Sequence of DPH2_PYRHO
EC Number:2.5.1.108
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
2-(3-amino-3-carboxypropyl)histidine synthase
O58832
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
342
38464
Reaction
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]
Other sequences found for EC No. 2.5.1.108
General information:
Sequence
show sequence in normal format
>O58832|2-(3-amino-3-carboxypropyl)histidine synthase|EC 2.5.1.108|Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)|Swiss-Prot
MLHEIPKSEILKELKRIGAKRVLIQSPEGLRREAEELAGFLEENNIEVFLHGEINYGACD
PADREAKLVGCDALIHLGHSYMKLPLEVPTIFVPAFARVSVVEALKENIGEIKKLGRKII
VTTTAQHIHQLKEAKEFLESEGFEVSIGRGDSRISWPGQVLGCNYSVAKVRGEGILFIGS
GIFHPLGLAVATRKKVLAIDPYTKAFSWIDPERFIRKRWAQIAKAMDAKKFGVIVSIKKG
QLRLAEAKRIVKLLKKHGREARLIVMNDVNYHKLEGFPFEAYVVVACPRVPLDDYGAWRK
PVLTPKEVEILLGLREEYEFDEILGGPRESDEPFGISIHSTR
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
285729
Kawarabayasi Y.,Sawada M.,Horikawa H.,Haikawa Y.,Hino Y.,Yamamoto S.,Sekine M.,Baba S.,Kosugi H.,Hosoyama A.,Nagai Y.,Sakai M.,Ogura K.,Otsuka R.,Nakazawa H.,Takamiya M.,Ohfuku Y.,Funahashi T.,Tanaka T.,Kudoh Y.,Yamazaki J.,Kushida N.,Oguchi A.,Aoki K.,Yoshizawa T.,Nakamura Y.,Robb F.T.,Horikoshi K.,Masuchi Y.,Shizuya H.,Kikuchi H.
Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.
DNA Res.
5
55-76
1998
285730
Zhu X.,Dzikovski B.,Su X.,Torelli A.T.,Zhang Y.,Ealick S.E.,Freed J.H.,Lin H.
Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis.
Mol. Biosyst.
7
74-81
2011
285731
Zhang Y.,Zhu X.,Torelli A.T.,Lee M.,Dzikovski B.,Koralewski R.M.,Wang E.,Freed J.,Krebs C.,Ealick S.E.,Lin H.
Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme.
Nature
465
891-896
2010
