DPH2_METJA
ID DPH2_METJA Reviewed; 340 AA.
AC Q57907;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase;
DE EC=2.5.1.108 {ECO:0000250|UniProtKB:O58832};
DE AltName: Full=Diphthamide biosynthesis protein Dph2;
DE AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase;
GN Name=dph2; OrderedLocusNames=MJ0483;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Catalyzes the first step of diphthamide biosynthesis, i.e.
CC the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-
CC methionine (SAM) to the C2 position of the imidazole ring of the target
CC histidine residue in translation elongation factor 2 (EF-2).
CC {ECO:0000250|UniProtKB:O58832}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[translation elongation factor 2] + S-adenosyl-L-
CC methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation
CC elongation factor 2] + H(+) + S-methyl-5'-thioadenosine;
CC Xref=Rhea:RHEA:36783, Rhea:RHEA-COMP:9748, Rhea:RHEA-COMP:9749,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:73995; EC=2.5.1.108;
CC Evidence={ECO:0000250|UniProtKB:O58832};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:O58832};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:O58832};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O58832}.
CC -!- MISCELLANEOUS: Unlike the enzymes in the radical SAM superfamily, Dph2
CC does not form the canonical 5'-deoxyadenosyl radical. Instead, it
CC breaks the C(gamma)-S bond of SAM and generates a 3-amino-3-
CC carboxypropyl radical intermediate. {ECO:0000250|UniProtKB:O58832}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. {ECO:0000305}.
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DR EMBL; L77117; AAB98474.1; -; Genomic_DNA.
DR PIR; C64360; C64360.
DR AlphaFoldDB; Q57907; -.
DR SMR; Q57907; -.
DR STRING; 243232.MJ_0483; -.
DR PRIDE; Q57907; -.
DR EnsemblBacteria; AAB98474; AAB98474; MJ_0483.
DR KEGG; mja:MJ_0483; -.
DR eggNOG; arCOG04112; Archaea.
DR HOGENOM; CLU_037146_0_0_2; -.
DR InParanoid; Q57907; -.
DR OMA; PGQVLGC; -.
DR PhylomeDB; Q57907; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000000805; Chromosome.
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; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IBA:GO_Central.
DR Gene3D; 3.40.50.11840; -; 1.
DR Gene3D; 3.40.50.11850; -; 1.
DR Gene3D; 3.40.50.11860; -; 1.
DR InterPro; IPR016435; DPH1/DPH2.
DR InterPro; IPR042263; DPH1/DPH2_1.
DR InterPro; IPR042264; DPH1/DPH2_2.
DR InterPro; IPR042265; DPH1/DPH2_3.
DR InterPro; IPR035435; DPH1/DPH2_euk_archaea.
DR InterPro; IPR022428; Dph2_arc.
DR PANTHER; PTHR10762; PTHR10762; 1.
DR Pfam; PF01866; Diphthamide_syn; 2.
DR PIRSF; PIRSF004967; DPH1; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR TIGRFAMs; TIGR03682; arCOG04112; 1.
DR TIGRFAMs; TIGR00322; diphth2_R; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..340
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase"
FT /id="PRO_0000106891"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 40014 MW; 9BBFA6B67179F392 CRC64;
MLFKTIFYQK LQKKVTTLFN LETERVIREI ENLNKNNPKV IFQAPEGLKL KVEKEIEKIK
QYFKQKNINI EIYLWGNTCF GACDLIDNHV KNLNVDLIIH YGHEKLSYAN PEIKTLFIPA
YHIFNKDEEE KILNDIKNFI EKHKSGGKKV AIATTIQYKK LLKDFNPSII LGCRGEVKEG
DVILFVGTGR FHPLMIAYKY QKEVFIYNPL SKCFDKISEE EINKFIKKRI LAISKLLLNK
PKKVGVVLST KKGQCRKRVF DEIIKLLEEN DVNYLPILVD NISPDILFYD VDCYIIVACP
RIVLDDYILY KKPIYTPEEF KLFLKNSFKY KFDEIKEDDF
