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DPH3_DROME
ID   DPH3_DROME              Reviewed;          86 AA.
AC   Q9VGQ9; Q4QPS1;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Diphthamide biosynthesis protein 3 {ECO:0000305};
GN   Name=Dph3 {ECO:0000305}; ORFNames=CG14701;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 Dph3 and a NADH-dependent
CC       reductase. Acts as an electron donor to reduce the Fe-S cluster in
CC       Dph1-Dph2 keeping the [4Fe-4S] clusters in the active and reduced
CC       state. Restores iron to Dph1-Dph2 iron-sulfur clusters which have
CC       degraded from [4Fe-4S] to [3Fe-4S] by donating an iron atom to reform
CC       [4Fe-4S] clusters, in a manner dependent on the presence of elongation
CC       factor 2 and SAM. Associates with the elongator complex and is required
CC       for tRNA Wobble base modifications mediated by the elongator complex.
CC       The elongator complex is required for multiple tRNA modifications,
CC       including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s 2U (5-
CC       methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl
CC       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:0000305}.
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       {ECO:0000250|UniProtKB:Q3E840}.
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; AE014297; AAF54617.1; -; Genomic_DNA.
DR   EMBL; BT023695; AAY85095.1; -; mRNA.
DR   RefSeq; NP_650057.1; NM_141800.2.
DR   AlphaFoldDB; Q9VGQ9; -.
DR   SMR; Q9VGQ9; -.
DR   STRING; 7227.FBpp0081829; -.
DR   PaxDb; Q9VGQ9; -.
DR   DNASU; 41352; -.
DR   EnsemblMetazoa; FBtr0082353; FBpp0081829; FBgn0037883.
DR   GeneID; 41352; -.
DR   KEGG; dme:Dmel_CG14701; -.
DR   UCSC; CG14701-RA; d. melanogaster.
DR   FlyBase; FBgn0037883; CG14701.
DR   VEuPathDB; VectorBase:FBgn0037883; -.
DR   eggNOG; KOG2923; Eukaryota.
DR   GeneTree; ENSGT00940000171548; -.
DR   HOGENOM; CLU_155991_3_0_1; -.
DR   InParanoid; Q9VGQ9; -.
DR   OMA; IYDPDMF; -.
DR   OrthoDB; 1634836at2759; -.
DR   PhylomeDB; Q9VGQ9; -.
DR   Reactome; R-DME-5358493; Synthesis of diphthamide-EEF2.
DR   UniPathway; UPA00559; -.
DR   BioGRID-ORCS; 41352; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 41352; -.
DR   PRO; PR:Q9VGQ9; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0037883; Expressed in adult Malpighian tubule (Drosophila) and 28 other tissues.
DR   Genevisible; Q9VGQ9; DM.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR   GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
DR   GO; GO:0034986; F:iron chaperone activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; ISS:FlyBase.
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   GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
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   Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..86
FT                   /note="Diphthamide biosynthesis protein 3"
FT                   /id="PRO_0000082625"
FT   DOMAIN          4..60
FT                   /note="DPH-type MB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         26
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
FT   BINDING         28
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
FT   BINDING         48
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
FT   BINDING         51
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
SQ   SEQUENCE   86 AA;  10115 MW;  F56639C0F9B1FF3D CRC64;
     MSIYHDEVEI EDFEYDEEEE MYYYPCPCGD RFQISKEELI EGEEVATCPS CSLVIKVIYD
     PEMFKAEEDE ESALNEKLGD LKLEKN
 
 
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