Curated BLAST for Genomes

 

Search for Curated Proteins

Found 39 curated entries in PaperBLAST's database that match '1.4.1.2' as complete word(s). Or try another search

These curated entries have 30 distinct sequences. Cluster these sequences (recent entries may not be included in clustering results).

DHE2_BACSU / P39633: Catabolic NAD-specific glutamate dehydrogenase RocG; NAD-GDH; Glutamate dehydrogenase; GlutDH; Trigger enzyme RocG; EC 1.4.1.2 from Bacillus subtilis

GUDB_BACSU / P50735: Cryptic catabolic NAD-specific glutamate dehydrogenase GudB; NAD-GDH; EC 1.4.1.2 from Bacillus subtilis

GLUD2_DICDI / Q54VI3: Glutamate dehydrogenase 2; NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Dictyostelium discoideum

AZOBR_RS00190: L-glutamate dehydrogenase (NAD+) (EC 1.4.1.2) from Azospirillum brasilense

AN7451: NAD dependent glutamate dehydrogenase; EC 1.4.1.2 from Emericella nidulans

DHE2_PYRCJ / A3MUY9: NAD(+)-dependent glutamate dehydrogenase; NAD-GDH; NAD-specific glutamate dehydrogenase; EC 1.4.1.2 from Pyrobaculum calidifontis
A3MUY9: glutamate dehydrogenase (EC 1.4.1.2) from Pyrobaculum calidifontis

Psest_1944: NAD-specific glutamate dehydrogenase (EC 1.4.1.2), large form from Pseudomonas stutzeri

DHE2_HALSI / P29051: NAD-specific glutamate dehydrogenase A; NAD-GDH A; EC 1.4.1.2 from Halobacterium salinarum
gdhA / GB|AAW19068.1: glutamate dehydrogenase; EC 1.4.1.2 from Halobacterium salinarum
P29051: glutamate dehydrogenase (EC 1.4.1.2) from Halobacterium salinarum

gluD / GB|AAA62756.1: NAD-specific glutamate dehydrogenase; EC 1.4.1.2 from Clostridium difficile
P27346: glutamate dehydrogenase (EC 1.4.1.2) from Clostridioides difficile

DHE2_CLOSY / P24295: NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Clostridium symbiosum
P24295: glutamate dehydrogenase (EC 1.4.1.2) from Clostridium symbiosum

DHE2_PEPAS / P28997: NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Peptoniphilus asaccharolyticus
gdhA / P28997: NAD-glutamate dehydrogenase subunit (EC 1.4.1.2) from Peptoniphilus asaccharolyticus
P28997: glutamate dehydrogenase (EC 1.4.1.2) from Peptoniphilus asaccharolyticus

DHE2_YEAST / P33327: NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Saccharomyces cerevisiae
P33327: glutamate dehydrogenase (EC 1.4.1.2) from Saccharomyces cerevisiae

DHE2_MYCTU / O53203: NAD-specific glutamate dehydrogenase; NAD-GDH; NAD(+)-dependent glutamate dehydrogenase; EC 1.4.1.2 from Mycobacterium tuberculosis

DHE2_HALED / E1V4J5: NAD-specific glutamate dehydrogenase; NAD-GDH; NAD(+)-dependent glutamate dehydrogenase; EC 1.4.1.2 from Halomonas elongata

DHE2_MYCS2 / A0R1C2: NAD-specific glutamate dehydrogenase; NAD-GDH; NAD(+)-dependent glutamate dehydrogenase; EC 1.4.1.2 from Mycolicibacterium smegmatis
A0R1C2: glutamate dehydrogenase (EC 1.4.1.2) from Mycolicibacterium smegmatis

DHE2_PSEAE / Q9HZE0: NAD-specific glutamate dehydrogenase; NAD-GDH; NAD(+)-dependent glutamate dehydrogenase; EC 1.4.1.2 from Pseudomonas aeruginosa

GDH2_SCHPO / Q9USN5: Probable NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Schizosaccharomyces pombe

GDH2 / Q38946: glutamate dehydrogenase β subunit (EC 1.4.1.2) from Arabidopsis thaliana

Q0E5H9: glutamate dehydrogenase (EC 1.4.1.2) from Halobacillus halophilus

Q0E5I0: glutamate dehydrogenase (EC 1.4.1.2) from Halobacillus halophilus

Q5QDM6: glutamate dehydrogenase (EC 1.4.1.2) from Lupinus luteus

Q977U6: glutamate dehydrogenase (EC 1.4.1.2) from Haloferax mediterranei

Q9TVN3: glutamate dehydrogenase (EC 1.4.1.2) from Entodinium caudatum

Q9Y8I4: glutamate dehydrogenase (EC 1.4.1.2) from Pyrobaculum islandicum

P00366: glutamate dehydrogenase (EC 1.4.1.2) from Bos taurus

Q852M0: glutamate dehydrogenase (EC 1.4.1.2) from Oryza sativa

Q8CJY0: glutamate dehydrogenase (EC 1.4.1.2) from Streptomyces coelicolor

A0A0H3C571: glutamate dehydrogenase (EC 1.4.1.2) from Caulobacter vibrioides

P93541: glutamate dehydrogenase (EC 1.4.1.2) from Solanum lycopersicum

P96110: trimer complex (EC 1.4.1.2) from Thermotoga maritima

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory