Entry
Name
2-(3-amino-3-carboxypropyl)histidine synthase;
Dph2
Class
Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:L-histidine-[translation elongation factor 2] 2-[(3S)-3-amino-3-carboxypropyl]transferase
Reaction(IUBMB)
S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2] = S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2] [RN:
R10455 ]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:
C00019 ];
L-histidine-[translation elongation factor 2] [CPD:
C20663 ]
Product
S-methyl-5'-thioadenosine [CPD:
C00170 ];
2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2] [CPD:
C04441 ]
Comment
A [4Fe-4S] enzyme that modifies a histidine residue of the translation elongation factor 2 (EF2) via a 3-amino-3-carboxypropyl radical. The enzyme is present in archae and eukaryotes but not in eubacteria. The enzyme is a member of the 'AdoMet radical' (radical SAM) family and generates the 3-amino-3-carboxypropyl radical by an uncanonical clevage of S-adenosyl-L-methionine. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii. Part of diphthamide biosynthesis.
History
EC 2.5.1.108 created 2013
Orthology
K07561 2-(3-amino-3-carboxypropyl)histidine synthase
Genes
SRX : 107743654(dph1) 107744807
SANH : 107664954 107685060
CCAR : 109056563 109095810
CAUA : 113058909 113069522(dph1) 113114859
MASI : 127422542 127430280
SASA : 106581169(dph1) 106612930
OMY : 110503945(dph1) 110507778
ONE : 115118172 115123823(dph1) 115125626
ARUT : 117429582 117430380
LCM : 102356549 102362800(DPH1)
DSI : Dsimw501_GD12784(Dsim_GD12784)
AMER : 121600001 121601355
AALB : 109431303 109432003 115264575
APLN : 108742182 112904624
SGRE : 126326039 126354043
PPOI : 119103350 119103382
RSAN : 119400505 119400516
DPTE : 113793774 113794438 113796754
CSCU : 111617475 111639168
CBR : CBG_09207(Cbr-dph-1)
BMY : BM_BM8194(Bma-dph-1)
HRO : HELRODRAFT_113590 HELRODRAFT_83835
OSN : 115212882 115227608 115229556 115229850
SHX : MS3_00008643(DPH1_1)
CSAT : 104726793 104739420 104762325
LJA : Lj2g3v2124830.1(Lj2g3v2124830.1)
ADU : 107475020 107475029 107475034 107475126 107488450
PDUL : 117625971 117627153
HBR : 110645538 110646025 110646064 110646074 110646083
SSPL : 121780297 121782839 121783065
PSOM : 113301694 113356111
DOSA : Os02t0815600-01(Os02g0815600)
TAES : 123128959 123139707 123146122
PVIR : 120646230 120657592
SMO : SELMODRAFT_156702 SELMODRAFT_271325
NCS : NCAS_0B06320(NCAS0B06320)
NDI : NDAI_0B03620(NDAI0B03620)
TPF : TPHA_0C03300(TPHA0C03300)
TBL : TBLA_0G02400(TBLA0G02400)
TDL : TDEL_0C03900(TDEL0C03900)
KAF : KAFR_0H03400(KAFR0H03400)
KNG : KNAG_0H02110(KNAG0H02110)
CAL : CAALFM_C205840WA(CaO19.5207)
NTE : NEUTE1DRAFT83361(NEUTE1DRAFT_83361)
ANG : ANI_1_2500024(An02g04630)
PNO : SNOG_07675(SNOG_07674)
ABP : AGABI1DRAFT58324(AGABI1DRAFT_58324)
ABV : AGABI2DRAFT202335(AGABI2DRAFT_202335)
SCM : SCHCO_02576699(SCHCODRAFT_02576699)
EHI : EHI_199050(87.t00020)
PTM : GSPATT00001229001 GSPATT00002800001
SMIN : v1.2.033984.t1(symbB.v1.2.033984.t1)
MCHK : MchiMG62_21480(dph2)
HALA : Hrd1104_04445(dph2)
HARC : HARCEL1_07870(dph2)
HALQ : Hrr1229_000620(dph2)
HACB : Hbl1158_09990(dph2)
HJT : DVR14_19995(dph2) DVR14_24135(dph2)
TVO : TVG1411317(TVG1411317)
» show all
Taxonomy
Reference
Authors
Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH
Title
Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2.
Journal
Sequence
Reference
Authors
Zhang Y, Zhu X, Torelli AT, Lee M, Dzikovski B, Koralewski RM, Wang E, Freed J, Krebs C, Ealick SE, Lin H
Title
Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme.
Journal
Sequence
Reference
Authors
Zhu X, Dzikovski B, Su X, Torelli AT, Zhang Y, Ealick SE, Freed JH, Lin H
Title
Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis.
Journal
Sequence
Reference
Authors
Dong M, Horitani M, Dzikovski B, Pandelia ME, Krebs C, Freed JH, Hoffman BM, Lin H
Title
Organometallic Complex Formed by an Unconventional Radical S-Adenosylmethionine Enzyme.
Journal
Other DBs
ExPASy - ENZYME nomenclature database: 2.5.1.108