DPH2_CAEEL
ID DPH2_CAEEL Reviewed; 476 AA.
AC Q09454; F5GU80;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 129.
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=dph-2; ORFNames=C09G5.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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). Dph-1 and dph-2 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 dph-3 and a NADH-dependent reductase (By similarity).
CC Facilitates the reduction of the catalytic iron-sulfur cluster found in
CC the dph-1 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 dph-1 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 dph-1, dph-2, dph-3 and a NADH-dependent reductase.
CC {ECO:0000250|UniProtKB:P32461}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q09454-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q09454-2; Sequence=VSP_044038;
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z46791; CAA86761.1; -; Genomic_DNA.
DR EMBL; Z46791; CCA65532.1; -; Genomic_DNA.
DR PIR; T19146; T19146.
DR RefSeq; NP_001254257.1; NM_001267328.1. [Q09454-1]
DR RefSeq; NP_001254258.1; NM_001267329.1. [Q09454-2]
DR AlphaFoldDB; Q09454; -.
DR SMR; Q09454; -.
DR BioGRID; 39963; 6.
DR IntAct; Q09454; 1.
DR STRING; 6239.C09G5.2a; -.
DR EPD; Q09454; -.
DR PaxDb; Q09454; -.
DR PeptideAtlas; Q09454; -.
DR PRIDE; Q09454; -.
DR EnsemblMetazoa; C09G5.2a.1; C09G5.2a.1; WBGene00007488. [Q09454-1]
DR EnsemblMetazoa; C09G5.2b.1; C09G5.2b.1; WBGene00007488. [Q09454-2]
DR GeneID; 174649; -.
DR KEGG; cel:CELE_C09G5.2; -.
DR UCSC; C09G5.2; c. elegans. [Q09454-1]
DR CTD; 174649; -.
DR WormBase; C09G5.2a; CE15608; WBGene00007488; dph-2. [Q09454-1]
DR WormBase; C09G5.2b; CE45960; WBGene00007488; dph-2. [Q09454-2]
DR eggNOG; KOG2648; Eukaryota.
DR GeneTree; ENSGT00940000153694; -.
DR HOGENOM; CLU_015210_1_0_1; -.
DR InParanoid; Q09454; -.
DR OMA; VDSREFW; -.
DR OrthoDB; 750182at2759; -.
DR PhylomeDB; Q09454; -.
DR Reactome; R-CEL-5358493; Synthesis of diphthamide-EEF2.
DR UniPathway; UPA00559; -.
DR PRO; PR:Q09454; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00007488; Expressed in germ line (C elegans) and 4 other tissues.
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 3: Inferred from homology;
KW Alternative splicing; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..476
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT subunit 2"
FT /id="PRO_0000083395"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
FT BINDING 123
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
FT BINDING 347
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
FT VAR_SEQ 1..307
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_044038"
SQ SEQUENCE 476 AA; 52955 MW; FCC54BBA611E10D9 CRC64;
MTESAPSAFF TTSTPADHVH EEESSNTGYF ENLPENDIHS FFEIDATSEW IKQGNHQRIA
LQFPDSLLPY SEKVTKLIES RFRSESAKKT FVLADTSYRS CCVDEVAAAH ADCTALVHFG
EACHSAPTDK IDVKYVLGSM PIFIDQFRME FQNVADQLTA EHIVLLMDSC FSHEQEKVAA
VIKEVLPGNR HVECSLLPSE DVLKQNRQNI YLGREIPSCL RNNQPTDLIF CGFPNSPLLP
IWLLSYPSCS TVSHFNPINK TIQHESTRSS RLLRKRLFLV EKLKDADTVG LVVGSVGVDK
HREAVKRMRE MCKKAGKKIY VISVGKINVP KLSNFSTDID VFVLLSCPFG VVLDSSDYFR
PVVSYFEAEI ALNPAKTWAA DFGWSAEFAA FLEDKIETEV PDDKAAGDFS LISGKVRVQK
TEEEKNGDGP SSVAIYNPGY CNDRTWKGLN DGVSTAEDST KMGEGRSGIA QGYSGK
