PKFF_EMENI
ID PKFF_EMENI Reviewed; 611 AA.
AC Q5B8A1; A0A1U8QJW1; C8VI77;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Dehydrogenase pkfF {ECO:0000303|PubMed:23706169};
DE EC=1.1.-.- {ECO:0000305|PubMed:23706169};
DE Flags: Precursor;
GN Name=pkfF {ECO:0000303|PubMed:23706169}; ORFNames=ANIA_03229;
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: Dehydrogenase; part of the gene cluster that mediates the
CC biosynthesis of aspernidine A, a prenylated isoindolinone
CC (PubMed:23706169). The starting point of the biosynthesis of aspernidin
CC A is the production of orsellinaldehyde by the non-reducing polyketide
CC synthase pkfA (PubMed:22510154). Hydroxylation, methylation of one of
CC the phenol groups, and prenylation, presumably catalyzed by the
CC prenyltransferase pkfE, would be needed to yield aspernidine D
CC (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is
CC responsible for hydroxylation of aspernidine D to yield aspernidine E
CC (PubMed:23706169). The dehydrogenase pkfF may be responsible for
CC further oxidation of aspernidine E to form a dialdehyde intermediate
CC which is further transformed in a series of steps, some of which are
CC enzyme-mediated, to generate aspernidine A (Probable). The possibility
CC that additional enzymes outside of the cluster are involved in
CC aspernidine A biosynthesis cannot be excluded (Probable).
CC {ECO:0000269|PubMed:22510154, ECO:0000269|PubMed:23706169,
CC ECO:0000305|PubMed:23706169}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:E4QP00};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:23706169}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of aspernidine A, but
CC accumulates the intermediate aspernidine E.
CC {ECO:0000269|PubMed:23706169}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AACD01000054; EAA63130.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF83141.1; -; Genomic_DNA.
DR RefSeq; XP_660833.1; XM_655741.1.
DR AlphaFoldDB; Q5B8A1; -.
DR SMR; Q5B8A1; -.
DR STRING; 227321.Q5B8A1; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR EnsemblFungi; CBF83141; CBF83141; ANIA_03229.
DR EnsemblFungi; EAA63130; EAA63130; AN3229.2.
DR GeneID; 2874279; -.
DR KEGG; ani:AN3229.2; -.
DR VEuPathDB; FungiDB:AN3229; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_3_1; -.
DR InParanoid; Q5B8A1; -.
DR OMA; SWANWVD; -.
DR OrthoDB; 798314at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..611
FT /note="Dehydrogenase pkfF"
FT /evidence="ECO:0000255"
FT /id="PRO_5010314143"
FT ACT_SITE 547
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 50..51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 71..72
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 137..140
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 581
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 592..593
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 611 AA; 65610 MW; 97680097DC12A3F7 CRC64;
MRHTALLPLV SSFIVPALAQ IPGQTTVNAT VNQGRFGNAT YDYVIVGGGT SGLAIAARLA
EDPSLSVAVI EAGGYYELDG TVASIIPGLA AGANVGTDAT EYSTVDWNFQ AQPLTSANDR
SLRYNRGKTL GGSSARHYMV YQRGTRGSYD QWAELTGDES WGWDSVFPYF QRSVNVTPAN
MTGRFPNTTV TYDPSGFNKA GGPLHVTWPN YGSPWSTWIE QGLEAIGILP DTDFNTGTLN
GSSWAPITIN PLSQKRDSSE TSFLQQSLKT TNLTVYLHTM ALKIGFDGTT ASSVDVRSPV
GRFTLSARRE IIVSAGALQS PQLLMVSGIG PRETLERHGI PVVKELAGVG QKMWEHPFFG
ITHQVNLVTA TELAINQQAL LQALNQYKSQ QGPLTSAGFG VLGWEKLPNS TLSDSTNEAL
ATFPSDWPTI EYLSIDGYLN GWHSAADQAT GNGQQWGTIA VALVAPLSRG NVTISSSDMD
DPPVFDLGFL THPADREIAV AAMRRIRQAF AAISEITIGD EVVPGADVST DEELLDFIRE
SIVPVYHVAG TCAMGREDDP EAVVDPQARV IGVNNLRVVD ASIFPTLPPG HPQSTCYMVA
EKIADLIKKG N
