DPH2_CHICK
ID DPH2_CHICK Reviewed; 477 AA.
AC Q5ZKI2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=RCJMB04_10j16;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720102; CAG31761.1; -; mRNA.
DR RefSeq; NP_001006538.1; NM_001006538.1.
DR AlphaFoldDB; Q5ZKI2; -.
DR SMR; Q5ZKI2; -.
DR STRING; 9031.ENSGALP00000016389; -.
DR PaxDb; Q5ZKI2; -.
DR GeneID; 424574; -.
DR KEGG; gga:424574; -.
DR CTD; 1802; -.
DR VEuPathDB; HostDB:geneid_424574; -.
DR eggNOG; KOG2648; Eukaryota.
DR InParanoid; Q5ZKI2; -.
DR OrthoDB; 750182at2759; -.
DR PhylomeDB; Q5ZKI2; -.
DR UniPathway; UPA00559; -.
DR PRO; PR:Q5ZKI2; -.
DR Proteomes; UP000000539; 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 Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..477
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT subunit 2"
FT /id="PRO_0000307893"
FT BINDING 88
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
FT BINDING 328
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
SQ SEQUENCE 477 AA; 52163 MW; 0E77B85BE4EAC81C CRC64;
MAAAFSSDGE AVLRRTLDPA AAAPRGDKDE FYEVDRAAAF VRDGGFRKVA LQFPDALLAD
AAAVAARMEE VTGAEMYVLG DTTYGSCCVD EVAAEHVSAG AVVHYGPACL SPCRKLPVLH
VFGRQPLDVG RCAEVFRELY PERQSRVVVL SDVVYAHAMG ELEKQLCHEY PNIIFSEVVC
GDAPSPTLPG EVRQFGRRFH MEAAEELQDC SMFYVGAEGL ALTSFMLTWN RFPFSSFDPA
TGHGRRETLN VNRALMRRLY LVERARDAHV VGILVGTLGV AGYLDVLEHL HQLVRRAGKR
SYTLSVGKPN PAKLANFLEV DIFVLVACAQ NSLLDSSEFY RPIVTPYELE LACNPAREWT
GNYLTDFRDL LPGACAHIEL PPAVPAAEAI PDVSLITGEM RATHLCDPLA PQPPSSTTLA
CRDQTRALAE MSPAATFLES RSWRGLEQQL GKTAVSKAVQ GRRGIAIAYE DEGREQS
