SitesBLAST
Comparing 351501 FitnessBrowser__Btheta:351501 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)
P24295 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Clostridium symbiosum (Bacteroides symbiosus) (see 4 papers)
57% identity, 99% coverage: 3:444/445 of query aligns to 5:448/450 of P24295
- K90 (= K88) 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 (= Q109) binding
- K114 (= K112) binding
- K126 (= K124) active site, Proton donor
- G165 (= G163) binding
- D166 (= D164) 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 (= S377) 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)
57% identity, 99% coverage: 3:444/445 of query aligns to 4:447/449 of 1bgvA
P00370 NADP-specific glutamate dehydrogenase; NADP-GDH; EC 1.4.1.4 from Escherichia coli (strain K12) (see 2 papers)
57% identity, 100% coverage: 2:445/445 of query aligns to 6:447/447 of P00370
- K92 (= K88) mutation to S: Complete loss of dehydrogenase activity.
- K128 (= K124) 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)
54% identity, 98% coverage: 10:445/445 of query aligns to 14:447/447 of 5ijzA
- active site: K128 (= K124), D168 (= D164)
- binding 2-oxoglutaric acid: K92 (= K88), G93 (= G89), G94 (= G90), Q113 (= Q109), K116 (= K112), K128 (= K124), A166 (= A162), R208 (= R203), V376 (= V374), S379 (= S377)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K136 (≠ R132), D168 (= D164), I169 (= I165), T212 (= T207), S241 (≠ F236), G242 (= G237), N243 (= N238), V244 (= V239), D264 (≠ G259), S265 (≠ P260), R290 (≠ G285), A321 (= A319), T322 (= T320), A346 (≠ S344), N347 (= N345), N372 (= N370)
5gudA Glutamate dehydrogenase from corynebacterium glutamicum (alpha- iminoglutarate/NADP+ complex) (see paper)
54% identity, 98% coverage: 10:445/445 of query aligns to 14:447/447 of 5gudA
- active site: K128 (= K124), D168 (= D164)
- binding (2Z)-2-iminopentanedioic acid: K92 (= K88), G93 (= G89), G94 (= G90), Q113 (= Q109), K116 (= K112), K128 (= K124), A166 (= A162), R208 (= R203), V376 (= V374), S379 (= S377)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K136 (≠ R132), D168 (= D164), I169 (= I165), R208 (= R203), T212 (= T207), S241 (≠ F236), G242 (= G237), N243 (= N238), V244 (= V239), D264 (≠ G259), S265 (≠ P260), R290 (≠ G285), A321 (= A319), T322 (= T320), G345 (≠ I343), A346 (≠ S344), N347 (= N345), N372 (= N370)
5gudE Glutamate dehydrogenase from corynebacterium glutamicum (alpha- iminoglutarate/NADP+ complex) (see paper)
54% identity, 98% coverage: 10:445/445 of query aligns to 27:460/460 of 5gudE
- active site: K141 (= K124), D181 (= D164)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: T225 (= T207), S254 (≠ F236), G255 (= G237), N256 (= N238), V257 (= V239), D277 (≠ G259), S278 (≠ P260), R303 (≠ G285), A334 (= A319), T335 (= T320), A359 (≠ S344), N360 (= N345)
7ecsA Crystal structure of aspergillus terreus glutamate dehydrogenase (atgdh) complexed with malonate and NADPH (see paper)
53% identity, 96% coverage: 15:443/445 of query aligns to 5:457/460 of 7ecsA
- binding malonate ion: G79 (= G89), G80 (= G90), Q99 (= Q109), K102 (= K112), K114 (= K124), S326 (≠ N325), G327 (= G326), E328 (= E327), T350 (= T349), A352 (≠ E351)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K122 (≠ R132), D154 (= D164), I155 (= I165), R193 (= R203), T197 (= T207), S229 (≠ F236), G230 (= G237), N231 (= N238), V232 (= V239), D252 (≠ G259), S253 (≠ P260), K279 (≠ R282), A320 (= A319), T321 (= T320), G344 (≠ I343), S345 (= S344), N346 (= N345), N379 (= N370)
