Sequence of TPIS_STAAR
EC Number:5.3.1.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
D-Glyceraldehyde 3-phosphate = glycerone phosphate
Other sequences found for EC No. 5.3.1.1
General information:
Sequence
0 MRTPIIAGNW KMNKTVQEAK DFVNALPTLP DSKEVESVIC APAIQLDALT TAVKEGKAQG
60 LEIGAQNTYF EDNGAFTGET SPVALADLGV KYVVIGHSER RELFHETDEE INKKAHAIFK
120 HGMTPIICVG ETDEERESGK ANDVVGEQVK KAVAGLSEDQ LKSVVIAYEP IWAIGTGKSS
180 TSEDANEMCA FVRQTIADLS SKEVSEATRI QYGGSVKPNN IKEYMAQTDI DGALVGGASL
240 KVEDFVQLLE GAK
Download this sequence
in fasta formatDownload all sequences for 5.3.1.1
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1266113
Holden M.T.G.,Feil E.J.,Lindsay J.A.,Peacock S.J.,Day N.P.J.,Enright M.C.,Foster T.J.,Moore C.E.,Hurst L.,Atkin R.,Barron A.,Bason N.,Bentley S.D.,Chillingworth C.,Chillingworth T.,Churcher C.,Clark L.,Corton C.,Cronin A.,Doggett J.,Dowd L.,Feltwell T.,Hance Z.,Harris B.,Hauser H.,Holroyd S.,Jagels K.,James K.D.,Lennard N.,Line A.,Mayes R.,Moule S.,Mungall K.,Ormond D.,Quail M.A.,Rabbinowitsch E.,Rutherford K.M.,Sanders M.,Sharp S.,Simmonds M.,Stevens K.,Whitehead S.,Barrell B.G.,Spratt B.G.,Parkhill J.
Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance.
Proc. Natl. Acad. Sci. U.S.A.
101
9786-9791
2004
1266114
Becker P.,Hufnagle W.,Peters G.,Herrmann M.
Detection of differential gene expression in biofilm-forming versus planktonic populations of Staphylococcus aureus using micro-representational-difference analysis.
Appl. Environ. Microbiol.
67
2958-2965
2001
1266115
Furuya H.,Ikeda R.
Interaction of triosephosphate isomerase from Staphylococcus aureus with plasminogen.
Microbiol. Immunol.
55
855-862
2011
1266116
Mukherjee S.,Roychowdhury A.,Dutta D.,Das A.K.
Crystal structures of triosephosphate isomerase from methicillin resistant Staphylococcus aureus MRSA252 provide structural insights into novel modes of ligand binding and unique conformations of catalytic loop.
Biochimie
94
2532-2544
2012
