8BIN4_DACHA
LinkDB: S8BIN4_DACHA
Original site: S8BIN4_DACHA 
ID   S8BIN4_DACHA            Unreviewed;       497 AA.
AC   S8BIN4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044146};
GN   ORFNames=H072_11540 {ECO:0000313|EMBL:EPS35122.1};
OS   Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS   (Monacrosporium haptotylum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Dactylellina.
OX   NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS35122.1, ECO:0000313|Proteomes:UP000015100};
RN   [1] {ECO:0000313|EMBL:EPS35122.1, ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS35122.1,
RC   ECO:0000313|Proteomes:UP000015100};
RX   PubMed=24244185;
RA   Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   PLoS Genet. 9:E1003909-E1003909(2013).
RN   [2] {ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA   Ahren D.G.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   Submitted (APR-2013) 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         Evidence={ECO:0000256|ARBA:ARBA00024149};
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPS35122.1}.
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DR   EMBL; AQGS01001233; EPS35122.1; -; Genomic_DNA.
DR   RefSeq; XP_011116842.1; XM_011118540.1.
DR   AlphaFoldDB; S8BIN4; -.
DR   STRING; 1284197.S8BIN4; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   HOGENOM; CLU_005391_0_0_1; -.
DR   OMA; HGIGYYP; -.
DR   OrthoDB; 216092at2759; -.
DR   Proteomes; UP000015100; Unassembled WGS sequence.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd07091; ALDH_F1-2_Ald2-like; 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: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   Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015100}.
FT   DOMAIN          28..488
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   497 AA;  54253 MW;  93DE2E8C36796A7C CRC64;
     MTTVQLETPI TGKYEQPVGL FINNEFIQGK KGQEFEVINP TTEKVICKVH EALEEDVDIA
     VAAARKAFAP GSEYRKLSTA NRGKLLLNLA DLFEKNIDTL AAIEALDNGK SITMARGDVG
     ACVGCLRYYG GWADKIHGKI ITTQEGNFAY TKREPIGVCG QIIPWNFPLL MWAWKIGPAI
     ACGCTLVLKT AEQTPLSGLY AAKLCKEAGF PPGVVNVISG FGKTAGAAIA SHMDIDKVAF
     TGSTFVGRSI LKAAASSNLK KVTLELGGKS PNIVFEDADI DEAISWVNFG IFYNHGQCCC
     AGSRIYVQES IYDKFVERFK ERAAENVVGD PFHDKTFQGP QVSQLQYDRI MDYIKIGKEE
     GAKVEIGGER HGDVGYFIQP TIFSNVKNDM KIMQEEIFGP VCAIAKFKDI DEALHIGNDT
     VYGLAAAVHT KNLNTALQVA DGLKAGTVWV NQYNMLHWSL PFGGFRQSGI GRELGKAALE
     NYTQIKTVSI NMKGAMF
//
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