XPTC_EMENI
ID XPTC_EMENI Reviewed; 622 AA.
AC Q5AUN2; A0A1U8QUL7; C8V5L9;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Dehydrogenase xptC {ECO:0000303|PubMed:21351751};
DE EC=1.1.-.- {ECO:0000305|PubMed:21351751};
DE AltName: Full=Prenyl xanthone synthesis protein C {ECO:0000303|PubMed:21351751};
DE Flags: Precursor;
GN Name=xptC {ECO:0000303|PubMed:21351751}; ORFNames=AN7998;
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, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=21351751; DOI=10.1021/ja1096682;
RA Sanchez J.F., Entwistle R., Hung J.H., Yaegashi J., Jain S., Chiang Y.M.,
RA Wang C.C., Oakley B.R.;
RT "Genome-based deletion analysis reveals the prenyl xanthone biosynthesis
RT pathway in Aspergillus nidulans.";
RL J. Am. Chem. Soc. 133:4010-4017(2011).
RN [4]
RP FUNCTION.
RX PubMed=22730213; DOI=10.1002/cbic.201200014;
RA Simpson T.J.;
RT "Genetic and biosynthetic studies of the fungal prenylated xanthone
RT shamixanthone and related metabolites in Aspergillus spp. revisited.";
RL ChemBioChem 13:1680-1688(2012).
RN [5]
RP FUNCTION.
RX PubMed=23150454; DOI=10.1002/cbic.201200545;
RA Pockrandt D., Ludwig L., Fan A., Koenig G.M., Li S.M.;
RT "New insights into the biosynthesis of prenylated xanthones: Xptb from
RT Aspergillus nidulans catalyses an O-prenylation of xanthones.";
RL ChemBioChem 13:2764-2771(2012).
CC -!- FUNCTION: Dehydrogenase involved in the conversion of monodictyphenone
CC to the prenyl xanthones such as emericellin, shamixanthone and
CC epishamixanthone (PubMed:21351751, PubMed:22730213). Monodictyphenone
CC is first converted to variecoxanthone A via a paeciloxanthone
CC intermediate by the consecutive actions of the FAD-dependent
CC monooxygenase mdpD and the xanthone prenyltransferase xptB
CC (PubMed:21351751). XptB catalyzes regular O-prenylation at the hydroxy
CC group of C-7 of the xanthone ring (PubMed:23150454). Variecoxanthone A
CC is further prenylated to emericellin by xptA before being reduced to
CC shamixanthone and epishamixanthone by the dehydrogenase xptC
CC (PubMed:21351751). {ECO:0000269|PubMed:21351751,
CC ECO:0000269|PubMed:22730213, ECO:0000269|PubMed:23150454}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:E4QP00};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:21351751}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q12062}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of the xanthones
CC shamixanthone and epishamixanthone; and accumulates variecoxanthone A
CC and emericellin (PubMed:21351751). {ECO:0000269|PubMed:21351751}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; BN001302; CBF73676.1; -; Genomic_DNA.
DR EMBL; AACD01000137; EAA58801.1; -; Genomic_DNA.
DR RefSeq; XP_681267.1; XM_676175.1.
DR AlphaFoldDB; Q5AUN2; -.
DR SMR; Q5AUN2; -.
DR STRING; 227321.Q5AUN2; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR EnsemblFungi; CBF73676; CBF73676; ANIA_07998.
DR EnsemblFungi; EAA58801; EAA58801; AN7998.2.
DR GeneID; 2869062; -.
DR KEGG; ani:AN7998.2; -.
DR VEuPathDB; FungiDB:AN7998; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_1_1; -.
DR InParanoid; Q5AUN2; -.
DR OMA; SNAHQCC; -.
DR OrthoDB; 798314at2759; -.
DR Proteomes; UP000000560; Chromosome II.
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; IBA:GO_Central.
DR GO; GO:1900793; P:shamixanthone 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 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..622
FT /note="Dehydrogenase xptC"
FT /id="PRO_5010328443"
FT BINDING 47..48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 68..69
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 123..126
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 598..599
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 622 AA; 67812 MW; 5092031B88D5DEA3 CRC64;
MAKLSVILLF RSLLLCGALT VSRHATLVTE REVQSSKYDF IVVGGGVSGL TVADRLTEIP
DVSVLVIEAG PVDRGEDFVY VPGSYERDPY IWPGLTNEPS AELNNRVFDS VVARVAGGGS
IVNAMIFLRG TALDFDGWES LGNHGWGWEG MLPYFIKSEN FTRPTPELAH EGNITWDDSV
RGHDGPVRYS YPNYIYPGLG RLYEAALHIG IQPRLDPNGG QNTGVFNQPF AIDAATWTRS
SARRNHYDPA VSRPNYHFLS DTTVARVIFD GTRAVGVEYL PSRGGGISTA FAAKEVLVAA
GALHTPQVLQ LSGVGPRDLL EALNIPIISD LPGVGSNLQD QTTFPFVYTW DSAVTPNVTT
FLTNTTWATE QRVLYDQHLP SVWTLTRPLA PKFAFLSYED ATANTAYASI LDDAQARDPA
DSLPGDIHPT VLAGYAVQRQ IMFNEFRDAG LAVGGMSWDT DANVQVFNVK PFSRGYVYIN
QTDPLANPVI DFRTASDPTD FQLHIALLHK QRELFNAPSL AALGPTEVVP GPAVQTDEDI
IKLMREILQP SNGHQCCSAP MMPRELGGVL SPEMKVYGTT GLRVIDISHW PKELSGPPMA
SIYAAGEKAA DIIKGEHGWL GN
