ID W8NWE0_9EURY Unreviewed; 344 AA.
AC W8NWE0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase {ECO:0000256|ARBA:ARBA00012221, ECO:0000256|PIRNR:PIRNR004967};
DE EC=2.5.1.108 {ECO:0000256|ARBA:ARBA00012221, ECO:0000256|PIRNR:PIRNR004967};
GN ORFNames=BD01_2020 {ECO:0000313|EMBL:AHL23618.1};
OS Thermococcus nautili.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=195522 {ECO:0000313|EMBL:AHL23618.1, ECO:0000313|Proteomes:UP000019434};
RN [1] {ECO:0000313|EMBL:AHL23618.1, ECO:0000313|Proteomes:UP000019434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30-1 {ECO:0000313|EMBL:AHL23618.1,
RC ECO:0000313|Proteomes:UP000019434};
RA Oberto J., Gaudin M., Cossu M., Gorlas A., Slesarev A., Marguet E.,
RA Forterre P.;
RT "Genome Sequence of an Hyperthermophilic Archaeon, Thermococcus nautili 30-
RT 1, producing viral vesicles.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|PIRNR:PIRNR004967}.
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:0000256|ARBA:ARBA00001323,
CC ECO:0000256|PIRNR:PIRNR004967};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|PIRNR:PIRNR004967};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005156, ECO:0000256|PIRNR:PIRNR004967}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family.
CC {ECO:0000256|PIRNR:PIRNR004967}.
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DR EMBL; CP007264; AHL23618.1; -; Genomic_DNA.
DR RefSeq; WP_042692505.1; NZ_CP007264.1.
DR AlphaFoldDB; W8NWE0; -.
DR STRING; 195522.BD01_2020; -.
DR GeneID; 24959253; -.
DR KEGG; tnu:BD01_2020; -.
DR eggNOG; arCOG04112; Archaea.
DR HOGENOM; CLU_037146_0_0_2; -.
DR OrthoDB; 314at2157; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000019434; Chromosome.
DR GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.11840; Diphthamide synthesis DPH1/DPH2 domain 1; 1.
DR Gene3D; 3.40.50.11850; Diphthamide synthesis DPH1/DPH2 domain 2; 1.
DR Gene3D; 3.40.50.11860; Diphthamide synthesis DPH1/DPH2 domain 3; 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 InterPro; IPR036237; Xyl_isomerase-like_sf.
DR NCBIfam; TIGR03682; arCOG04112; 1.
DR NCBIfam; TIGR00322; diphth2_R; 1.
DR PANTHER; PTHR10762:SF1; 2-(3-AMINO-3-CARBOXYPROPYL)HISTIDINE SYNTHASE SUBUNIT 1; 1.
DR PANTHER; PTHR10762; DIPHTHAMIDE BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF01866; Diphthamide_syn; 1.
DR PIRSF; PIRSF004967; DPH1; 1.
DR SFLD; SFLDG01121; Diphthamide_biosynthesis; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR SUPFAM; SSF51658; Xylose isomerase-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|PIRNR:PIRNR004967};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR004967};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRNR:PIRNR004967};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR004967};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR004967};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR004967}.
SQ SEQUENCE 344 AA; 38561 MW; 60A40CDFE58ED129 CRC64;
MHEVPHGEIL KELRKLGARC VLIQSPEGLR RETEELARFL EENGLAVILH GEINYGACDP
ADSDAKRLGC DALIHLGHSY MRLNLEVPTI FVPAFAKVEL VPALEKNIEE IRKLGRRIAL
VTTAQHVHRL DEAREFLEEN GFEVLIGKGD SRVSWPGQVL GCNFSSAKVE ADGVLFIGAG
YFHPLGVALA VKKPTLAINP YSGDALWMDE EAERLVRKRW AQIAKAMDAK SFGVVVSTKK
GQLRLAEARR VVELLREHGR EARLIAMDHI SYPKLEGFPF DAYVVVACPR VPIDDYENWR
KPVLTPREVE LLLGLREDYE FDEIPGVERR EDEPLGIAVH GVRG
//
