Sequence of AAPAT_THET8
EC Number:2.6.1.78
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
aspartate-prephenate aminotransferase
Q56232
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
385
42051
Reaction
L-arogenate + oxaloacetate = prephenate + L-aspartate
Other sequences found for EC No. 2.6.1.78
General information:
Sequence
0 MRGLSRRVQA MKPSATVAVN AKALELRRQG VDLVALTAGE PDFDTPEHVK EAARRALAQG
60 KTKYAPPAGI PELREALAEK FRRENGLSVT PEETIVTVGG KQALFNLFQA ILDPGDEVIV
120 LSPYWVSYPE MVRFAGGVVV EVETLPEEGF VPDPERVRRA ITPRTKALVV NSPNNPTGAV
180 YPKEVLEALA RLAVEHDFYL VSDEIYEHLL YEGEHFSPGR VAPEHTLTVN GAAKAFAMTG
240 WRIGYACGPK EVIKAMASVS SQSTTSPDTI AQWATLEALT NQEASRAFVE MAREAYRRRR
300 DLLLEGLTAL GLKAVRPSGA FYVLMDTSPI APDEVRAAER LLEAGVAVVP GTDFAAFGHV
360 RLSYATSEEN LRKALERFAR VLGRA
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
638042
Okamoto A.,Kato R.,Masui R.,Yamagishi A.,Oshima T.,Kuramitsu S.
An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8.
J. Biochem.
119
135-144
1996
638044
Dornfeld C.,Weisberg A.J.,Ritesh K.C.,Dudareva N.,Jelesko J.G.,Maeda H.A.
Phylobiochemical characterization of class-Ib aspartate/prephenate aminotransferases reveals evolution of the plant arogenate phenylalanine pathway.
Plant Cell
26
3101-3114
2014
638045
Giustini C.,Graindorge M.,Cobessi D.,Crouzy S.,Robin A.,Curien G.,Matringe M.
Tyrosine metabolism: identification of a key residue in the acquisition of prephenate aminotransferase activity by 1beta aspartate aminotransferase.
FEBS J.
286
2118-2134
2019
638046
Nakai T.,Okada K.,Akutsu S.,Miyahara I.,Kawaguchi S.,Kato R.,Kuramitsu S.,Hirotsu K.
Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate.
Biochemistry
38
2413-2424
1999
638047
Ura H.,Nakai T.,Kawaguchi S.,Miyahara I.,Hirotsu K.,Kuramitsu S.
Substrate recognition mechanism of thermophilic dual-substrate enzyme.
J. Biochem.
130
89-98
2001
