SitesBLAST
Comparing Ac3H11_315 FitnessBrowser__acidovorax_3H11:Ac3H11_315 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
71% identity, 95% coverage: 22:464/464 of query aligns to 6:447/447 of P00370
- K92 (= K108) mutation to S: Complete loss of dehydrogenase activity.
- K128 (= K144) 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)
56% identity, 95% coverage: 25:464/464 of query aligns to 9:447/447 of 5ijzA
- active site: K128 (= K144), D168 (= D184)
- binding 2-oxoglutaric acid: K92 (= K108), G93 (= G109), G94 (= G110), Q113 (= Q129), K116 (= K132), K128 (= K144), A166 (= A182), R208 (= R223), V376 (= V393), S379 (= S396)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K136 (= K152), D168 (= D184), I169 (= I185), T212 (= T227), S241 (= S256), G242 (= G257), N243 (= N258), V244 (= V259), D264 (= D279), S265 (= S280), R290 (= R308), A321 (= A338), T322 (= T339), A346 (= A363), N347 (= N364), N372 (= N389)
5gudA Glutamate dehydrogenase from corynebacterium glutamicum (alpha- iminoglutarate/NADP+ complex) (see paper)
57% identity, 93% coverage: 33:464/464 of query aligns to 17:447/447 of 5gudA
- active site: K128 (= K144), D168 (= D184)
- binding (2Z)-2-iminopentanedioic acid: K92 (= K108), G93 (= G109), G94 (= G110), Q113 (= Q129), K116 (= K132), K128 (= K144), A166 (= A182), R208 (= R223), V376 (= V393), S379 (= S396)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K136 (= K152), D168 (= D184), I169 (= I185), R208 (= R223), T212 (= T227), S241 (= S256), G242 (= G257), N243 (= N258), V244 (= V259), D264 (= D279), S265 (= S280), R290 (= R308), A321 (= A338), T322 (= T339), G345 (= G362), A346 (= A363), N347 (= N364), N372 (= N389)
5gudE Glutamate dehydrogenase from corynebacterium glutamicum (alpha- iminoglutarate/NADP+ complex) (see paper)
57% identity, 93% coverage: 33:464/464 of query aligns to 30:460/460 of 5gudE
- active site: K141 (= K144), D181 (= D184)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: T225 (= T227), S254 (= S256), G255 (= G257), N256 (= N258), V257 (= V259), D277 (= D279), S278 (= S280), R303 (= R308), A334 (= A338), T335 (= T339), A359 (= A363), N360 (= N364)
P24295 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Clostridium symbiosum (Bacteroides symbiosus) (see 4 papers)
52% identity, 94% coverage: 27:463/464 of query aligns to 9:448/450 of P24295
- K90 (= K108) 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 (= Q129) binding
- K114 (= K132) binding
- K126 (= K144) active site, Proton donor
- G165 (= G183) binding
- D166 (= D184) 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 (= S396) 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)
52% identity, 94% coverage: 27:463/464 of query aligns to 8:447/449 of 1bgvA
7f79C Crystal structure of glutamate dehydrogenase 3 from candida albicans in complex with alpha-ketoglutarate and NADPH (see paper)
51% identity, 94% coverage: 28:464/464 of query aligns to 1:457/458 of 7f79C
- binding 2-oxoglutaric acid: K79 (= K108), G80 (= G109), G81 (= G110), Q100 (= Q129), K103 (= K132), K115 (= K144), V380 (= V393), S383 (= S396)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R83 (= R112), H85 (= H114), K123 (= K152), D155 (= D184), I156 (= I185), R194 (= R223), T198 (= T227), S230 (= S256), G231 (= G257), N232 (= N258), V233 (= V259), D253 (= D279), S254 (= S280), K276 (= K302), A321 (= A338), T322 (= T339), G345 (= G362), S346 (≠ A363), N347 (= N364), N376 (= N389)
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)
54% identity, 92% coverage: 35:462/464 of query aligns to 5:448/454 of P00369
