DPH2_BOVIN
ID DPH2_BOVIN Reviewed; 489 AA.
AC Q08DM2; A5D957;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) 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; BT030476; ABQ12916.1; -; mRNA.
DR EMBL; BC123671; AAI23672.1; -; mRNA.
DR RefSeq; NP_001071567.2; NM_001078099.2.
DR AlphaFoldDB; Q08DM2; -.
DR SMR; Q08DM2; -.
DR STRING; 9913.ENSBTAP00000025143; -.
DR PaxDb; Q08DM2; -.
DR GeneID; 768224; -.
DR KEGG; bta:768224; -.
DR CTD; 1802; -.
DR eggNOG; KOG2648; Eukaryota.
DR HOGENOM; CLU_015210_0_0_1; -.
DR InParanoid; Q08DM2; -.
DR OrthoDB; 750182at2759; -.
DR TreeFam; TF313832; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000009136; Unplaced.
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_0000307887"
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 CONFLICT 422
FT /note="V -> A (in Ref. 1; ABQ12916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 51795 MW; 9F6FB6AFCDC3D976 CRC64;
MESTFSSPAE AALQREAGSA GLRTSLGDLD RVYELERVVG FVRDLGCQRV ALQFPDQLLG
DAGAVAALLE EATGSKMFIL GDTAYGSCCV DVLGAEQAGA QALVHFGPAC LSPPARPLPV
AFVLGQRSVA LELCAKAFEA QNPDPTAPVV LLSEPSCAHA LEALATLLRP RYLDLLVSSP
ALPLPAGSFN PNPEPLERFG RRFPLAPGRC LEEYGAFYVG GSEAISDPDL DPDLSRLLLG
WAPGRPFSSC CPDTGRTQDE GVRAGRLRAR RRYLIERARD ARVVGLLAGT LGVARHREAL
AHLRNLTQAA GKRSYVLALG RPTPAKLANF PEVDVFVLLA CPLGTLAPQP SGSFFRPVLA
PCELEAACNP AWPPPGLAPH LTHYTDLLPG SPFHVPLPPP DSELWDAPDV SLITGDLRPP
PVWKPSDDPG CSALTPKPQL ELAESSPAAS FLSSRSWKGL QPSLGQTPVT GAVSGRRGIA
IAYEDEGNS
