DPH2_DICDI
ID DPH2_DICDI Reviewed; 588 AA.
AC B0G132;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000305};
DE AltName: Full=Diphthamide biosynthesis protein 2;
DE AltName: Full=Diphtheria toxin resistance protein 2 {ECO:0000305};
DE AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 2 {ECO:0000305};
GN Name=dph2; ORFNames=DDB_G0295687;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Required for the first step of diphthamide biosynthesis, a
CC post-translational modification of histidine which occurs in elongation
CC factor 2 (By similarity). Dph1 and dph2 transfer a 3-amino-3-
CC carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a
CC histidine residue, the reaction is assisted by a reduction system
CC comprising dph3 and a NADH-dependent reductase (By similarity).
CC Facilitates the reduction of the catalytic iron-sulfur cluster found in
CC the dph1 subunit (By similarity). {ECO:0000250|UniProtKB:P32461}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P32461};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the
CC reduction of the catalytic iron-sulfur cluster in the dph1 subunit.
CC {ECO:0000250|UniProtKB:P32461};
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:P32461}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AAFI02000033; EDR41076.1; -; Genomic_DNA.
DR RefSeq; XP_001732995.1; XM_001732943.1.
DR AlphaFoldDB; B0G132; -.
DR SMR; B0G132; -.
DR STRING; 44689.DDB0238859; -.
DR PaxDb; B0G132; -.
DR PRIDE; B0G132; -.
DR EnsemblProtists; EDR41076; EDR41076; DDB_G0295687.
DR GeneID; 8622261; -.
DR KEGG; ddi:DDB_G0295687; -.
DR dictyBase; DDB_G0295687; dph2.
DR eggNOG; KOG2648; Eukaryota.
DR HOGENOM; CLU_015210_1_0_1; -.
DR InParanoid; B0G132; -.
DR OMA; PFNNMYD; -.
DR PhylomeDB; B0G132; -.
DR Reactome; R-DDI-5358493; Synthesis of diphthamide-EEF2.
DR UniPathway; UPA00559; -.
DR PRO; PR:B0G132; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR Gene3D; 3.40.50.11840; -; 1.
DR Gene3D; 3.40.50.11860; -; 1.
DR InterPro; IPR010014; DHP2.
DR InterPro; IPR016435; DPH1/DPH2.
DR InterPro; IPR042263; DPH1/DPH2_1.
DR InterPro; IPR042265; DPH1/DPH2_3.
DR PANTHER; PTHR10762; PTHR10762; 1.
DR PANTHER; PTHR10762:SF2; PTHR10762:SF2; 1.
DR Pfam; PF01866; Diphthamide_syn; 2.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR TIGRFAMs; TIGR00322; diphth2_R; 2.
DR TIGRFAMs; TIGR00272; DPH2; 1.
PE 3: Inferred from homology;
KW Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..588
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT subunit 2"
FT /id="PRO_0000329959"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
FT BINDING 127
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
FT BINDING 425
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
SQ SEQUENCE 588 AA; 67193 MW; 1539D868E959AE06 CRC64;
MSAAPPPSIY TESFSTSSNN TTESESINVE ETRENILSGF SFEEYFQVSE SISVIIKNNF
KKIALQLPDY LLWASSELSN KIQNSVPLEY GIKVFILGDT SYGSCCVDEV TSSHLKSDFI
IHYGHSCLSP SSKIPVQYVF GKKKNFNVDK FSIELNKLVE SKKEENFVIF YDLLYHHNRD
SIENLYKNND NIIVTNINNF NNIYLNNSFK NNKLNETQNC NNNYNNDCCG SDNNNNNNDS
GCCGGNNNNN NNNSGCCQSQ SQQQQQQNDC CQQKLNNEIN NENDNNNEEL ISGRKIEFKN
EKDIKKFNFI WIGEESLTLT NLLMNFNQQM VYRYYIDDNK LLQETLPRNK SLMRRYHISE
KCKDASIIGI VVSTLSVQKY SETIDGLKKL IIASGKKPYV FVVGRLNVPK LANFSEIDIY
VIVACHENTM VDSKDFYKPI ATPFELNLSL RNEKWTGEYI TDFGRVFPKL IKDLSFDEDD
ENKCEIPEDQ VEDDQGNIHH FSLVTGRIVI QNKNQSTLQQ QQQQQQTQQS GDLISVNNQF
KQVSLVGEHL SNKTYKGLDM RIGETPVTTA IEGMSGIPKN YNTDKNNL
