ID   DPH2_NEMVE              Reviewed;         531 AA.
AC   A7SKJ3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=v1g121715;
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6;
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
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; DS469688; EDO35768.1; -; Genomic_DNA.
DR   RefSeq; XP_001627831.1; XM_001627781.1.
DR   AlphaFoldDB; A7SKJ3; -.
DR   SMR; A7SKJ3; -.
DR   STRING; 45351.EDO35768; -.
DR   EnsemblMetazoa; EDO35768; EDO35768; NEMVEDRAFT_v1g121715.
DR   eggNOG; KOG2648; Eukaryota.
DR   HOGENOM; CLU_015210_1_0_1; -.
DR   InParanoid; A7SKJ3; -.
DR   OMA; PFNNMYD; -.
DR   OrthoDB; 750182at2759; -.
DR   PhylomeDB; A7SKJ3; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
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; -; 2.
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; 2.
DR   TIGRFAMs; TIGR00272; DPH2; 1.
PE   3: Inferred from homology;
KW   Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT   CHAIN           1..531
FT                   /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT                   subunit 2"
FT                   /id="PRO_0000329960"
FT   REGION          222..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         130
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P32461"
FT   BINDING         151
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P32461"
FT   BINDING         388
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P32461"
SQ   SEQUENCE   531 AA;  59360 MW;  5F0DF031BAE53ACE CRC64;
     MEVETTAKSY DVPASAFSES AVIDTHLDVP STKTESIERM VEVYEIERSV QVITSSGFNK
     VALQFPDSLL ADSASVARLI EQRASCKAFI LADTSYGRHP PLPANKTFLK LYNVRICFKL
     LAFLHFSSCC VDEIAAEHAD AELIIHYGQA CLSQTKRLPV LYVFGKNPIN VIECSQHFRQ
     LYPDTGIRVL VFYDVVYNHC IGALDEALSP LYPNMTISTI APEGLPSEPT SQQSSRNPQA
     SDVEGMEVNQ CNRRFGRDFT LAANSSISDY QIFYIGEQSL TLRNLMMTYN KCQFSTYDPI
     TNESRRETLN VNKALMKRYH MIQRAKDAQI VGIVVGTLGV ADYLKIIERL KKVLAIAGKK
     SYVFVMGKLN VAKLANFLEI DVFVLVSCPE NSLIDSKEFY KPVVTPYEME IACLRTQEWT
     GDYVTDFHEL LPGKSINTFW TDDNDDSPYI SLITGKMQHN YKSSAKEAGE TSTSLVQRNQ
     ETTLATQQPL TAEFLASRSW QGLQQNLGDT PVTTAVEGRR GIAAGYTDEG E