7ecrA Crystal structure of aspergillus terreus glutamate dehydrogenase (atgdh) complexed with succinate and adp-ribose (see paper)
53% identity, 96% coverage: 15:443/445 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 (≠ R132), D154 (= D164), I155 (= I165), S229 (≠ F236), G230 (= G237), N231 (= N238), V232 (= V239), D252 (≠ G259), S253 (≠ P260), K279 (≠ R282), A320 (= A319), T321 (= T320), G344 (≠ I343), S345 (= S344), N346 (= N345), N379 (= N370)
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)
52% identity, 96% coverage: 15:443/445 of query aligns to 5:448/454 of P00369
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
7f79C Crystal structure of glutamate dehydrogenase 3 from candida albicans in complex with alpha-ketoglutarate and NADPH (see paper)
51% identity, 96% coverage: 15:443/445 of query aligns to 6:455/458 of 7f79C
- binding 2-oxoglutaric acid: K79 (= K88), G80 (= G89), G81 (= G90), Q100 (= Q109), K103 (= K112), K115 (= K124), V380 (= V374), S383 (= S377)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R83 (= R92), H85 (= H94), K123 (≠ R132), D155 (= D164), I156 (= I165), R194 (= R203), T198 (= T207), S230 (≠ F236), G231 (= G237), N232 (= N238), V233 (= V239), D253 (≠ G259), S254 (≠ P260), K276 (≠ R282), A321 (= A319), T322 (= T320), G345 (≠ I343), S346 (= S344), N347 (= N345), N376 (= N370)
5xwcA Crystal structure of aspergillus niger glutamate dehydrogenase complexed with alpha-iminoglutarate, 2-amino-2-hydroxyglutarate and NADP (see paper)
51% identity, 96% coverage: 15:443/445 of query aligns to 4:456/459 of 5xwcA
- binding (2Z)-2-iminopentanedioic acid: K77 (= K88), G78 (= G89), Q98 (= Q109), K101 (= K112), K113 (= K124), A151 (= A162), R192 (= R203), V382 (= V374), S385 (= S377)
- binding (2S)-2-azanyl-2-oxidanyl-pentanedioic acid: K77 (= K88), G78 (= G89), G79 (= G90), Q98 (= Q109), K101 (= K112), K113 (= K124), A151 (= A162), D153 (= D164), R192 (= R203), V382 (= V374), S385 (= S377)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H83 (= H94), K121 (≠ R132), D153 (= D164), I154 (= I165), R192 (= R203), T196 (= T207), S228 (≠ F236), G229 (= G237), N230 (= N238), V231 (= V239), D251 (≠ G259), S252 (≠ P260), A319 (= A319), T320 (= T320), G343 (≠ I343), S344 (= S344), N345 (= N345), N378 (= N370)
5xw0A Crystal structure of aspergillus niger glutamate dehydrogenase complexed with isophthalate and NADPH (see paper)
51% identity, 96% coverage: 15:443/445 of query aligns to 4:456/459 of 5xw0A
- binding benzene-1,3-dicarboxylic acid: K77 (= K88), G78 (= G89), Q98 (= Q109), K101 (= K112), K113 (= K124), A151 (= A162), G152 (= G163), D153 (= D164), R192 (= R203), S385 (= S377)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H83 (= H94), K121 (≠ R132), D153 (= D164), I154 (= I165), R192 (= R203), T196 (= T207), S228 (≠ F236), G229 (= G237), N230 (= N238), V231 (= V239), D251 (≠ G259), S252 (≠ P260), A319 (= A319), T320 (= T320), G343 (≠ I343), S344 (= S344), N345 (= N345), N378 (= N370)
5xvxA Crystal structure of aspergillus niger glutamate dehydrogenase complexed with alpha-ketoglutarate and NADPH (see paper)
51% identity, 96% coverage: 15:443/445 of query aligns to 4:456/459 of 5xvxA
