AT1G32440.1 :

DomainDescriptionEvalueBitsGAStartEnd
IMPDHIMP dehydrogenase / GMP reductase domain2E-051224.0043150
PKPyruvate kinase, barrel domain038320.4099435
CellulaseCellulase (glycosyl hydrolase family 5)3.1E-051220.50107164
HpcH_HpaIHpcH/HpaI aldolase/citrate lyase family5E-061420.00273345
IMPDHIMP dehydrogenase / GMP reductase domain0.19-124.00389406
HpcH_HpaIHpcH/HpaI aldolase/citrate lyase family0.25-120.00392411
PK_CPyruvate kinase, alpha/beta domain1.3E-175321.70468548

 571

IMPDH
PK
Cellulase
HpcH_HpaI
IMPDH
HpcH_HpaI
PK_C


References:

PK_C
9308890 Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution. Arch Biochem Biophys 1997;345:199-206.

HpcH_HpaI
9073078 The bphDEF meta-cleavage pathway genes involved in biphenyl/polychlorinated biphenyl degradation are located on a linear plasmid and separated from the initial bphACB genes in Rhodococcus sp. strain RHA1. Gene 1997;187:141-149.
8529896 Sequence of the Escherichia coli C homoprotocatechuic acid degradative operon completed with that of the 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase-encoding gene (hpcH). Gene 1995;166:73-76.

IMPDH
9271497 Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex. Biochemistry 1997;36:10666-10674.
10200156 Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase. Biochemistry 1999;38:4691-4700.

PK
9308890 Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution. Arch Biochem Biophys 1997;345:199-206.

Cellulase