SitesBLAST
Comparing GFF3373 FitnessBrowser__psRCH2:GFF3373 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)
65% identity, 99% coverage: 4:445/445 of query aligns to 6:447/447 of P00370
- K92 (= K90) mutation to S: Complete loss of dehydrogenase activity.
- K128 (= K126) 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.
5gudA Glutamate dehydrogenase from corynebacterium glutamicum (alpha- iminoglutarate/NADP+ complex) (see paper)
62% identity, 100% coverage: 3:445/445 of query aligns to 5:447/447 of 5gudA
- active site: K128 (= K126), D168 (= D166)
- binding (2Z)-2-iminopentanedioic acid: K92 (= K90), G93 (= G91), G94 (= G92), Q113 (= Q111), K116 (= K114), K128 (= K126), A166 (= A164), R208 (= R205), V376 (= V375), S379 (= S378)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K136 (= K134), D168 (= D166), I169 (= I167), R208 (= R205), T212 (= T209), S241 (= S238), G242 (= G239), N243 (= N240), V244 (= V241), D264 (= D261), S265 (= S262), R290 (= R290), A321 (= A320), T322 (= T321), G345 (= G344), A346 (= A345), N347 (= N346), N372 (= N371)
5ijzA Crystal structure of glutamate dehydrogenase(gdh) from corynebacterium glutamicum (see paper)
62% identity, 100% coverage: 3:445/445 of query aligns to 5:447/447 of 5ijzA
- active site: K128 (= K126), D168 (= D166)
- binding 2-oxoglutaric acid: K92 (= K90), G93 (= G91), G94 (= G92), Q113 (= Q111), K116 (= K114), K128 (= K126), A166 (= A164), R208 (= R205), V376 (= V375), S379 (= S378)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K136 (= K134), D168 (= D166), I169 (= I167), T212 (= T209), S241 (= S238), G242 (= G239), N243 (= N240), V244 (= V241), D264 (= D261), S265 (= S262), R290 (= R290), A321 (= A320), T322 (= T321), A346 (= A345), N347 (= N346), N372 (= N371)
5gudE Glutamate dehydrogenase from corynebacterium glutamicum (alpha- iminoglutarate/NADP+ complex) (see paper)
62% identity, 100% coverage: 3:445/445 of query aligns to 18:460/460 of 5gudE
- active site: K141 (= K126), D181 (= D166)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: T225 (= T209), S254 (= S238), G255 (= G239), N256 (= N240), V257 (= V241), D277 (= D261), S278 (= S262), R303 (= R290), A334 (= A320), T335 (= T321), A359 (= A345), N360 (= N346)
P24295 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Clostridium symbiosum (Bacteroides symbiosus) (see 4 papers)
53% identity, 100% coverage: 1:444/445 of query aligns to 1:448/450 of P24295
- M1 (= M1) modified: Initiator methionine, Removed
- K90 (= K90) 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 (= Q111) binding
- K114 (= K114) binding
- K126 (= K126) active site, Proton donor
- G165 (= G165) binding
- D166 (= D166) 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 (= S378) binding ; mutation to V: Dramatic reduction in the dehydrogenase activity with glutamate as the substrate; when associated with L-90.
1bgvA Glutamate dehydrogenase (see paper)
53% identity, 99% coverage: 5:444/445 of query aligns to 4:447/449 of 1bgvA
7f79C Crystal structure of glutamate dehydrogenase 3 from candida albicans in complex with alpha-ketoglutarate and NADPH (see paper)
56% identity, 96% coverage: 17:445/445 of query aligns to 6:457/458 of 7f79C
- binding 2-oxoglutaric acid: K79 (= K90), G80 (= G91), G81 (= G92), Q100 (= Q111), K103 (= K114), K115 (= K126), V380 (= V375), S383 (= S378)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R83 (= R94), H85 (= H96), K123 (= K134), D155 (= D166), I156 (= I167), R194 (= R205), T198 (= T209), S230 (= S238), G231 (= G239), N232 (= N240), V233 (= V241), D253 (= D261), S254 (= S262), K276 (≠ N285), A321 (= A320), T322 (= T321), G345 (= G344), S346 (≠ A345), N347 (= N346), N376 (= N371)
5xwcA Crystal structure of aspergillus niger glutamate dehydrogenase complexed with alpha-iminoglutarate, 2-amino-2-hydroxyglutarate and NADP (see paper)
55% identity, 96% coverage: 17:443/445 of query aligns to 4:456/459 of 5xwcA
- binding (2Z)-2-iminopentanedioic acid: K77 (= K90), G78 (= G91), Q98 (= Q111), K101 (= K114), K113 (= K126), A151 (= A164), R192 (= R205), V382 (= V375), S385 (= S378)
- binding (2S)-2-azanyl-2-oxidanyl-pentanedioic acid: K77 (= K90), G78 (= G91), G79 (= G92), Q98 (= Q111), K101 (= K114), K113 (= K126), A151 (= A164), D153 (= D166), R192 (= R205), V382 (= V375), S385 (= S378)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H83 (= H96), K121 (= K134), D153 (= D166), I154 (= I167), R192 (= R205), T196 (= T209), S228 (= S238), G229 (= G239), N230 (= N240), V231 (= V241), D251 (= D261), S252 (= S262), A319 (= A320), T320 (= T321), G343 (= G344), S344 (≠ A345), N345 (= N346), N378 (= N371)
5xw0A Crystal structure of aspergillus niger glutamate dehydrogenase complexed with isophthalate and NADPH (see paper)
55% identity, 96% coverage: 17:443/445 of query aligns to 4:456/459 of 5xw0A
- binding benzene-1,3-dicarboxylic acid: K77 (= K90), G78 (= G91), Q98 (= Q111), K101 (= K114), K113 (= K126), A151 (= A164), G152 (= G165), D153 (= D166), R192 (= R205), S385 (= S378)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H83 (= H96), K121 (= K134), D153 (= D166), I154 (= I167), R192 (= R205), T196 (= T209), S228 (= S238), G229 (= G239), N230 (= N240), V231 (= V241), D251 (= D261), S252 (= S262), A319 (= A320), T320 (= T321), G343 (= G344), S344 (≠ A345), N345 (= N346), N378 (= N371)
5xvxA Crystal structure of aspergillus niger glutamate dehydrogenase complexed with alpha-ketoglutarate and NADPH (see paper)
55% identity, 96% coverage: 17:443/445 of query aligns to 4:456/459 of 5xvxA
- binding 2-oxoglutaric acid: K77 (= K90), Q98 (= Q111), K101 (= K114), K113 (= K126), A151 (= A164), R192 (= R205), V382 (= V375), S385 (= S378)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K121 (= K134), D153 (= D166), I154 (= I167), R192 (= R205), T196 (= T209), S228 (= S238), G229 (= G239), N230 (= N240), V231 (= V241), D251 (= D261), S252 (= S262), A319 (= A320), T320 (= T321), G343 (= G344), S344 (≠ A345), N345 (= N346), N378 (= N371)
5xvvB Crystal structure of forward inhibited aspergillus niger glutamate dehydrogenase with both apo- and alpha ketoglutarate bound subunits (see paper)
55% identity, 96% coverage: 17:443/445 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)
56% identity, 96% coverage: 17:443/445 of query aligns to 5:457/460 of 7ecsA
- binding malonate ion: G79 (= G91), G80 (= G92), Q99 (= Q111), K102 (= K114), K114 (= K126), S326 (≠ D326), G327 (= G327), E328 (= E328), T350 (= T350), A352 (≠ E352)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K122 (= K134), D154 (= D166), I155 (= I167), R193 (= R205), T197 (= T209), S229 (= S238), G230 (= G239), N231 (= N240), V232 (= V241), D252 (= D261), S253 (= S262), K279 (= K284), A320 (= A320), T321 (= T321), G344 (= G344), S345 (≠ A345), N346 (= N346), N379 (= N371)
7ecrA Crystal structure of aspergillus terreus glutamate dehydrogenase (atgdh) complexed with succinate and adp-ribose (see paper)
56% identity, 96% coverage: 17:443/445 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 (= K134), D154 (= D166), I155 (= I167), S229 (= S238), G230 (= G239), N231 (= N240), V232 (= V241), D252 (= D261), S253 (= S262), K279 (= K284), A320 (= A320), T321 (= T321), G344 (= G344), S345 (≠ A345), N346 (= N346), N379 (= N371)
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)
55% identity, 96% coverage: 17:443/445 of query aligns to 5:448/454 of P00369
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
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)
52% identity, 96% coverage: 17:443/445 of query aligns to 4:448/451 of P78804
- S252 (= S262) modified: Phosphoserine
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)
32% identity, 89% coverage: 50:445/445 of query aligns to 40:424/424 of P39633
- E93 (≠ V103) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (≠ N132) 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 (≠ R154) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ G168) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (≠ Q243) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ G344) 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.
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction
33% identity, 92% coverage: 37:445/445 of query aligns to 14:417/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K90), M90 (≠ Q111), K105 (= K126), A143 (= A164), D145 (= D166), S351 (= S378)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R94), D145 (= D166), V146 (≠ I167), Y147 (≠ G168), T191 (= T209), Y220 (≠ S238), G221 (= G239), N222 (= N240), A223 (≠ V241), D244 (= D261), S245 (= S262), K264 (= K284), N281 (≠ D305), A295 (≠ C319), A296 (= A320), I297 (≠ T321), N319 (= N346), N344 (= N371)
8xcsA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADPH, akg and nh4 in the initial stage of reaction
33% identity, 92% coverage: 37:445/445 of query aligns to 13:416/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (= K90), G70 (= G92), M89 (≠ Q111), K92 (= K114), K104 (= K126), A142 (= A164), D144 (= D166), G346 (= G374), S350 (= S378)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R94), K112 (= K134), P143 (≠ G165), D144 (= D166), V145 (≠ I167), Y146 (≠ G168), T190 (= T209), Y219 (≠ S238), G220 (= G239), N221 (= N240), A222 (≠ V241), D243 (= D261), S244 (= S262), K263 (= K284), A295 (= A320), I296 (≠ T321), N318 (= N346)
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction
33% identity, 92% coverage: 37:445/445 of query aligns to 11:414/416 of 8xcoA
P50735 Cryptic catabolic NAD-specific glutamate dehydrogenase GudB; NAD-GDH; EC 1.4.1.2 from Bacillus subtilis (strain 168) (see paper)
32% identity, 89% coverage: 48:443/445 of query aligns to 38:425/427 of P50735
- VKA 97:99 (≠ LKF 104:106) mutation Missing: In gudB1; gains glutamate dehydrogenase activity, restores growth on proline, arginine, ornithine.
Query Sequence
>GFF3373 FitnessBrowser__psRCH2:GFF3373
MIETVDAFLARLKQRDPHQPEFHQAVEEVVRSLWPFLEAHPHYMQAGIIERMVEPERAII
FRVPWVDDQGRVQVNRGFRIQMNSAIGPYKGGLRFHPSVNIGVLKFLAFEQVFKNSLTSL
PMGGGKGGSDFNPKGKSDNEVMRFCQSFMSELYRHIGADLDVPAGDIGVGGREIGFLFGQ
YKRLSNQFTSVLTGKGLPYGGSLIRPEATGYGCVYFAEEMLKSTHSSFEGKRVSISGSGN
VAQYAAQKVMELGGRVISLSDSGGTLHFPDGLTGEQWDYLMDLKNVRRGRLEEMGAHFGV
TYLADQRPWSLPCDIALPCATQNELDGEDARMLLKNGCVCVAEGANMPSTLEAVDLFLEA
GILYAPGKASNAGGVACSGLEMSQNAMRLHWTAGEVDTKLHSIMQSIHHACVAHGEENGR
INYVKGANIAGFVKVADAMLAQGVV
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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