- binding 2-oxoglutaric acid: K77 (= K88), Q98 (= Q109), K101 (= K112), K113 (= K124), A151 (= A162), R192 (= R203), V382 (= V374), S385 (= S377)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K121 (≠ R132), D153 (= D164), I154 (= I165), R192 (= R203), T196 (= T207), S228 (≠ F236), G229 (= G237), N230 (= N238), V231 (= V239), D251 (≠ G259), S252 (≠ P260), A319 (= A319), T320 (= T320), G343 (≠ I343), S344 (= S344), N345 (= N345), N378 (= N370)
5xvvB Crystal structure of forward inhibited aspergillus niger glutamate dehydrogenase with both apo- and alpha ketoglutarate bound subunits (see paper)
51% identity, 96% coverage: 15:443/445 of query aligns to 4:456/459 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)
51% identity, 96% coverage: 15:443/445 of query aligns to 4:448/451 of P78804
- S252 (≠ P260) modified: Phosphoserine
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction
34% identity, 90% coverage: 47:445/445 of query aligns to 28:417/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K88), M90 (≠ Q109), K105 (= K124), A143 (= A162), D145 (= D164), S351 (= S377)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R92), D145 (= D164), V146 (≠ I165), Y147 (≠ G166), T191 (= T207), Y220 (≠ F236), G221 (= G237), N222 (= N238), A223 (≠ V239), D244 (≠ G259), S245 (≠ P260), K264 (≠ L279), N281 (≠ G304), A295 (≠ C318), A296 (= A319), I297 (≠ T320), N319 (= N345), N344 (= N370)
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction
34% identity, 90% coverage: 47:445/445 of query aligns to 25:414/416 of 8xcoA
8xcsA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADPH, akg and nh4 in the initial stage of reaction
34% identity, 90% coverage: 47:445/445 of query aligns to 27:416/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (= K88), G70 (= G90), M89 (≠ Q109), K92 (= K112), K104 (= K124), A142 (= A162), D144 (= D164), G346 (= G373), S350 (= S377)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R92), K112 (≠ R132), P143 (≠ G163), D144 (= D164), V145 (≠ I165), Y146 (≠ G166), T190 (= T207), Y219 (≠ F236), G220 (= G237), N221 (= N238), A222 (≠ V239), D243 (≠ G259), S244 (≠ P260), K263 (≠ L279), A295 (= A319), I296 (≠ T320), N318 (= N345)
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, 89% coverage: 48:443/445 of query aligns to 40:422/424 of P39633
- E93 (≠ I101) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (≠ S130) 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 (≠ R152) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ G166) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (≠ W241) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ I343) 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.
P50735 Cryptic catabolic NAD-specific glutamate dehydrogenase GudB; NAD-GDH; EC 1.4.1.2 from Bacillus subtilis (strain 168) (see paper)
33% identity, 82% coverage: 26:391/445 of query aligns to 16:375/427 of P50735
- VKA 97:99 (≠ LKF 102:104) mutation Missing: In gudB1; gains glutamate dehydrogenase activity, restores growth on proline, arginine, ornithine.
Query Sequence
>351501 FitnessBrowser__Btheta:351501
MNIQKIMSSLEAKHPGELEYLQAVKEVLLSIEDIYNQHPEFEKVKIIERLVEPDRIFTFR
VTWVDDKGEVQTNLGYRVQFNNAIGPYKGGIRFHASVNLSILKFLGFEQTFKNALTTLPM
GGGKGGSDFSPRGKSDAEIMRFCQAFMLELWRHLGPDMDVPAGDIGVGGREVGYMFGMYK
KLTREFTGTFTGKGLEFGGSLIRPEATGFGGLYFVYQMLQAKNIDIKGKTVAISGFGNVA
WGAATKATELGAKVITISGPDGYIYDPDGISGEKIDYMLELRASGNDIVAPYAEKYPGAT
FVEGKRPWEVKADIALPCATQNELNGEDAQNLIKNNVLCIGEISNMGCTPEAIDLFIEKK
IMYAPGKAVNAGGVATSGLEMSQNAMHLSWSAAEVDEKLHAIMHGIHAQCVKYGTEPDGY
INYVKGANIAGFMKVAHAMMGQGVI
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