PEX4_GIBZE
ID PEX4_GIBZE Reviewed; 172 AA.
AC I1RRW0;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 PEX4 {ECO:0000303|PubMed:30603875};
DE EC=2.3.2.23 {ECO:0000305|PubMed:30603875};
DE AltName: Full=E2 ubiquitin-conjugating enzyme PEX4 {ECO:0000303|PubMed:30603875};
DE AltName: Full=Peroxin-4 {ECO:0000303|PubMed:30603875};
DE AltName: Full=Peroxisome biogenesis factor 4 {ECO:0000303|PubMed:30603875};
GN Name=PEX4 {ECO:0000303|PubMed:30603875};
GN ORFNames=FG06857, FGRAMPH1_01T23345;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30603875; DOI=10.1007/s00294-018-0925-6;
RA Zhang L., Wang L., Liang Y., Yu J.;
RT "FgPEX4 is involved in development, pathogenicity, and cell wall integrity
RT in Fusarium graminearum.";
RL Curr. Genet. 65:747-758(2019).
CC -!- FUNCTION: Ubiquitin-conjugating enzyme E2 that is essential for
CC peroxisome biogenesis and plays a key role in development,
CC pathogenicity, and cell wall integrity (PubMed:30603875). Required for
CC long and very long-chain fatty acid utilization and is involved in
CC lipid droplet accumulation and the elimination of reactive oxygen
CC species (PubMed:30603875). Controls the expression of proteins involved
CC in protein biosynthesis, fatty acid metabolism, cell wall synthesis,
CC oxidation-reduction reactions, as well as of the enzymes involved in
CC the biosynthesis of the mycotoxin deoxynivalenol (DON), including TRI5,
CC TRI6, and TRI10 (PubMed:30603875). {ECO:0000269|PubMed:30603875}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000305|PubMed:30603875};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- DISRUPTION PHENOTYPE: Impairs hyphal growth, conidiation, conidial
CC germination, and sexual reproduction (PubMed:30603875). Leads to a
CC defect in pathogenicity and production of the mycotoxin deoxynivalenol
CC (DON) (PubMed:30603875). Displays lipid droplet accumulation
CC (PubMed:30603875). Shows reduced tolerance towards oxidative stress
CC (PubMed:30603875). Leads to down-regulation of protein expression
CC levels related to protein biosynthesis, fatty acid metabolism, cell
CC wall synthesis, and oxidation-reduction reactions (PubMed:30603875).
CC {ECO:0000269|PubMed:30603875}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; HG970335; CEF85136.1; -; Genomic_DNA.
DR RefSeq; XP_011326512.1; XM_011328210.1.
DR AlphaFoldDB; I1RRW0; -.
DR SMR; I1RRW0; -.
DR STRING; 5518.FGSG_06857P0; -.
DR GeneID; 23553966; -.
DR KEGG; fgr:FGSG_06857; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G23345; -.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_030988_13_0_1; -.
DR InParanoid; I1RRW0; -.
DR UniPathway; UPA00143; -.
DR PHI-base; PHI:8743; -.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0005777; C:peroxisome; TAS:PHI-base.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; TAS:PHI-base.
DR GO; GO:0016557; P:peroxisome membrane biogenesis; EXP:PHI-base.
DR GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; TAS:PHI-base.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Peroxisome biogenesis; Reference proteome;
KW Transferase; Ubl conjugation pathway; Virulence.
FT CHAIN 1..172
FT /note="Ubiquitin-conjugating enzyme E2 PEX4"
FT /id="PRO_0000449259"
FT DOMAIN 14..167
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 104
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 172 AA; 18966 MW; E9F13B019559F773 CRC64;
MPPSSSNTAA ASRSASKRLI KELETWSREQ KEEKGIERLG PVNEGDLMEW EAVINGRGIG
QGYDEGRWLV NISIPSTYPL APPKMTFVTP IVHPNIALQN GEICLDLLKD AWTPAYSVLE
CVRAVRMLLG CPETDSPLNV DVAALLRSGD VLGTRKLVEL WCQDSDSRYE GP
