ID   LUC3_FUSSX              Reviewed;         461 AA.
AC   A0A6J4B898;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 1.
DT   03-AUG-2022, entry version 5.
DE   RecName: Full=Putative aldehyde dehydrogenase LUC3 {ECO:0000303|PubMed:32043422};
DE            EC=1.2.1.3 {ECO:0000250|UniProtKB:O34660};
DE   AltName: Full=Lucilactaene biosynthesis cluster protein 3 {ECO:0000303|PubMed:32043422};
GN   Name=LUC3 {ECO:0000303|PubMed:32043422};
OS   Fusarium sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=29916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=RK97-94;
RX   PubMed=32043422; DOI=10.1080/09168451.2020.1725419;
RA   Kato S., Motoyama T., Futamura Y., Uramoto M., Nogawa T., Hayashi T.,
RA   Hirota H., Tanaka A., Takahashi-Ando N., Kamakura T., Osada H.;
RT   "Biosynthetic gene cluster identification and biological activity of
RT   lucilactaene from Fusarium sp. RK97-94.";
RL   Biosci. Biotechnol. Biochem. 84:1303-1307(2020).
CC   -!- FUNCTION: Putative aldehyde dehydrogenase; part of the gene cluster
CC       that mediates the biosynthesis of the mycotoxin lucilactaene and the
CC       lucilactaene-related compound NG-391 that act as cell cycle inhibitors
CC       with potent growth inhibitory activity against malarial parasites,
CC       moderate growth inhibitory activity against cancer cells, and no
CC       activity against bacteria and fungi (PubMed:32043422). Within the
CC       cluster, LUC5, LUC6, LUC2 and LUC1 are sufficient for lucilactaene
CC       production (Probable). The roles of the other LUC members are yet
CC       undetermined (Probable). {ECO:0000269|PubMed:32043422,
CC       ECO:0000305|PubMed:32043422}.
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:0000250|UniProtKB:O34660};
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; LC515193; BBQ09590.1; -; Genomic_DNA.
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; cd07106; ALDH_AldA-AAD23400; 1.
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; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR044086; FUS7/LUC3-like.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..461
FT                   /note="Putative aldehyde dehydrogenase LUC3"
FT                   /id="PRO_0000454635"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   BINDING         215..220
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O34660"
SQ   SEQUENCE   461 AA;  49296 MW;  3662C511E749EAB2 CRC64;
     MDFTTFHNII GGKPRGSDNS HSGVDPLTRT TLWPVPTASP QDVDDAVEAA QRALPAWSQA
     SYDERTGLLE KFADLYLSRA GDFCQLLASE CGRTVENAAI EVYWAAQWLR YPSSYKLPEE
     QIEDDTKTAI VTYEPLGVVA AICPWNSIGK IAPALATGNC VILKPSPFTP YTSLKLVELA
     QEVFPPSVIQ VLSGGNGLGP ALVKHPGIQK ISFTGSTATG KQILKDGADT MKRITLETAG
     NNPAIILPDI DVTATVPHIS GGLWFNAGQV CIAPRRLYIH ADIFDVFVDA LVETTKEATK
     EMTKIGPVQN ELQFRKLVKT LDDAKSAGHD MATGGPLADA ETGGFFLRPT IIKDASPESS
     IVSGEHFGPI VTCVRFSDAD EAVHLANAGE SGLAASIWTT NLTAAKALAS RLDVGSVYIN
     GPPQPDPRVP FGGHKQSGLG VEYGLQGLLS FCQTKAVYLY K