ID   DPH2_XENLA              Reviewed;         478 AA.
AC   Q6DE00;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-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.
CC       {ECO:0000250|UniProtKB:P32461}.
CC   -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC077348; AAH77348.1; -; mRNA.
DR   RefSeq; NP_001086718.1; NM_001093249.1.
DR   AlphaFoldDB; Q6DE00; -.
DR   SMR; Q6DE00; -.
DR   DNASU; 446553; -.
DR   GeneID; 446553; -.
DR   KEGG; xla:446553; -.
DR   CTD; 446553; -.
DR   Xenbase; XB-GENE-980248; dph2.L.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 446553; Expressed in ovary and 19 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   2: Evidence at transcript level;
KW   Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT   CHAIN           1..478
FT                   /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT                   subunit 2"
FT                   /id="PRO_0000307895"
FT   BINDING         93
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P32461"
FT   BINDING         114
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P32461"
FT   BINDING         331
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P32461"
SQ   SEQUENCE   478 AA;  52686 MW;  2AC419EE83916377 CRC64;
     MAAALFSSNG EEAIGRNIDI GQVDIQSSPE KDLGEFYEIE KTVEFIQRNA AQKVALQFPD
     DLLLDSVKVA RKLEEATGAK TYILGDTSYG SCCVDEVAAE HVKANVLVHY GRACLSPCCR
     LPVSYVFGRK AVNMDLCAEA FLSHYRDTES HVVVLSDVVY DHALGELAKR IRSAYPNVIF
     SKLTSCGETA SPDEIVKFGR RFSPDLRLWP ESYGIFYVGG EGSTLNNLML TWPRCSFFSF
     NPFTGEGRTE GLHVNRALMI RFYLIERARD AHVFGILVGT LGVSDYLSAL KHLKNIIHLA
     GKKSYMFSVG KLNPAKLANF PEIDVFVLVA CPENSLLDSS EFYKPVVTPD EMEIACNPAR
     EWHGYCITNF RELLPGGSAY VEFPETDPSD AHHTDVSLIT GNLRSSHLTV AETLEKDSDT
     SLVQRNSKTA LAQMSSAASY LASRSWQGLD KALGQTPVVK AVEGRKGIAI AYEDEICS