Sequence of PHYA2_ASPTE
EC Number:3.1.3.8
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Other sequences found for EC No. 3.1.3.8
General information:
Sequence
0 MGVFVVLLSI ATLFGSTSGT ALGPRGNHSD CTSVDRGYQC FPELSHKWGL YAPYFSLQDE
60 SPFPLDVPDD CHITFVQVLA RHGARSPTDS KTKAYAATIA AIQKNATALP GKYAFLKSYN
120 YSMGSENLNP FGRNQLQDLG AQFYRRYDTL TRHINPFVRA ADSSRVHESA EKFVEGFQNA
180 RQGDPHANPH QPSPRVDVVI PEGTAYNNTL EHSICTAFEA STVGDAAADN FTAVFAPAIA
240 KRLEADLPGV QLSADDVVNL MAMCPFETVS LTDDAHTLSP FCDLFTAAEW TQYNYLLSLD
300 KYYGYGGGNP LGPVQGVGWA NELIARLTRS PVHDHTCVNN TLDANPATFP LNATLYADFS
360 HDSNLVSIFW ALGLYNGTKP LSQTTVEDIT RTDGYAAAWT VPFAARAYIE MMQCRAEKQP
420 LVRVLVNDRV MPLHGCAVDN LGRCKRDDFV EGLSFARAGG NWAECF
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
74947
Wyss M.,Pasamontes L.,Friedlein A.,Remy R.,Tessier M.,Kronenberger A.,Middendorf A.,Lehmann M.,Schnoebelen L.,Roethlisberger U.,Kusznir E.,Wahl G.,Mueller F.,Lahm H.-W.,Vogel K.,van Loon A.P.G.M.
Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): molecular size, glycosylation pattern, and engineering of proteolytic resistance.
Appl. Environ. Microbiol.
65
359-366
1999
74948
Wyss M.,Brugger R.,Kronenberger A.,Remy R.,Fimbel R.,Oesterhelt G.,Lehmann M.,van Loon A.P.G.M.
Biochemical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): catalytic properties.
Appl. Environ. Microbiol.
65
367-373
1999
