ID K6TWK7_9EURY Unreviewed; 329 AA.
AC K6TWK7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=B655_2059 {ECO:0000313|EMBL:EKQ51946.1};
OS Methanobacterium sp. Maddingley MBC34.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=1220534 {ECO:0000313|EMBL:EKQ51946.1, ECO:0000313|Proteomes:UP000001147};
RN [1] {ECO:0000313|EMBL:EKQ51946.1, ECO:0000313|Proteomes:UP000001147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34 {ECO:0000313|Proteomes:UP000001147};
RX PubMed=23405289;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Midgley D.J.,
RA Hendry P.;
RT "Draft Genome Sequence of Methanobacterium sp. Maddingley, Reconstructed
RT from Metagenomic Sequencing of a Methanogenic Microbial Consortium Enriched
RT from Coal-Seam Gas Formation Water.";
RL Genome Announc. 1:E00082-12(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKQ51946.1}.
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DR EMBL; AMGN01000054; EKQ51946.1; -; Genomic_DNA.
DR AlphaFoldDB; K6TWK7; -.
DR STRING; 1220534.B655_2059; -.
DR PATRIC; fig|1220534.3.peg.2040; -.
DR eggNOG; arCOG04112; Archaea.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000001147; Unassembled WGS sequence.
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 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 329 AA; 37449 MW; 1A3B85362900288F CRC64;
MTNYQFKVEQ ILDKIRETGA KIVGLQFPEG LKVHATELAR RIENETGVMV LISGDPCYGA
CDLSDMEMNG MVDLLVHFGH TPLPIDYKVP TLFVEAYYQL ESMEIFKEAV EHLEGKEKIG
LVTTTQHLHL LEDVAHFLEE NGKEVLMKDG AGTLKGQVLG CNFSSVQDLP VDAYLYLGSG
NFHPLGIKLS TQKPVVIADP YLNQVRDIDE FTDRILRIRF ARITRASEAK KFGILISSKE
GQCRWELAKD LKKMIYKKGR EAYLILLDEI NPPSLLPYMD LDAFIVTACP RIAIDDSKMY
EKPLLTPQEL EIVLGLREWE DYQMDEIKY
//