ID H8I9T5_METCZ Unreviewed; 316 AA.
AC H8I9T5;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 Name=dph2 {ECO:0000313|EMBL:AFD00536.1};
GN OrderedLocusNames=Mtc_1792 {ECO:0000313|EMBL:AFD00536.1};
OS Methanocella conradii (strain DSM 24694 / JCM 17849 / CGMCC 1.5162 /
OS HZ254).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=1041930 {ECO:0000313|EMBL:AFD00536.1, ECO:0000313|Proteomes:UP000005233};
RN [1] {ECO:0000313|EMBL:AFD00536.1, ECO:0000313|Proteomes:UP000005233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24694 / JCM 17849 / CGMCC 1.5162 / HZ254
RC {ECO:0000313|Proteomes:UP000005233};
RX PubMed=22493204; DOI=10.1128/JB.00207-12;
RA Lu Z., Lu Y.;
RT "Complete genome sequence of a thermophilic methanogen, Methanocella
RT conradii HZ254, isolated from Chinese rice field soil.";
RL J. Bacteriol. 194:2398-2399(2012).
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; CP003243; AFD00536.1; -; Genomic_DNA.
DR RefSeq; WP_014406367.1; NC_017034.1.
DR AlphaFoldDB; H8I9T5; -.
DR STRING; 1041930.Mtc_1792; -.
DR GeneID; 11971938; -.
DR KEGG; mez:Mtc_1792; -.
DR eggNOG; arCOG04112; Archaea.
DR HOGENOM; CLU_037146_0_0_2; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000005233; 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 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000005233};
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 316 AA; 34985 MW; 11259F59B35ACEF1 CRC64;
MMFDVPKILD IIKTRNAKTV GFQFPEGLKR QGPALAKEVE EKSGALVIVS GDPCYGACDI
DEGLLGIVDV LFHFGHSRMM DDERIVFMEY YHDVDVERAV INALPLLGRK VGVTTTVQHI
HKLDEIARTL KNADREPIIA NGDSRVVYPG QVLGCNFSAV PEGVDSILFV GTGNFHPVGM
RLARKLPVVA ADPFTGEARL VDVEKMMRQR YAVMAKAMDA KKWGIIVGMK PGQRRMELAK
RIKGLAGDAV LISIREITPD RLQSFKVDAF VSTACPRIAI DDAGMFPAPV LTPIEFEMLK
GKRKWEDMAF DEIKGD
//
