DPH2_DANRE
ID DPH2_DANRE Reviewed; 498 AA.
AC A4QN59;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=zgc:162269;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) 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.
CC {ECO:0000250|UniProtKB:P32461}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC134939; AAI34940.1; -; mRNA.
DR RefSeq; NP_001082866.1; NM_001089397.1.
DR AlphaFoldDB; A4QN59; -.
DR SMR; A4QN59; -.
DR STRING; 7955.ENSDARP00000112114; -.
DR PaxDb; A4QN59; -.
DR PeptideAtlas; A4QN59; -.
DR Ensembl; ENSDART00000114076; ENSDARP00000097722; ENSDARG00000078077.
DR GeneID; 562538; -.
DR KEGG; dre:562538; -.
DR CTD; 1802; -.
DR ZFIN; ZDB-GENE-030219-100; dph2.
DR eggNOG; KOG2648; Eukaryota.
DR GeneTree; ENSGT00940000153694; -.
DR HOGENOM; CLU_015210_0_0_1; -.
DR InParanoid; A4QN59; -.
DR OMA; PFNNMYD; -.
DR OrthoDB; 750182at2759; -.
DR PhylomeDB; A4QN59; -.
DR TreeFam; TF313832; -.
DR Reactome; R-DRE-5358493; Synthesis of diphthamide-EEF2.
DR UniPathway; UPA00559; -.
DR PRO; PR:A4QN59; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000078077; Expressed in granulocyte and 27 other tissues.
DR ExpressionAtlas; A4QN59; baseline and differential.
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 Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..498
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT subunit 2"
FT /id="PRO_0000307894"
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"
SQ SEQUENCE 498 AA; 55152 MW; 8E9F723AA67AF896 CRC64;
MTDAFSSSSE AVLQRSVTST HSFHPSGDLL LLYQTPETCR FITSNHFKKV ALQFPDELLP
DAVRVSAEIE DKTKAKTYIL GDTSYGSCCV DEVAAEHVGA DCIVHYGSSC LSPCRRLPLL
YVFGKRPIDV HQCASSFKEL YPNLQSHIIV LFDVTYSHAI DDLRTLLCDV YPNVVVSRLK
TDHSCGAELI QDSCVDLQSN DDGVIFKFGR QFRIKEGQTV NDYSIFYIGQ EGLTLTNFMM
SWNNCVFSSF NPETSTGRVE SVQINKALMK RYYAIERAKD ASVVGILVGT LGVANYLIII
EQLKDTIQRA GKKSYMFAMG KINVPKLANF LEIDIYVLVA CPENSLLDSS EFYRPVVTPF
EMELACNKHR EWTGEYVTDF RELLPGGSSH VGFPEPSQSA TEEETTDVSL ITGALRSCST
NSSEMMHNSE TSSLVLRNQT LTVANTNAAA SFLAGRSWQG LEPKLGQTPV VKAVKGQRGI
AIAYEEEGNE DASTQQKL
