SitesBLAST
Comparing 3610460 FitnessBrowser__Dino:3610460 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P00370 NADP-specific glutamate dehydrogenase; NADP-GDH; EC 1.4.1.4 from Escherichia coli (strain K12) (see 2 papers)
53% identity, 98% coverage: 9:447/447 of query aligns to 8:447/447 of P00370
- K92 (= K93) mutation to S: Complete loss of dehydrogenase activity.
- K128 (= K129) mutation to H: Reduces catalytic activity and increases pH optima for activity. Increases relative activity with amino acid substrates other than glutamate, especially L-norvaline.; mutation to R: Reduced catalytic activity and increases pH optima for activity. NADP-specific glutamate dehydrogenase.
5ijzA Crystal structure of glutamate dehydrogenase(gdh) from corynebacterium glutamicum (see paper)
50% identity, 95% coverage: 22:447/447 of query aligns to 21:447/447 of 5ijzA
- active site: K128 (= K129), D168 (= D169)
- binding 2-oxoglutaric acid: K92 (= K93), G93 (= G94), G94 (= G95), Q113 (= Q114), K116 (= K117), K128 (= K129), A166 (= A167), R208 (= R208), V376 (= V377), S379 (= S380)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K136 (≠ R137), D168 (= D169), I169 (= I170), T212 (= T212), S241 (≠ K241), G242 (= G242), N243 (= N243), V244 (= V244), D264 (= D264), S265 (≠ T265), R290 (≠ G290), A321 (= A322), T322 (= T323), A346 (= A347), N347 (= N348), N372 (= N373)
5gudA Glutamate dehydrogenase from corynebacterium glutamicum (alpha- iminoglutarate/NADP+ complex) (see paper)
50% identity, 95% coverage: 22:447/447 of query aligns to 21:447/447 of 5gudA
- active site: K128 (= K129), D168 (= D169)
- binding (2Z)-2-iminopentanedioic acid: K92 (= K93), G93 (= G94), G94 (= G95), Q113 (= Q114), K116 (= K117), K128 (= K129), A166 (= A167), R208 (= R208), V376 (= V377), S379 (= S380)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K136 (≠ R137), D168 (= D169), I169 (= I170), R208 (= R208), T212 (= T212), S241 (≠ K241), G242 (= G242), N243 (= N243), V244 (= V244), D264 (= D264), S265 (≠ T265), R290 (≠ G290), A321 (= A322), T322 (= T323), G345 (= G346), A346 (= A347), N347 (= N348), N372 (= N373)
5gudE Glutamate dehydrogenase from corynebacterium glutamicum (alpha- iminoglutarate/NADP+ complex) (see paper)
50% identity, 95% coverage: 22:447/447 of query aligns to 34:460/460 of 5gudE
- active site: K141 (= K129), D181 (= D169)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: T225 (= T212), S254 (≠ K241), G255 (= G242), N256 (= N243), V257 (= V244), D277 (= D264), S278 (≠ T265), R303 (≠ G290), A334 (= A322), T335 (= T323), A359 (= A347), N360 (= N348)
P00369 NADP-specific glutamate dehydrogenase; NADP-GDH; NADP-dependent glutamate dehydrogenase; EC 1.4.1.4 from Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) (see paper)
49% identity, 97% coverage: 12:445/447 of query aligns to 1:448/454 of P00369
- M1 (≠ L12) modified: Initiator methionine, Removed
- S2 (= S13) modified: N-acetylserine
7f79C Crystal structure of glutamate dehydrogenase 3 from candida albicans in complex with alpha-ketoglutarate and NADPH (see paper)
48% identity, 95% coverage: 22:445/447 of query aligns to 8:455/458 of 7f79C
- binding 2-oxoglutaric acid: K79 (= K93), G80 (= G94), G81 (= G95), Q100 (= Q114), K103 (= K117), K115 (= K129), V380 (= V377), S383 (= S380)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R83 (= R97), H85 (= H99), K123 (≠ R137), D155 (= D169), I156 (= I170), R194 (= R208), T198 (= T212), S230 (≠ K241), G231 (= G242), N232 (= N243), V233 (= V244), D253 (= D264), S254 (≠ T265), K276 (≠ Q284), A321 (= A322), T322 (= T323), G345 (= G346), S346 (≠ A347), N347 (= N348), N376 (= N373)
P24295 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Clostridium symbiosum (Bacteroides symbiosus) (see 4 papers)
46% identity, 95% coverage: 22:446/447 of query aligns to 19:448/450 of P24295
- K90 (= K93) binding ; mutation to L: Increased substrate activity for methionine and norleucine but negligible activity with either glutamate or leucine. Dramatic reduction in the dehydrogenase activity with glutamate as the substrate; when associated with V-381.
