INPF_EMENI
ID INPF_EMENI Reviewed; 437 AA.
AC Q5B7I6; C8V547;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Esterase inpF {ECO:0000303|PubMed:27294372};
DE EC=3.1.2.- {ECO:0000305};
DE AltName: Full=Fellutamide B biosynthesis cluster protein F {ECO:0000303|PubMed:27294372};
DE AltName: Full=Inp cluster protein F {ECO:0000303|PubMed:20952652};
GN Name=inpF {ECO:0000303|PubMed:20952652}; ORFNames=ANIA_03494;
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 IDENTIFICATION.
RX PubMed=20952652; DOI=10.1128/aem.00683-10;
RA Bergmann S., Funk A.N., Scherlach K., Schroeckh V., Shelest E., Horn U.,
RA Hertweck C., Brakhage A.A.;
RT "Activation of a silent fungal polyketide biosynthesis pathway through
RT regulatory cross talk with a cryptic nonribosomal peptide synthetase gene
RT cluster.";
RL Appl. Environ. Microbiol. 76:8143-8149(2010).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=27294372; DOI=10.1021/acschembio.6b00213;
RA Yeh H.H., Ahuja M., Chiang Y.M., Oakley C.E., Moore S., Yoon O.,
RA Hajovsky H., Bok J.W., Keller N.P., Wang C.C., Oakley B.R.;
RT "Resistance gene-guided genome mining: serial promoter exchanges in
RT Aspergillus nidulans reveal the biosynthetic pathway for fellutamide B, a
RT proteasome inhibitor.";
RL ACS Chem. Biol. 11:2275-2284(2016).
CC -!- FUNCTION: Esterase; part of the inp gene cluster that mediates the
CC biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome
CC inhibitor (PubMed:20952652, PubMed:27294372). In the first step of
CC fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to
CC generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain
CC of inpB (PubMed:27294372). The 3-hydroxydodecanoyl-S-
CC phosphopantetheinyl-T0 is sequentially extended with L-Asn and L-Gln by
CC the two CAT modules of inpB (PubMed:27294372). The linear lipodipeptide
CC from inpB is then transferred onto inpA for the addition of the third
CC amino acid, L-Leu (PubMed:27294372). Reductive releasing of the
CC lipotripeptide by the TE domain of inpA produces (2S)-fellutamide B
CC (PubMed:27294372). InpF might be involved in the release and transfer
CC of the lipodipeptide from inpB to inpA (PubMed:27294372). The inp
CC cluster-encoded proteasome subunit inpE confers resistance to
CC internally produced fellutamides (PubMed:27294372). The MFS efflux
CC transporter inpD may contribute to fellutamide resistance as well
CC (PubMed:27294372). {ECO:0000269|PubMed:27294372,
CC ECO:0000305|PubMed:20952652}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:27294372}.
CC -!- DISRUPTION PHENOTYPE: Greatly diminishes the production of fellutamides
CC (PubMed:27294372). {ECO:0000269|PubMed:27294372}.
CC -!- SIMILARITY: Belongs to the LovG family. {ECO:0000305}.
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DR EMBL; BN001302; CBF76040.1; -; Genomic_DNA.
DR RefSeq; XP_661098.1; XM_656006.1.
DR AlphaFoldDB; Q5B7I6; -.
DR SMR; Q5B7I6; -.
DR STRING; 162425.CADANIAP00005263; -.
DR ESTHER; emeni-q5b7i6; FSH1.
DR EnsemblFungi; CBF76040; CBF76040; ANIA_03494.
DR EnsemblFungi; EAA59055; EAA59055; AN3494.2.
DR GeneID; 2872914; -.
DR KEGG; ani:AN3494.2; -.
DR eggNOG; KOG2551; Eukaryota.
DR HOGENOM; CLU_627035_0_0_1; -.
DR InParanoid; Q5B7I6; -.
DR OrthoDB; 1190789at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0019748; P:secondary metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR005645; FSH_dom.
DR Pfam; PF03959; FSH1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..437
FT /note="Esterase inpF"
FT /id="PRO_0000444113"
FT REGION 306..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 112
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P38777"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P38777"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P38777"
SQ SEQUENCE 437 AA; 49125 MW; E283649C330040B0 CRC64;
MRILFFHGHT QTGPVFERKT VRLREHIQRA YPGSTFFFPT GPIAYKVSDR LDYLSEIQRE
RSDNFKDPDL IETHAWFRLF EDDPPRGLLE SLDIAAEILR VEGPFDGVIC FSQGSVVGSM
MASLLEGPRR RQRFDEYAAS FPGAVRYPKS YKNINHPPLK FGITYGAYMG TSPVFNAFYS
EPLIETPFLH FMGEFDPVVP SEMVAAVDKA QIGGSRRRKV MHPGAHAIPV GDRYHEAVVD
FIRSACETSP TYFDLPSDEV PLLSYNDTPE QTPFQTPLLT PSLSSAVSTT SIPSSEATIL
ATRRLDQWEK SRSPRSNIRP RSTRRTVFSG RRSTSSSAES SAASQHSDHF EATRTPTSST
STVQMIEPTV NKEPNLAVRV VEDDTIVSGS EYEGEGWQEL LLSDLLNEML RRHGRPGRFY
FVPDGEGGRL ENGMRLN
