SitesBLAST
Comparing BWI76_RS11610 FitnessBrowser__Koxy:BWI76_RS11610 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)
91% identity, 100% coverage: 1:447/447 of query aligns to 1:447/447 of P00370
- K92 (= K92) mutation to S: Complete loss of dehydrogenase activity.
- K128 (= K128) 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)
59% identity, 97% coverage: 16:447/447 of query aligns to 16:447/447 of 5gudA
- active site: K128 (= K128), D168 (= D168)
- binding (2Z)-2-iminopentanedioic acid: K92 (= K92), G93 (= G93), G94 (= G94), Q113 (= Q113), K116 (= K116), K128 (= K128), A166 (= A166), R208 (= R207), V376 (= V377), S379 (= S380)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K136 (= K136), D168 (= D168), I169 (= I169), R208 (= R207), T212 (= T211), S241 (= S240), G242 (= G241), N243 (= N242), V244 (= V243), D264 (= D263), S265 (= S264), R290 (= R292), A321 (= A322), T322 (= T323), G345 (= G346), A346 (= A347), N347 (= N348), N372 (= N373)
5gudE Glutamate dehydrogenase from corynebacterium glutamicum (alpha- iminoglutarate/NADP+ complex) (see paper)
59% identity, 97% coverage: 16:447/447 of query aligns to 29:460/460 of 5gudE
- active site: K141 (= K128), D181 (= D168)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: T225 (= T211), S254 (= S240), G255 (= G241), N256 (= N242), V257 (= V243), D277 (= D263), S278 (= S264), R303 (= R292), A334 (= A322), T335 (= T323), A359 (= A347), N360 (= N348)
5ijzA Crystal structure of glutamate dehydrogenase(gdh) from corynebacterium glutamicum (see paper)
59% identity, 97% coverage: 16:447/447 of query aligns to 16:447/447 of 5ijzA
- active site: K128 (= K128), D168 (= D168)
- binding 2-oxoglutaric acid: K92 (= K92), G93 (= G93), G94 (= G94), Q113 (= Q113), K116 (= K116), K128 (= K128), A166 (= A166), R208 (= R207), V376 (= V377), S379 (= S380)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K136 (= K136), D168 (= D168), I169 (= I169), T212 (= T211), S241 (= S240), G242 (= G241), N243 (= N242), V244 (= V243), D264 (= D263), S265 (= S264), R290 (= R292), A321 (= A322), T322 (= T323), A346 (= A347), N347 (= N348), N372 (= N373)
1bgvA Glutamate dehydrogenase (see paper)
53% identity, 98% coverage: 11:446/447 of query aligns to 8:447/449 of 1bgvA
P24295 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Clostridium symbiosum (Bacteroides symbiosus) (see 4 papers)
53% identity, 98% coverage: 11:446/447 of query aligns to 9:448/450 of P24295
- K90 (= K92) 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 (= Q113) binding
- K114 (= K116) binding
- K126 (= K128) active site, Proton donor
- G165 (= G167) binding
- D166 (= D168) 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
7ecsA Crystal structure of aspergillus terreus glutamate dehydrogenase (atgdh) complexed with malonate and NADPH (see paper)
55% identity, 96% coverage: 19:445/447 of query aligns to 5:457/460 of 7ecsA
- binding malonate ion: G79 (= G93), G80 (= G94), Q99 (= Q113), K102 (= K116), K114 (= K128), S326 (≠ D328), G327 (≠ V329), E328 (≠ D330), T350 (= T352), A352 (= A354)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K122 (= K136), D154 (= D168), I155 (= I169), R193 (= R207), T197 (= T211), S229 (= S240), G230 (= G241), N231 (= N242), V232 (= V243), D252 (= D263), S253 (= S264), K279 (≠ L282), 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)
55% identity, 96% coverage: 19:445/447 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 (= K136), D154 (= D168), I155 (= I169), S229 (= S240), G230 (= G241), N231 (= N242), V232 (= V243), D252 (= D263), S253 (= S264), K279 (≠ L282), A320 (= A322), T321 (= T323), G344 (= G346), S345 (≠ A347), N346 (= N348), N379 (= N373)
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: 19:445/447 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)
55% identity, 96% coverage: 19:445/447 of query aligns to 4:456/459 of 5xwcA
- binding (2Z)-2-iminopentanedioic acid: K77 (= K92), G78 (= G93), Q98 (= Q113), K101 (= K116), K113 (= K128), A151 (= A166), R192 (= R207), V382 (= V377), S385 (= S380)
- binding (2S)-2-azanyl-2-oxidanyl-pentanedioic acid: K77 (= K92), G78 (= G93), G79 (= G94), Q98 (= Q113), K101 (= K116), K113 (= K128), A151 (= A166), D153 (= D168), R192 (= R207), V382 (= V377), S385 (= S380)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H83 (= H98), K121 (= K136), D153 (= D168), I154 (= I169), R192 (= R207), T196 (= T211), S228 (= S240), G229 (= G241), N230 (= N242), V231 (= V243), D251 (= D263), S252 (= S264), 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)