- Q111 (= Q114) binding
- K114 (= K117) binding
- K126 (= K129) active site, Proton donor
- G165 (= G168) binding
- D166 (= D169) mutation to S: Dramatic reduction in the dehydrogenase activity. Specific activity is decreased 1000-fold in the reductive amination reaction and 100000-fold for oxidative deamination.
- S381 (= S380) binding ; mutation to V: Dramatic reduction in the dehydrogenase activity with glutamate as the substrate; when associated with L-90.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1bgvA Glutamate dehydrogenase (see paper)
46% identity, 95% coverage: 22:446/447 of query aligns to 18:447/449 of 1bgvA
7ecsA Crystal structure of aspergillus terreus glutamate dehydrogenase (atgdh) complexed with malonate and NADPH (see paper)
47% identity, 97% coverage: 12:445/447 of query aligns to 1:457/460 of 7ecsA
- binding malonate ion: G79 (= G94), G80 (= G95), Q99 (= Q114), K102 (= K117), K114 (= K129), S326 (≠ D328), G327 (≠ Q329), E328 (≠ S330), T350 (= T352), A352 (≠ G354)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K122 (≠ R137), D154 (= D169), I155 (= I170), R193 (= R208), T197 (= T212), S229 (≠ K241), G230 (= G242), N231 (= N243), V232 (= V244), D252 (= D264), S253 (≠ T265), K279 (≠ Q284), A320 (= A322), T321 (= T323), G344 (= G346), S345 (≠ A347), N346 (= N348), N379 (= N373)
7ecrA Crystal structure of aspergillus terreus glutamate dehydrogenase (atgdh) complexed with succinate and adp-ribose (see paper)
47% identity, 97% coverage: 12:445/447 of query aligns to 1:457/460 of 7ecrA
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4r,5r)-3,4,5-trihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: K122 (≠ R137), D154 (= D169), I155 (= I170), S229 (≠ K241), G230 (= G242), N231 (= N243), V232 (= V244), D252 (= D264), S253 (≠ T265), K279 (≠ Q284), A320 (= A322), T321 (= T323), G344 (= G346), S345 (≠ A347), N346 (= N348), N379 (= N373)
5xwcA Crystal structure of aspergillus niger glutamate dehydrogenase complexed with alpha-iminoglutarate, 2-amino-2-hydroxyglutarate and NADP (see paper)
47% identity, 97% coverage: 13:445/447 of query aligns to 1:456/459 of 5xwcA
- binding (2Z)-2-iminopentanedioic acid: K77 (= K93), G78 (= G94), Q98 (= Q114), K101 (= K117), K113 (= K129), A151 (= A167), R192 (= R208), V382 (= V377), S385 (= S380)
- binding (2S)-2-azanyl-2-oxidanyl-pentanedioic acid: K77 (= K93), G78 (= G94), G79 (= G95), Q98 (= Q114), K101 (= K117), K113 (= K129), A151 (= A167), D153 (= D169), R192 (= R208), V382 (= V377), S385 (= S380)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H83 (= H99), K121 (≠ R137), D153 (= D169), I154 (= I170), R192 (= R208), T196 (= T212), S228 (≠ K241), G229 (= G242), N230 (= N243), V231 (= V244), D251 (= D264), S252 (≠ T265), A319 (= A322), T320 (= T323), G343 (= G346), S344 (≠ A347), N345 (= N348), N378 (= N373)
5xw0A Crystal structure of aspergillus niger glutamate dehydrogenase complexed with isophthalate and NADPH (see paper)
47% identity, 97% coverage: 13:445/447 of query aligns to 1:456/459 of 5xw0A
- binding benzene-1,3-dicarboxylic acid: K77 (= K93), G78 (= G94), Q98 (= Q114), K101 (= K117), K113 (= K129), A151 (= A167), G152 (= G168), D153 (= D169), R192 (= R208), S385 (= S380)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H83 (= H99), K121 (≠ R137), D153 (= D169), I154 (= I170), R192 (= R208), T196 (= T212), S228 (≠ K241), G229 (= G242), N230 (= N243), V231 (= V244), D251 (= D264), S252 (≠ T265), A319 (= A322), T320 (= T323), G343 (= G346), S344 (≠ A347), N345 (= N348), N378 (= N373)
5xvxA Crystal structure of aspergillus niger glutamate dehydrogenase complexed with alpha-ketoglutarate and NADPH (see paper)
47% identity, 97% coverage: 13:445/447 of query aligns to 1:456/459 of 5xvxA
