Sequence of G7J7Q5_MEDTR
EC Number:3.1.3.15
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
L-histidinol phosphate + H2O = L-histidinol + phosphate
Other sequences found for EC No. 3.1.3.15
EC Number:3.1.3.25
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
myo-inositol phosphate + H2O = myo-inositol + phosphate
Other sequences found for EC No. 3.1.3.25
General information:
Sequence
0 MLLSQCHLLH SKIPNIEKNN PFRNQYQLQF QPNKLTSPLL LSSSSPKFRI RAMSSSSSPP
60 HQLNHFSDVA NKAANAAGDV IRKYFRKNNF DIIHKNDLSP VTIADQSAEE AMVSVILDNF
120 PSHAVYGEEK GWRCKQDSAD YVWVLDPIDG TKSFITGKPL FGTLIALLQN GTPILGIIDQ
180 PVLKERWIGI TGKRTTLNGQ EVSTRTCADL SQAYLYTTSP HLFSGDAEEA FIRVRDKVKI
240 PLYGCDCYAY ALLSSGFVDL VVESGLKPYD FLALIPVIEG SGGVITDWKG HQLRWEASPL
300 SIATSFNVVA AGDKQIHQQA LDSLQW
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
227736505
Young N.D.,Debelle F.,Oldroyd G.E.D.,Geurts R.,Cannon S.B.,Udvardi M.K.,Benedito V.A.,Mayer K.F.X.,Gouzy J.,Schoof H.,Van de Peer Y.,Proost S.,Cook D.R.,Meyers B.C.,Spannagl M.,Cheung F.,De Mita S.,Krishnakumar V.,Gundlach H.,Zhou S.,Mudge J.,Bharti A.K.,Murray J.D.,Naoumkina M.A.,Rosen B.,Silverstein K.A.T.,Tang H.,Rombauts S.,Zhao P.X.,Zhou P.,Barbe V.,Bardou P.,Bechner M.,Bellec A.,Berger A.,Berges H.,Bidwell S.,Bisseling T.,Choisne N.,Couloux A.,Denny R.,Deshpande S.,Dai X.,Doyle J.J.,Dudez A.-M.,Farmer A.D.,Fouteau S.,Franken C.,Gibelin C.,Gish J.,Goldstein S.,Gonzalez A.J.,Green P.J.,Hallab A.,Hartog M.,Hua A.,Humphray S.J.,Jeong D.-H.,Jing Y.,Jocker A.,Kenton S.M.,Kim D.-J.,Klee K.,Lai H.,Lang C.,Lin S.,Macmil S.L.,Magdelenat G.,Matthews L.,McCorrison J.,Monaghan E.L.,Mun J.-H.,Najar F.Z.,Nicholson C.,Noirot C.,O'Bleness M.,Paule C.R.,Poulain J.,Prion F.,Qin B.,Qu C.,Retzel E.F.,Riddle C.,Sallet E.,Samain S.,Samson N.,Sanders I.,Saurat O.,Scarpelli C.,Schiex T.,Segurens B.,Severin A.J.,Sherrier D.J.,Shi R.,Sims S.,Singer S.R.,Sinharoy S.,Sterck L.,Viollet A.,Wang B.-B.,Wang K.,Wang M.,Wang X.,Warfsmann J.,Weissenbach J.,White D.D.,White J.D.,Wiley G.B.,Wincker P.,Xing Y.,Yang L.,Yao Z.,Ying F.,Zhai J.,Zhou L.,Zuber A.,Denarie J.,Dixon R.A.,May G.D.,Schwartz D.C.,Rogers J.,Quetier F.,Town C.D.,Roe B.A.
The Medicago genome provides insight into the evolution of rhizobial symbioses.
Nature
480
520-524
2011
227736506
Tang H.,Krishnakumar V.,Bidwell S.,Rosen B.,Chan A.,Zhou S.,Gentzbittel L.,Childs K.L.,Yandell M.,Gundlach H.,Mayer K.F.,Schwartz D.C.,Town C.D.
An improved genome release (version Mt4.0) for the model legume Medicago truncatula.
BMC Genomics
15
312-312
2014
227736508
Ruszkowski M.,Dauter Z.
Structural Studies of Medicago truncatula Histidinol Phosphate Phosphatase from Inositol Monophosphatase Superfamily Reveal Details of Penultimate Step of Histidine Biosynthesis in Plants.
J. Biol. Chem.
291
9960-9973
2016
227736509
Luo Z.
Selenourea: a convenient phasing vehicle for macromolecular X-ray crystal structures.
Sci. Rep.
6
37123-37123
2016
227736510
Pecrix Y.,Staton S.E.,Sallet E.,Lelandais-Briere C.,Moreau S.,Carrere S.,Blein T.,Jardinaud M.F.,Latrasse D.,Zouine M.,Zahm M.,Kreplak J.,Mayjonade B.,Satge C.,Perez M.,Cauet S.,Marande W.,Chantry-Darmon C.,Lopez-Roques C.,Bouchez O.,Berard A.,Debelle F.,Munos S.,Bendahmane A.,Berges H.,Niebel A.,Buitink J.,Frugier F.,Benhamed M.,Crespi M.,Gouzy J.,Gamas P.
Whole-genome landscape of Medicago truncatula symbiotic genes.
Nat. Plants
4
1017-1025
2018
