DPH2_CRIGR
ID DPH2_CRIGR Reviewed; 489 AA.
AC Q002B5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 56.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH DPH1.
RX PubMed=21203470; DOI=10.1371/journal.pone.0015753;
RA Roy V., Ghani K., Caruso M.;
RT "A dominant-negative approach that prevents diphthamide formation confers
RT resistance to Pseudomonas exotoxin A and diphtheria toxin.";
RL PLoS ONE 5:e15753-e15753(2010).
CC -!- FUNCTION: Required for the first step of diphthamide biosynthesis, a
CC post-translational modification of histidine which occurs in elongation
CC factor 2 (PubMed:21203470). 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 ECO:0000269|PubMed:21203470}.
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 (PubMed:21203470).
CC {ECO:0000250|UniProtKB:P32461, ECO:0000269|PubMed:21203470}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ981502; ABI97860.1; -; mRNA.
DR RefSeq; NP_001233722.1; NM_001246793.1.
DR AlphaFoldDB; Q002B5; -.
DR SMR; Q002B5; -.
DR STRING; 10029.NP_001233722.1; -.
DR Ensembl; ENSCGRT00001002960; ENSCGRP00001002285; ENSCGRG00001002429.
DR GeneID; 100689365; -.
DR KEGG; cge:100689365; -.
DR CTD; 1802; -.
DR eggNOG; KOG2648; Eukaryota.
DR GeneTree; ENSGT00940000153694; -.
DR OMA; PFNNMYD; -.
DR OrthoDB; 750182at2759; -.
DR UniPathway; UPA00559; -.
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; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR TIGRFAMs; TIGR00322; diphth2_R; 1.
DR TIGRFAMs; TIGR00272; DPH2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Iron; Iron-sulfur; Metal-binding; Phosphoprotein.
FT CHAIN 1..489
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT subunit 2"
FT /id="PRO_0000307888"
FT REGION 398..489
FT /note="Required for function"
FT /evidence="ECO:0000269|PubMed:21203470"
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; 52072 MW; C3107E5D7558E925 CRC64;
MESTFSSPAE AALQREAGVP GLFTPPEDLD RVYELERVTK FVCDLGCQRV ALQFPDQLLG
DAGAVAVRLE EVTGSKMFIL GDTAYGSCCV DVLGAEQAGA EALVHFGPAC LSPPASLLPI
TFVLGQRSVA LELCAKAFEA RNPDPTAPVV LLSEPACAHA LEALATLLRP KYQDLLISSP
ALPLPVGSPS SQPEPLERFG RRFPLSPGRC LEEYGAFYVG GSQASSDPVL DPDLSRLLLG
WTPGRPFISC CPDTGQTQDQ GVQAGRLRAR RLYLIERARD AHVVGLLAGT LGVAQHREAL
AHLRKLTEAA GKRSYVLALG RPTPAKLANF PEMDIFVLLA CPLGALAPQP SGGFFRPILT
PCELEAACNP AWPPPGLAPH LTHYAELLPG SPFYVPLPPP ESELWDTPDV SLISGDLRPP
PSWKSSSDTG CSALTPRPQL ELAESSPAAS FLSSRSWQGL EPRLGQTPVK EAVQGRRGIA
IAYEDEGSG