- binding 2-oxoglutaric acid: K77 (= K93), Q98 (= Q114), K101 (= K117), K113 (= K129), A151 (= A167), R192 (= R208), V382 (= V377), S385 (= S380)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K121 (≠ R137), D153 (= D169), I154 (= I170), R192 (= R208), T196 (= T212), S228 (≠ K241), G229 (= G242), N230 (= N243), V231 (= V244), D251 (= D264), S252 (≠ T265), A319 (= A322), T320 (= T323), G343 (= G346), S344 (≠ A347), N345 (= N348), N378 (= N373)
5xvvB Crystal structure of forward inhibited aspergillus niger glutamate dehydrogenase with both apo- and alpha ketoglutarate bound subunits (see paper)
47% identity, 97% coverage: 13:445/447 of query aligns to 1:456/459 of 5xvvB
P78804 NADP-specific glutamate dehydrogenase; NADP-GDH; NADP-dependent glutamate dehydrogenase; EC 1.4.1.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
47% identity, 95% coverage: 21:445/447 of query aligns to 5:448/451 of P78804
- S252 (≠ T265) modified: Phosphoserine
P80053 Glutamate dehydrogenase 2; GDH-2; EC 1.4.1.3 from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
30% identity, 86% coverage: 29:412/447 of query aligns to 2:381/420 of P80053
- M2 (≠ L29) modified: N-acetylmethionine
- K254 (≠ E273) modified: N6-methyllysine
- K260 (≠ A281) modified: N6-methyllysine
- K372 (vs. gap) modified: N6-methyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 391 modified: N6-methyllysine
- 392 modified: N6-methyllysine
8owmC Crystal structure of glutamate dehydrogenase 2 from arabidopsis thaliana binding ca, NAD and 2,2-dihydroxyglutarate (see paper)
32% identity, 81% coverage: 49:408/447 of query aligns to 24:374/413 of 8owmC
- binding calcium ion: S29 (≠ R54), I32 (≠ V57)
- binding nicotinamide-adenine-dinucleotide: D144 (= D169), M145 (≠ I170), R183 (= R208), T187 (= T212), F216 (≠ K241), G217 (= G242), N218 (= N243), V219 (= V244), D239 (= D264), I240 (≠ T265), C290 (= C321), A291 (= A322), A313 (= A347), N314 (= N348), N339 (= N373)
- binding 2,2-bis(oxidanyl)pentanedioic acid: K68 (= K93), G70 (= G95), M89 (≠ Q114), K92 (= K117), K104 (= K129), A142 (= A167), R183 (= R208), N314 (= N348), V343 (= V377), S346 (= S380)
1v9lA L-glutamate dehydrogenase from pyrobaculum islandicum complexed with NAD (see paper)
33% identity, 80% coverage: 55:411/447 of query aligns to 28:386/418 of 1v9lA
- active site: K102 (= K129), D142 (= D169)
- binding nicotinamide-adenine-dinucleotide: T186 (= T212), Q213 (≠ S239), G216 (= G242), N217 (= N243), V218 (= V244), D238 (= D264), I239 (≠ T265), A296 (= A322), I297 (≠ T323), A318 (= A347), N319 (= N348), N344 (= N373)
P39633 Catabolic NAD-specific glutamate dehydrogenase RocG; NAD-GDH; Glutamate dehydrogenase; GlutDH; Trigger enzyme RocG; EC 1.4.1.2 from Bacillus subtilis (strain 168) (see 2 papers)
31% identity, 86% coverage: 58:440/447 of query aligns to 45:417/424 of P39633
- E93 (≠ T106) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (≠ N135) mutation to N: Unable to control gltAB expression via an inhibitory interactions with the transcriptional regulator GltC. Reduces the affinity for glutamate and ammonium.
- Q144 (≠ P157) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ N171) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (≠ T246) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ G346) mutation to R: No effect.
Sites not aligning to the query:
- 27 E→F: Increase of thermostability 8 degrees Celsius higher than that of the wild-type.
3aoeB Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
34% identity, 79% coverage: 55:409/447 of query aligns to 40:390/424 of 3aoeB
Sites not aligning to the query:
Query Sequence
>3610460 FitnessBrowser__Dino:3610460
MERRDALSELFLSELATNPDFEPNFYNALAEVAQDVLTIEKNDKAYAAARVLARLAVPDR
ILSFRVTWADDAGEVQVNQAWRVQTSNAIGPYKGGLRFHPSVTQDTLKFLGFEQCFKNAL
TGLPMGGAKGGADFNPRGRSRQEIMRFCQALMAQMAPFIGPDQDVPAGDINVGTREVGWL
FGAWRQRRGMFGGAFTGKGLSFGGSKMRVEATGFGVVYFVACMLAEMGTSLEGKRVLVSG
KGNVATHAAQKAVEEGAKVLTLSDTGGTLLAEEGLTLDAIAWVQARKDAGEDIAAPPAEL
GLRYLEGQTPWHIPADIALPCATQNELDQSAAEILRDNGLMLLAEGANMPLTPGASRVMR
LAGIAVAPGKAANAGGVAVSGLEMTQNAQRLTWSAARVDETLRDIMERIHRAVVAEGRVD
GRIDYGRGANIAAYRKLADAITAQGVL
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory