ID   CLAH_PASFU              Reviewed;         154 AA.
AC   P0CU76;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2018, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Decarboxylase claH {ECO:0000303|PubMed:27274078};
DE            EC=4.1.1.- {ECO:0000269|PubMed:27274078};
DE   AltName: Full=Cladofulvin biosynthesis protein H {ECO:0000303|PubMed:27274078};
GN   Name=claH {ECO:0000303|PubMed:27274078}; ORFNames=Clafu190728;
OS   Passalora fulva (Tomato leaf mold) (Cladosporium fulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Fulvia.
OX   NCBI_TaxID=5499;
RN   [1]
RP   INDUCTION, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=27274078; DOI=10.1073/pnas.1603528113;
RA   Griffiths S., Mesarich C.H., Saccomanno B., Vaisberg A., De Wit P.J.,
RA   Cox R., Collemare J.;
RT   "Elucidation of cladofulvin biosynthesis reveals a cytochrome P450
RT   monooxygenase required for anthraquinone dimerization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:6851-6856(2016).
RN   [2]
RP   INDUCTION.
RX   PubMed=27997759; DOI=10.1111/mpp.12527;
RA   Griffiths S., Mesarich C.H., Overdijk E.J.R., Saccomanno B.,
RA   de Wit P.J.G.M., Collemare J.;
RT   "Down-regulation of cladofulvin biosynthesis is required for biotrophic
RT   growth of Cladosporium fulvum on tomato.";
RL   Mol. Plant Pathol. 19:369-380(2018).
CC   -!- FUNCTION: Decarboxylase involved in the biosynthesis of the
CC       bianthraquinone cladofulvin, a conidial pigment not required for
CC       virulence but that plays a role in fitness and resistance to
CC       environmental stresses including UV light and low-temperature stress
CC       (PubMed:27274078). The pathway begins with the synthesis of
CC       atrochrysone thioester by the polyketide synthase (PKS) claG. The
CC       atrochrysone carboxyl ACP thioesterase claF then breaks the thioester
CC       bond and releases the atrochrysone carboxylic acid from claG
CC       (PubMed:27274078). This compound is decarboxylated by claH to yield
CC       emodin, which is further converted to chrysophanol hydroquinone by the
CC       reductase claC and the dehydratase claB (PubMed:27274078). The
CC       cytochrome monooxygenase P450 claM then catalyzes the dimerization of
CC       nataloe-emodin to cladofulvin (PubMed:27274078).
CC       {ECO:0000269|PubMed:27274078}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=atrochrysone carboxylate + H(+) = atrochrysone + CO2;
CC         Xref=Rhea:RHEA:64264, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:149713, ChEBI:CHEBI:150016;
CC         Evidence={ECO:0000269|PubMed:27274078};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64265;
CC         Evidence={ECO:0000269|PubMed:27274078};
CC   -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:27274078}.
CC   -!- INDUCTION: Expression is positively regulated by the transcriptional
CC       regulator wor1 (PubMed:27274078). Expression is down-regulated during
CC       biotrophic growth within tomato leaves (PubMed:27997759).
CC       {ECO:0000269|PubMed:27274078, ECO:0000269|PubMed:27997759}.
CC   -!- MISCELLANEOUS: Contrary to the other identified cladofulvin
CC       biosynthesis genes, claH is not locatilzed in the cladofulvin cluster,
CC       but is co-regulated with the cluster genes.
CC       {ECO:0000269|PubMed:27274078}.
CC   -!- SIMILARITY: Belongs to the tpcK family. {ECO:0000305}.
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DR   AlphaFoldDB; P0CU76; -.
DR   OMA; WTQIHNQ; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR009799; EthD_dom.
DR   Pfam; PF07110; EthD; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
PE   1: Evidence at protein level;
KW   Lyase.
FT   CHAIN           1..154
FT                   /note="Decarboxylase claH"
FT                   /id="PRO_0000445896"
SQ   SEQUENCE   154 AA;  17845 MW;  426CF88CC71C26A0 CRC64;
     MATATTTTAT ESPSNSGRRQ ARYLCLTILG YRKPGMSEED YRNHMVNVSA PLTKDLMVKY
     GVKRWTQIHN QSETKALMSQ LFDPQMCNLA DYDCFSQVVF ENIEDYKRMK QDPWYKKHLV
     GDHENFADTK RSQMTIGWVE EFVRDGQVVE GFKG