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
5xwcA Crystal structure of aspergillus niger glutamate dehydrogenase complexed with alpha-iminoglutarate, 2-amino-2-hydroxyglutarate and NADP (see paper)
53% identity, 92% coverage: 35:462/464 of query aligns to 4:456/459 of 5xwcA
- binding (2Z)-2-iminopentanedioic acid: K77 (= K108), G78 (= G109), Q98 (= Q129), K101 (= K132), K113 (= K144), A151 (= A182), R192 (= R223), V382 (= V393), S385 (= S396)
- binding (2S)-2-azanyl-2-oxidanyl-pentanedioic acid: K77 (= K108), G78 (= G109), G79 (= G110), Q98 (= Q129), K101 (= K132), K113 (= K144), A151 (= A182), D153 (= D184), R192 (= R223), V382 (= V393), S385 (= S396)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H83 (= H114), K121 (= K152), D153 (= D184), I154 (= I185), R192 (= R223), T196 (= T227), S228 (= S256), G229 (= G257), N230 (= N258), V231 (= V259), D251 (= D279), S252 (= S280), A319 (= A338), T320 (= T339), G343 (= G362), S344 (≠ A363), N345 (= N364), N378 (= N389)
5xw0A Crystal structure of aspergillus niger glutamate dehydrogenase complexed with isophthalate and NADPH (see paper)
53% identity, 92% coverage: 35:462/464 of query aligns to 4:456/459 of 5xw0A
- binding benzene-1,3-dicarboxylic acid: K77 (= K108), G78 (= G109), Q98 (= Q129), K101 (= K132), K113 (= K144), A151 (= A182), G152 (= G183), D153 (= D184), R192 (= R223), S385 (= S396)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H83 (= H114), K121 (= K152), D153 (= D184), I154 (= I185), R192 (= R223), T196 (= T227), S228 (= S256), G229 (= G257), N230 (= N258), V231 (= V259), D251 (= D279), S252 (= S280), A319 (= A338), T320 (= T339), G343 (= G362), S344 (≠ A363), N345 (= N364), N378 (= N389)
5xvxA Crystal structure of aspergillus niger glutamate dehydrogenase complexed with alpha-ketoglutarate and NADPH (see paper)
53% identity, 92% coverage: 35:462/464 of query aligns to 4:456/459 of 5xvxA
- binding 2-oxoglutaric acid: K77 (= K108), Q98 (= Q129), K101 (= K132), K113 (= K144), A151 (= A182), R192 (= R223), V382 (= V393), S385 (= S396)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K121 (= K152), D153 (= D184), I154 (= I185), R192 (= R223), T196 (= T227), S228 (= S256), G229 (= G257), N230 (= N258), V231 (= V259), D251 (= D279), S252 (= S280), A319 (= A338), T320 (= T339), G343 (= G362), S344 (≠ A363), N345 (= N364), N378 (= N389)
5xvvB Crystal structure of forward inhibited aspergillus niger glutamate dehydrogenase with both apo- and alpha ketoglutarate bound subunits (see paper)
53% identity, 92% coverage: 35:462/464 of query aligns to 4:456/459 of 5xvvB
7ecsA Crystal structure of aspergillus terreus glutamate dehydrogenase (atgdh) complexed with malonate and NADPH (see paper)
53% identity, 92% coverage: 35:462/464 of query aligns to 5:457/460 of 7ecsA
- binding malonate ion: G79 (= G109), G80 (= G110), Q99 (= Q129), K102 (= K132), K114 (= K144), S326 (≠ D344), G327 (≠ A345), E328 (≠ R346), T350 (= T368), A352 (≠ E370)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K122 (= K152), D154 (= D184), I155 (= I185), R193 (= R223), T197 (= T227), S229 (= S256), G230 (= G257), N231 (= N258), V232 (= V259), D252 (= D279), S253 (= S280), K279 (≠ M299), A320 (= A338), T321 (= T339), G344 (= G362), S345 (≠ A363), N346 (= N364), N379 (= N389)
7ecrA Crystal structure of aspergillus terreus glutamate dehydrogenase (atgdh) complexed with succinate and adp-ribose (see paper)
