TROPH_TALSN
ID TROPH_TALSN Reviewed; 515 AA.
AC B8M9K4;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Aldehyde dehydrogenase tropH {ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000303|PubMed:22508998};
DE EC=1.2.1.3 {ECO:0000255|PROSITE-ProRule:PRU10007};
DE AltName: Full=Tropolone synthesis protein H {ECO:0000303|PubMed:24863423};
GN Name=tropH {ECO:0000303|PubMed:24863423};
GN Synonyms=tsR4 {ECO:0000303|PubMed:22508998}; ORFNames=TSTA_117790;
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=22508998; DOI=10.1073/pnas.1201469109;
RA Davison J., al Fahad A., Cai M., Song Z., Yehia S.Y., Lazarus C.M.,
RA Bailey A.M., Simpson T.J., Cox R.J.;
RT "Genetic, molecular, and biochemical basis of fungal tropolone
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7642-7647(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=24863423; DOI=10.1002/anie.201403450;
RA al Fahad A., Abood A., Simpson T.J., Cox R.J.;
RT "The biosynthesis and catabolism of the maleic anhydride moiety of
RT stipitatonic acid.";
RL Angew. Chem. Int. Ed. 53:7519-7523(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- FUNCTION: Aldehyde dehydrogenase; part of the gene cluster that
CC mediates the biosynthesis of the tropolone class of fungal maleic
CC anhydrides (PubMed:22508998, PubMed:24863423). The pathway begins with
CC the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide
CC synthase (PKS) tropA (PubMed:22508998). 3-methylorcinaldehyde is the
CC substrate for the FAD-dependent monooxygenase tropB to yield a
CC dearomatized hydroxycyclohexadione (PubMed:22508998, PubMed:24863423).
CC The 2-oxoglutarate-dependent dioxygenase tropC then performs the
CC oxidative ring expansion to provide the first tropolone metabolite
CC stipitaldehyde (PubMed:22508998, PubMed:24863423). Trop D converts
CC stipitaldehyde into stipitacetal which is in turn converted to
CC stipitalide by the short-chain dehydrogenase/reductase tropE
CC (PubMed:24863423). The next steps involve tropF, tropG, tropH, tropI
CC and tropJ to form successive tropolone maleic anhydrides including
CC stipitaldehydic, stipitatonic and stipitatic acids (PubMed:24863423).
CC {ECO:0000269|PubMed:22508998, ECO:0000269|PubMed:24863423}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10007};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:24863423}.
CC -!- DISRUPTION PHENOTYPE: Leads to the accumulation of stipitaldehydic acid
CC (PubMed:24863423). {ECO:0000269|PubMed:24863423}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255}.
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DR EMBL; BK008910; DAA64705.1; -; Genomic_DNA.
DR EMBL; EQ962655; EED18006.1; -; Genomic_DNA.
DR RefSeq; XP_002481998.1; XM_002481953.1.
DR AlphaFoldDB; B8M9K4; -.
DR SMR; B8M9K4; -.
DR STRING; 28564.XP_002481998.1; -.
DR EnsemblFungi; EED18006; EED18006; TSTA_117790.
DR GeneID; 8105837; -.
DR VEuPathDB; FungiDB:TSTA_117790; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_0_1; -.
DR InParanoid; B8M9K4; -.
DR OrthoDB; 486019at2759; -.
DR PhylomeDB; B8M9K4; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
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; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..515
FT /note="Aldehyde dehydrogenase tropH"
FT /id="PRO_0000437134"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q28399,
FT ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 295
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q28399,
FT ECO:0000255|PROSITE-ProRule:PRU10007"
FT BINDING 238..243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q28399"
SQ SEQUENCE 515 AA; 55559 MW; D7AE8E7C9170E873 CRC64;
MAPNFPPIEE ALPLHHDLFY DGKWQTPITD SRRETLNPST GQVIGKIADA STTDVDKAVE
AAHKAFLSWK KTTMAERQGY MRRAAAILRE HAAELALVES YNTGNPVAAM VIDAERAANA
LDYFAGLIPM LRGEVLPGPF PTEDYLHYTV REPMGVVARF VASNHPFMFA GARMASVIAG
GNTVIIKPPE QAPLSCLRLA ELLENVFPPG VVNILPGGAE CGQALTCHPL VRKVSLIGSV
ATGKIIMRNA GSLMKQTSME LGGKNALIAF PDADIDHLVR SVAAGMNFTW AGQSCGSTSR
VFLHDSIHDE VLARVVEVVR KGFRPGLATD PTTTMGSLIS KAAQDRVLNY IASAREEGAR
LVTGGGMFDD LAGTPVEGGF FVQPTIFADV TPDMKIAREE IFGPVMSVLR WSDESELIRI
VNSTNYGLTG SIFTKDLATA QRMIRQVEAG FVWVNDVCKH FLNVPYGGIK DSGIGRDECI
DELFAYTNIK SVNINLGGAT HLGSRLSQAG QISNT