55% identity, 96% coverage: 19:445/447 of query aligns to 4:456/459 of 5xw0A
- binding benzene-1,3-dicarboxylic acid: K77 (= K92), G78 (= G93), Q98 (= Q113), K101 (= K116), K113 (= K128), A151 (= A166), G152 (= G167), D153 (= D168), R192 (= R207), S385 (= S380)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H83 (= H98), K121 (= K136), D153 (= D168), I154 (= I169), R192 (= R207), T196 (= T211), S228 (= S240), G229 (= G241), N230 (= N242), V231 (= V243), D251 (= D263), S252 (= S264), 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)
55% identity, 96% coverage: 19:445/447 of query aligns to 4:456/459 of 5xvxA
- binding 2-oxoglutaric acid: K77 (= K92), Q98 (= Q113), K101 (= K116), K113 (= K128), A151 (= A166), R192 (= R207), V382 (= V377), S385 (= S380)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K121 (= K136), D153 (= D168), I154 (= I169), R192 (= R207), T196 (= T211), S228 (= S240), G229 (= G241), N230 (= N242), V231 (= V243), D251 (= D263), S252 (= S264), 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)
55% identity, 96% coverage: 19:445/447 of query aligns to 4:456/459 of 5xvvB
7f79C Crystal structure of glutamate dehydrogenase 3 from candida albicans in complex with alpha-ketoglutarate and NADPH (see paper)
51% identity, 96% coverage: 19:445/447 of query aligns to 6:455/458 of 7f79C
- binding 2-oxoglutaric acid: K79 (= K92), G80 (= G93), G81 (= G94), Q100 (= Q113), K103 (= K116), K115 (= K128), V380 (= V377), S383 (= S380)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R83 (= R96), H85 (= H98), K123 (= K136), D155 (= D168), I156 (= I169), R194 (= R207), T198 (= T211), S230 (= S240), G231 (= G241), N232 (= N242), V233 (= V243), D253 (= D263), S254 (= S264), K276 (vs. gap), A321 (= A322), T322 (= T323), G345 (= G346), S346 (≠ A347), N347 (= N348), N376 (= N373)
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)
50% identity, 96% coverage: 19:445/447 of query aligns to 4:448/451 of P78804
- S252 (= S264) modified: Phosphoserine
3aogA Crystal structure of glutamate dehydrogenase (gdhb) from thermus thermophilus (glu bound form)
39% identity, 84% coverage: 46:421/447 of query aligns to 29:395/421 of 3aogA
Sites not aligning to the query:
3aoeB Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
39% identity, 84% coverage: 46:421/447 of query aligns to 32:398/424 of 3aoeB
Sites not aligning to the query:
4xgiA Crystal structure of glutamate dehydrogenase from burkholderia thailandensis
36% identity, 83% coverage: 37:406/447 of query aligns to 26:375/416 of 4xgiA
- active site: K112 (= K128), D152 (= D168)
- binding 2-oxoglutaric acid: K76 (= K92), G78 (= G94), M97 (≠ Q113), K100 (= K116), K112 (= K128), A150 (= A166), R192 (= R207), S355 (= S380)
- binding nicotinamide-adenine-dinucleotide: R80 (= R96), D152 (= D168), V153 (≠ I169), T196 (= T211), G224 (= G239), G226 (= G241), N227 (= N242), V228 (= V243), D248 (= D263), H249 (≠ S264), A299 (≠ C321), A300 (= A322), A322 (= A347), N323 (= N348), N348 (= N373)
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)
32% identity, 89% coverage: 51:447/447 of query aligns to 32:420/420 of P80053
- K254 (≠ A272) modified: N6-methyllysine
- K260 (≠ R281) modified: N6-methyllysine
- K372 (≠ A400) modified: N6-methyllysine
- K391 (≠ E419) modified: N6-methyllysine
- K392 (≠ A420) modified: N6-methyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylmethionine
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction
36% identity, 80% coverage: 51:406/447 of query aligns to 28:377/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K92), M90 (≠ Q113), K105 (= K128), A143 (= A166), D145 (= D168), S351 (= S380)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R96), D145 (= D168), V146 (≠ I169), Y147 (≠ G170), T191 (= T211), Y220 (≠ S240), G221 (= G241), N222 (= N242), A223 (≠ V243), D244 (= D263), S245 (= S264), K264 (≠ E287), N281 (≠ G307), A295 (≠ C321), A296 (= A322), I297 (≠ T323), N319 (= N348), N344 (= N373)
Query Sequence
>BWI76_RS11610 FitnessBrowser__Koxy:BWI76_RS11610
MDQTCTLEGFLARVQQRDPNQTEFAQAVREVMTTLWPFLEENPRYRQMNLLERLVEPERA
IQFRVVWVDDRNQVQVNRAWRVQFNSAIGPYKGGMRFHPSVNLSILKFLGFEQTFKNALT
TLPMGGGKGGSDFDPKGKSDGEVMRFCQALMTELYRHLGPDTDVPAGDIGVGGREVGFMA
GMMRKLSNNSACVFTGKGLSFGGSLIRPEATGYGLIYFTEAMLKRHGLGFEGARVAVSGS
GNVAQYAIEKAMELGARVITASDSNGTVVDEAGFTKEKLARLIDIKERSHGRVADYAREF
GLTYLEGKQPWSVPVDIALPCATQNELDVDAARQLIANGVKAVAEGANMPTTIAATDLFL
EAGVLFAPGKAANAGGVATSGLEMAQNAARMGWKAEKVDARLHHIMLDIHHACVEYGGEA
KQTNYVRGANIAGFVKVADAMLAQGVI
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