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Sequence of KDADA_AZOBR

EC Number:4.2.1.43

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
2-dehydro-3-deoxy-L-arabinonate dehydratase
Q1JUQ0
Azospirillum brasilense
309
33756
Reaction
2-dehydro-3-deoxy-L-arabinonate = 2,5-dioxopentanoate + H2O
Other sequences found for EC No. 4.2.1.43

General information:

Sequence
show sequence in fasta format
  0 MTSSSTPRHR GIFPVVPTTF ADTGELDLAS QKRAVDFMID AGSDGLCILA NFSEQFAITD
 60 DERDVLTRTI LEHVAGRVPV IVTTSHYSTQ VCAARSLRAQ QLGAAMVMAM PPYHGATFRV
120 PEAQIFEFYA RVSDAIAIPI MVQDAPASGT ALSAPFLARM AREIEQVAYF KIETPGAANK
180 LRELIRLGGD AIEGPWDGEE AITLLADLHA GATGAMTGGG FPDGIRPILE AWREGRHDDA
240 YARYQAWLPL INHENRQSGI LTAKALMREG GVIASERPRH PMPELHPDTR AELLAIARRL
300 DPLVLRWAH
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
816207
Watanabe S.,Shimada N.,Tajima K.,Kodaki T.,Makino K.
Identification and characterization of L-arabonate dehydratase, L-2-keto-3-deoxyarabonate dehydratase and L-arabinolactonase involved in an alternative pathway of L-arabinose metabolism: novel evolutionary insight into sugar metabolism.
J. Biol. Chem.
281
33521-33536
2006
816208
Novick N.J.,Tyler M.E.
L-arabinose metabolism in Azospirillum brasiliense.
J. Bacteriol.
149
364-367
1982
816209
Shimada N.,Mikami B.,Watanabe S.,Makino K.
Preliminary crystallographic analysis of L-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of L-arabinose metabolism.
Acta Crystallogr. F
63
393-395
2007