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DPH3_GIBZE
ID   DPH3_GIBZE              Reviewed;          86 AA.
AC   Q4I9U7; A0A0E0SKC8; V6RCR0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-SEP-2016, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Diphthamide biosynthesis protein 3;
GN   Name=DPH3; ORFNames=FGRRES_16587, FGSG_06011;
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).
CC   -!- FUNCTION: Required for the first step of diphthamide biosynthesis, a
CC       post-translational modification of histidine which occurs in elongation
CC       factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group
CC       from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction
CC       is assisted by a reduction system comprising KTI11/DPH3 and a NADH-
CC       dependent reductase, predominantly CBR1. Acts as an electron donor to
CC       reduce the Fe-S cluster in DPH1-DPH2 keeping the [4Fe-4S] clusters in
CC       the active and reduced state. Restores iron to DPH1-DPH2 iron-sulfur
CC       clusters which have degraded from [4Fe-4S] to [3Fe-4S] by donating an
CC       iron atom to reform [4Fe-4S] clusters, in a manner dependent on the
CC       presence of elongation factor 2 and SAM. Associates with the elongator
CC       complex and is required for tRNA Wobble base modifications mediated by
CC       the elongator complex. The elongator complex is required for multiple
CC       tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine),
CC       mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-
CC       carbamoylmethyl uridine). {ECO:0000250|UniProtKB:Q3E840}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[3Fe-4S](1+)-[protein] + Fe(2+)-[Dph3] = [3Fe-4S](0)-[protein]
CC         + Fe(3+)-[Dph3]; Xref=Rhea:RHEA:71235, Rhea:RHEA-COMP:17996,
CC         Rhea:RHEA-COMP:17997, Rhea:RHEA-COMP:18002, Rhea:RHEA-COMP:18003,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:33751,
CC         ChEBI:CHEBI:47402, ChEBI:CHEBI:83228;
CC         Evidence={ECO:0000250|UniProtKB:Q3E840};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 [3Fe-4S](0)-[protein] + 2 Fe(2+)-[Dph3] + NADH = 2 [4Fe-
CC         4S](1+)-[protein] + 2 [Dph3] + H(+) + NAD(+); Xref=Rhea:RHEA:71239,
CC         Rhea:RHEA-COMP:17997, Rhea:RHEA-COMP:17998, Rhea:RHEA-COMP:18001,
CC         Rhea:RHEA-COMP:18002, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:33723, ChEBI:CHEBI:47402, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:83228;
CC         Evidence={ECO:0000250|UniProtKB:Q3E840};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q3E840};
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC       {ECO:0000250|UniProtKB:Q3E840}.
CC   -!- SUBUNIT: Component of the 2-(3-amino-3-carboxypropyl)histidine synthase
CC       complex composed of DPH1, DPH2, DPH3 and a NADH-dependent reductase,
CC       predominantly CBR1. {ECO:0000250|UniProtKB:Q3E840}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The DPH-type metal-binding (MB) domain can also bind zinc.
CC       However, iron is the physiological binding partner as zinc binding
CC       impairs the protein electron donor function.
CC       {ECO:0000250|UniProtKB:Q3E840}.
CC   -!- SIMILARITY: Belongs to the DPH3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ESU12054.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS231665; ESU12054.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; HG970334; CEF86891.1; -; Genomic_DNA.
DR   RefSeq; XP_011324630.1; XM_011326328.1.
DR   AlphaFoldDB; Q4I9U7; -.
DR   SMR; Q4I9U7; -.
DR   STRING; 5518.FGSG_06011P0; -.
DR   EnsemblFungi; ESU12054; ESU12054; FGSG_06011.
DR   GeneID; 23553158; -.
DR   KEGG; fgr:FGSG_06011; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G19285; -.
DR   eggNOG; KOG2923; Eukaryota.
DR   HOGENOM; CLU_2197231_0_0_1; -.
DR   InParanoid; Q4I9U7; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000070720; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
DR   GO; GO:0034986; F:iron chaperone activity; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR   GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR   GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; ISS:UniProtKB.
DR   Gene3D; 3.10.660.10; -; 1.
DR   InterPro; IPR044248; DPH3/4-like.
DR   InterPro; IPR007872; DPH_MB_dom.
DR   InterPro; IPR036671; DPH_MB_sf.
DR   PANTHER; PTHR21454; PTHR21454; 1.
DR   Pfam; PF05207; zf-CSL; 1.
DR   SUPFAM; SSF144217; SSF144217; 1.
DR   PROSITE; PS51074; DPH_MB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..86
FT                   /note="Diphthamide biosynthesis protein 3"
FT                   /id="PRO_0000082633"
FT   DOMAIN          9..65
FT                   /note="DPH-type MB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         31
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
FT   BINDING         33
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
FT   BINDING         53
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
FT   BINDING         56
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
SQ   SEQUENCE   86 AA;  9394 MW;  4687EA16C5BC2F2F CRC64;
     MSDDEGISIY DEVEIEDMTF DEAMGVYQFP CPCGDKFQIT LEDLLDEQDI AVCPSCSLMI
     RVIFDLDDLP KPPTSGASGG QVPITA
 
 
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