DPH2_PONAB
ID DPH2_PONAB Reviewed; 489 AA.
AC Q5RE82;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 (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; CR857652; CAH89925.1; -; mRNA.
DR RefSeq; NP_001124904.1; NM_001131432.1.
DR AlphaFoldDB; Q5RE82; -.
DR SMR; Q5RE82; -.
DR STRING; 9601.ENSPPYP00000001667; -.
DR Ensembl; ENSPPYT00000001723; ENSPPYP00000001667; ENSPPYG00000001439.
DR GeneID; 100171771; -.
DR KEGG; pon:100171771; -.
DR CTD; 1802; -.
DR eggNOG; KOG2648; Eukaryota.
DR GeneTree; ENSGT00940000153694; -.
DR InParanoid; Q5RE82; -.
DR OrthoDB; 750182at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000001595; Chromosome 1.
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 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_0000307891"
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; 52201 MW; CE09F1948A0CFBE2 CRC64;
MESMFSSPAE AALQREAGMP GLLTPLPDLD RVYELERVAG FVRDLGCERV ALQFPDQLLG
DAVAVAARLE ETTGSKMFIL GDTAYGSCCV DVLGAEQAGA QAVIHFGPAC LSPPARPLPV
TFVLCRRSVA LELCVKAFEA QNPDPKAPVV LLSEPACAHA LEALATLLRP RYLDLLVSSP
AFPLPVGSLS PEPKPLERFG RRFPLAPGRR LEEYGAFYVG GSKASPDPDL DPDLSRLLLG
WAPGQPFSSC CPDTGKTQDE GARAGRLRAR RRYLVERARD ARVVGLLVGT LGVAQHREAL
AHLRNLTQAA GKRSYVLALG RPTPAKLANF PEVDVFVLLA CPLGALAPQL SGSFFQPILA
PCELEAACNP AWPPPGLAPH LTHYADLLPG SPFHVPLPPS ESELWETPDV SLITGDLRPP
PAWKSSNDHG SLALTPRPQL ELAESSPAAS FLSSRSWQGL EPRLGQTPVT EAVSGRRGIA
IAYEDEGSG
