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Sequence of GAPN_THETE

EC Number:1.2.1.90

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+]
O57693
Thermoproteus tenax
501
54090
Reaction
D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O = 3-phospho-D-glycerate + NAD(P)H + 2 H+
Other sequences found for EC No. 1.2.1.90

General information:

Sequence
show sequence in fasta format
  0 MRAGLLEGVI KEKGGVPVYP SYLAGEWGGS GQEIEVKSPI DLATIAKVIS PSREEVERTL
 60 DVLFKRGRWS ARDMPGTERL AVLRKAADII ERNLDVFAEV LVMNAGKPKS AAVGEVKAAV
120 DRLRLAELDL KKIGGDYIPG DWTYDTLETE GLVRREPLGV VAAITPFNYP LFDAVNKITY
180 SFIYGNAVVV KPSISDPLPA AMAVKALLDA GFPPDAIALL NLPGKEAEKI VADDRVAAVS
240 FTGSTEVGER VVKVGGVKQY VMELGGGDPA IVLEDADLDL AADKIARGIY SYAGQRCDAI
300 KLVLAERPVY GKLVEEVAKR LSSLRVGDPR DPTVDVGPLI SPSAVDEMMA AIEDAVEKGG
360 RVLAGGRRLG PTYVQPTLVE APADRVKDMV LYKREVFAPV ASAVEVKDLD QAIELANGRP
420 YGLDAAVFGR DVVKIRRAVR LLEVGAIYIN DMPRHGIGYY PFGGRKKSGV FREGIGYAVE
480 AVTAYKTIVF NYKGKGVWKY E
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
674119
Brunner N.A.,Brinkmann H.,Siebers B.,Hensel R.
NAD+-dependent GAPDH from Thermoproteus tenax - the first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties.
J. Biol. Chem.
273
6149-6156
1998
674120
Hensel R.,Laumann S.,Lang J.,Heumann H.,Lottspeich F.
Characterization of two D-glyceraldehyde-3-phosphate dehydrogenases from the extremely thermophilic archaebacterium Thermoproteus tenax.
Eur. J. Biochem.
170
325-333
1987
674121
Pohl E.,Brunner N.,Wilmanns M.,Hensel R.
The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax.
J. Biol. Chem.
277
19938-19945
2002
674122
Lorentzen E.,Hensel R.,Knura T.,Ahmed H.,Pohl E.
Structural basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase from Thermoproteus tenax.
J. Mol. Biol.
341
815-828
2004