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DPH3_KLULA
ID   DPH3_KLULA              Reviewed;          82 AA.
AC   Q6CMG4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Diphthamide biosynthesis protein 3;
GN   Name=DPH3; OrderedLocusNames=KLLA0E20537g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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}.
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DR   EMBL; CR382125; CAG99962.1; -; Genomic_DNA.
DR   RefSeq; XP_454875.1; XM_454875.1.
DR   AlphaFoldDB; Q6CMG4; -.
DR   SMR; Q6CMG4; -.
DR   STRING; 28985.XP_454875.1; -.
DR   EnsemblFungi; CAG99962; CAG99962; KLLA0_E20439g.
DR   GeneID; 2894676; -.
DR   KEGG; kla:KLLA0_E20439g; -.
DR   eggNOG; KOG2923; Eukaryota.
DR   HOGENOM; CLU_155991_4_1_1; -.
DR   InParanoid; Q6CMG4; -.
DR   OMA; LFTYPCP; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000000598; Chromosome E.
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:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:EnsemblFungi.
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..82
FT                   /note="Diphthamide biosynthesis protein 3"
FT                   /id="PRO_0000082634"
FT   DOMAIN          3..59
FT                   /note="DPH-type MB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         25
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
FT   BINDING         27
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
FT   BINDING         47
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
FT   BINDING         50
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
SQ   SEQUENCE   82 AA;  9285 MW;  A6763CD11CBF678A CRC64;
     MSTYDEVEIE DMTFDPDTQI FTYPCPCGDR FQISIDDMYD GEDIAVCPSC SLMIQVVFDK
     EDLVEYYVEA NLEPPGKIAV AV
 
 
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