DPH2_RAT
ID DPH2_RAT Reviewed; 489 AA.
AC Q568Y2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(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 (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 (By
CC similarity). Interacts with DPH1 (By similarity).
CC {ECO:0000250|UniProtKB:P32461, ECO:0000250|UniProtKB:Q9CR25}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC092656; AAH92656.1; -; mRNA.
DR RefSeq; NP_001015007.1; NM_001015007.1.
DR AlphaFoldDB; Q568Y2; -.
DR SMR; Q568Y2; -.
DR STRING; 10116.ENSRNOP00000026739; -.
DR jPOST; Q568Y2; -.
DR PaxDb; Q568Y2; -.
DR Ensembl; ENSRNOT00000026739; ENSRNOP00000026739; ENSRNOG00000019735.
DR GeneID; 298452; -.
DR KEGG; rno:298452; -.
DR UCSC; RGD:1304634; rat.
DR CTD; 1802; -.
DR RGD; 1304634; Dph2.
DR eggNOG; KOG2648; Eukaryota.
DR GeneTree; ENSGT00940000153694; -.
DR HOGENOM; CLU_015210_0_0_1; -.
DR InParanoid; Q568Y2; -.
DR OMA; PFNNMYD; -.
DR OrthoDB; 750182at2759; -.
DR PhylomeDB; Q568Y2; -.
DR TreeFam; TF313832; -.
DR Reactome; R-RNO-5358493; Synthesis of diphthamide-EEF2.
DR UniPathway; UPA00559; -.
DR PRO; PR:Q568Y2; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000019735; Expressed in thymus and 19 other tissues.
DR Genevisible; Q568Y2; RN.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; ISO:RGD.
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; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR TIGRFAMs; TIGR00322; diphth2_R; 1.
DR TIGRFAMs; TIGR00272; DPH2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Iron; Iron-sulfur; Metal-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..489
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT subunit 2"
FT /id="PRO_0000307892"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
FT BINDING 110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
FT BINDING 341
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQC3"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQC3"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQC3"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQC3"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQC3"
FT MOD_RES 467
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQC3"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQC3"
SQ SEQUENCE 489 AA; 52325 MW; 8C8F0F4720E9C14F CRC64;
MESTFSSPAE AALQREAGVP GQFTPPEDLD RVYELERVTR FICDLGCQRV ALQFPDQLLG
DAGAVAARLE EVTGSKMFIL GDTAYGSCCV DVLGAEQAGA QALVHFGPAC LSPPASLLPI
TFVLGRRPVA LELCAKAFEA QNPDPTALVV LLSEPACAHA LEPLATLLRP KYQDLLISSP
ALPLPVGSLS SQPESLERFG RRFPLNPGRS LEEYGAFYVG ASQASSDPNL DPDLSRLLLG
WTPGRPFFSC CPDTGQTQDQ GAKAGRLRAR RLYLVERARD ARVVGLLVGT LGVAQHLEAL
AHLRKLTEAA GKRSYVLALG KPTPAKLANF PEMDVFVLLA CPLGALTLQP SGGFFRPILT
PCELEAACNP AWPPPGLAPH LTHYAELLPG SPFHVPLPPP ESELWDTPDV SLISGELRPP
PPWKSSDDTK CSALTPRPQL ELAESSPAAS FLSSRSWQGL EPRLGQTPVK EAVQGRRGIA
IAYEDEGSS
