PKFC_EMENI
ID PKFC_EMENI Reviewed; 312 AA.
AC C8VI80; Q5B8A4;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Short-chain dehydrogenase/reductase pkfC {ECO:0000303|PubMed:23706169};
DE EC=1.1.1.- {ECO:0000305|PubMed:23706169};
DE AltName: Full=Aspernidine A biosynthesis cluster protein pkfC {ECO:0000303|PubMed:23706169};
GN Name=pkfC {ECO:0000303|PubMed:23706169}; ORFNames=ANIA_03226;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION.
RX PubMed=22510154; DOI=10.1021/ja3016395;
RA Ahuja M., Chiang Y.M., Chang S.L., Praseuth M.B., Entwistle R.,
RA Sanchez J.F., Lo H.C., Yeh H.H., Oakley B.R., Wang C.C.;
RT "Illuminating the diversity of aromatic polyketide synthases in Aspergillus
RT nidulans.";
RL J. Am. Chem. Soc. 134:8212-8221(2012).
RN [4]
RP IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION, AND PATHWAY.
RX PubMed=23706169; DOI=10.1021/ol401187b;
RA Yaegashi J., Praseuth M.B., Tyan S.W., Sanchez J.F., Entwistle R.,
RA Chiang Y.M., Oakley B.R., Wang C.C.;
RT "Molecular genetic characterization of the biosynthesis cluster of a
RT prenylated isoindolinone alkaloid aspernidine A in Aspergillus nidulans.";
RL Org. Lett. 15:2862-2865(2013).
RN [5]
RP INDUCTION.
RX PubMed=25701285; DOI=10.1534/genetics.115.174342;
RA Oiartzabal-Arano E., Garzia A., Gorostidi A., Ugalde U., Espeso E.A.,
RA Etxebeste O.;
RT "Beyond asexual development: modifications in the gene expression profile
RT caused by the absence of the Aspergillus nidulans transcription factor
RT FlbB.";
RL Genetics 199:1127-1142(2015).
CC -!- FUNCTION: Short-chain dehydrogenase/reductase; part of the gene cluster
CC that mediates the biosynthesis of aspernidine A, a prenylated
CC isoindolinone (PubMed:23706169). The starting point of the biosynthesis
CC of aspernidin A is the production of orsellinaldehyde by the non-
CC reducing polyketide synthase pkfA (PubMed:22510154). Hydroxylation,
CC methylation of one of the phenol groups, and prenylation, presumably
CC catalyzed by the prenyltransferase pkfE, would be needed to yield
CC aspernidine D (Probable). Subsequently, the cytochrome P450
CC monooxygenase pkfB is responsible for hydroxylation of aspernidine D to
CC yield aspernidine E (PubMed:23706169). The dehydrogenase pkfF may be
CC responsible for further oxidation of aspernidine E to form a dialdehyde
CC intermediate which is further transformed in a series of steps, some of
CC which are enzyme-mediated, to generate aspernidine A (Probable). The
CC possibility that additional enzymes outside of the cluster are involved
CC in aspernidine A biosynthesis cannot be excluded (Probable).
CC {ECO:0000269|PubMed:22510154, ECO:0000269|PubMed:23706169,
CC ECO:0000305|PubMed:23706169}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:23706169}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of Aspernidine A.
CC {ECO:0000269|PubMed:23706169}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA63127.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000054; EAA63127.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001306; CBF83147.1; -; Genomic_DNA.
DR RefSeq; XP_660830.1; XM_655738.1.
DR AlphaFoldDB; C8VI80; -.
DR SMR; C8VI80; -.
DR STRING; 162425.CADANIAP00009836; -.
DR EnsemblFungi; CBF83147; CBF83147; ANIA_03226.
DR EnsemblFungi; EAA63127; EAA63127; AN3226.2.
DR GeneID; 2874147; -.
DR KEGG; ani:AN3226.2; -.
DR VEuPathDB; FungiDB:AN3226; -.
DR eggNOG; KOG1208; Eukaryota.
DR HOGENOM; CLU_010194_44_6_1; -.
DR InParanoid; C8VI80; -.
DR OMA; MGKIQFD; -.
DR OrthoDB; 1032903at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0097308; P:cellular response to farnesol; IEP:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..312
FT /note="Short-chain dehydrogenase/reductase pkfC"
FT /id="PRO_0000446361"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 24..32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 51..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 87..89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 193..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 228..230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 312 AA; 34218 MW; D8BD74C513722FB3 CRC64;
MVFGSRPPAL TEANIGDQSG KVFIVTGATS GYGLLLSTYL YQNNGTVYLA ARNAKKTAEV
IADLKQRFPA SRGRLDSISL NLSDLSTIKK SAEEFLAKET RLHVLWNNAG VMFPPAGSTT
SQGYELQLGT NNVGPHLFTK LLYPTLAATA KEAPKNTVRV VWVSSDAASW APKPAIDFNN
LDYRRNESDR SKYGRSKAGT VMQAVELARR ARKDGSGIVS IALDPGIANT GLQRDMGRLM
STMVKLIANK PEIGAYTQLF AGLSPEITAE VAEKEWVVPP GKIGCPRRDL FTDTETSRKW
WEWNEEQVKA YL