53% identity, 92% coverage: 35:462/464 of query aligns to 5:457/460 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 (= K152), D154 (= D184), I155 (= I185), S229 (= S256), G230 (= G257), N231 (= N258), V232 (= V259), D252 (= D279), S253 (= S280), K279 (≠ M299), A320 (= A338), T321 (= T339), G344 (= G362), S345 (≠ A363), N346 (= N364), N379 (= N389)
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)
51% identity, 93% coverage: 32:462/464 of query aligns to 1:448/451 of P78804
- S252 (= S280) modified: Phosphoserine
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction
37% identity, 86% coverage: 67:464/464 of query aligns to 25:414/416 of 8xcoA
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction
37% identity, 86% coverage: 67:464/464 of query aligns to 28:417/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K108), M90 (≠ Q129), K105 (= K144), A143 (= A182), D145 (= D184), S351 (= S396)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R112), D145 (= D184), V146 (≠ I185), Y147 (≠ G186), T191 (= T227), Y220 (≠ S256), G221 (= G257), N222 (= N258), A223 (≠ V259), D244 (= D279), S245 (= S280), K264 (= K302), N281 (≠ F320), A295 (≠ C337), A296 (= A338), I297 (≠ T339), N319 (= N364), N344 (= N389)
8xcsA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADPH, akg and nh4 in the initial stage of reaction
37% identity, 86% coverage: 67:464/464 of query aligns to 27:416/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (= K108), G70 (= G110), M89 (≠ Q129), K92 (= K132), K104 (= K144), A142 (= A182), D144 (= D184), G346 (= G392), S350 (= S396)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R112), K112 (= K152), P143 (≠ G183), D144 (= D184), V145 (≠ I185), Y146 (≠ G186), T190 (= T227), Y219 (≠ S256), G220 (= G257), N221 (= N258), A222 (≠ V259), D243 (= D279), S244 (= S280), K263 (= K302), A295 (= A338), I296 (≠ T339), N318 (= N364)
4xgiA Crystal structure of glutamate dehydrogenase from burkholderia thailandensis
35% identity, 83% coverage: 40:423/464 of query aligns to 17:376/416 of 4xgiA
- active site: K112 (= K144), D152 (= D184)
- binding 2-oxoglutaric acid: K76 (= K108), G78 (= G110), M97 (≠ Q129), K100 (= K132), K112 (= K144), A150 (= A182), R192 (= R223), S355 (= S396)
- binding nicotinamide-adenine-dinucleotide: R80 (= R112), D152 (= D184), V153 (≠ I185), T196 (= T227), G224 (= G255), G226 (= G257), N227 (= N258), V228 (= V259), D248 (= D279), H249 (≠ S280), A299 (≠ C337), A300 (= A338), A322 (= A363), N323 (= N364), N348 (= N389)
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)
33% identity, 86% coverage: 66:464/464 of query aligns to 38:424/424 of P39633
- E93 (≠ V121) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (= D150) 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 (≠ R172) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ G186) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (≠ Q261) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ G362) 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.
Query Sequence
>Ac3H11_315 FitnessBrowser__acidovorax_3H11:Ac3H11_315
MLQRAIACFFDTEGLPPMKHASAGSFLSHVALRNPGQPEFLQAVTEVMESLWPFIAEHPR
YAEHGLLERLVEPERIVMFRVSWVDDHGTVQVNRGYRIQHSMAIGPFKGGIRFHPSVNLS
VLKFLAFEQTFKNALTTLPMGGGKGGSDFDPKGRSPGEVMRFCQAFVSELFRHVGADTDV
PAGDIGVGGREVGFMAGMMKKLSNRADCVFTGKGLSFGGSLIRPEATGYGTVYFAQEMLR
ANGRSLDGLRVSVSGSGNVAQYAVEKALQLGAKVITVSDSSGTIVDEDGFTPEKLAILMD
VKNHHYGRVSDYAERTGVKFEAGVRPWHVPVDVALPCATQNELDARDAATLIKNGVVCVA
EGANMPSTIEAAKVFEAAGVLYAPGKASNAGGVATSGLEMSQNAARLAWPREEVDARLLQ
IMQGIHAACLRYGKHADGRVSYVDGANIAGFVKVADAMLAQGVV
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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