SitesBLAST
Comparing BPHYT_RS16705 FitnessBrowser__BFirm:BPHYT_RS16705 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)
4xgiA Crystal structure of glutamate dehydrogenase from burkholderia thailandensis
85% identity, 97% coverage: 16:437/437 of query aligns to 1:416/416 of 4xgiA
- active site: K112 (= K127), D152 (= D167)
- binding 2-oxoglutaric acid: K76 (= K91), G78 (= G93), M97 (= M112), K100 (= K115), K112 (= K127), A150 (= A165), R192 (= R207), S355 (= S370)
- binding nicotinamide-adenine-dinucleotide: R80 (= R95), D152 (= D167), V153 (= V168), T196 (= T211), G224 (= G239), G226 (= G241), N227 (= N242), V228 (= V243), D248 (= D263), H249 (= H264), A299 (= A314), A300 (= A315), A322 (= A337), N323 (= N338), N348 (= N363)
3aoeB Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
68% identity, 97% coverage: 14:437/437 of query aligns to 1:424/424 of 3aoeB
3aogA Crystal structure of glutamate dehydrogenase (gdhb) from thermus thermophilus (glu bound form)
68% identity, 96% coverage: 19:437/437 of query aligns to 4:421/421 of 3aogA
- active site: K111 (= K127), D151 (= D167)
- binding glutamic acid: A70 (≠ S86), G77 (= G93), M96 (= M112), K111 (= K127), P150 (= P166), D151 (= D167), D164 (= D180), M168 (= M184), S354 (= S370), R417 (= R433), G418 (= G434), L419 (= L435), Y420 (= Y436)
8xcsA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADPH, akg and nh4 in the initial stage of reaction
49% identity, 94% coverage: 25:434/437 of query aligns to 2:414/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (= K91), G70 (= G93), M89 (= M112), K92 (= K115), K104 (= K127), A142 (= A165), D144 (= D167), G346 (= G366), S350 (= S370)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R95), K112 (≠ R135), P143 (= P166), D144 (= D167), V145 (= V168), Y146 (≠ N169), T190 (= T211), Y219 (≠ F240), G220 (= G241), N221 (= N242), A222 (≠ V243), D243 (= D263), S244 (≠ H264), K263 (≠ V283), A295 (= A315), I296 (≠ L316), N318 (= N338)
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction
49% identity, 94% coverage: 25:434/437 of query aligns to 3:415/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K91), M90 (= M112), K105 (= K127), A143 (= A165), D145 (= D167), S351 (= S370)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R95), D145 (= D167), V146 (= V168), Y147 (≠ N169), T191 (= T211), Y220 (≠ F240), G221 (= G241), N222 (= N242), A223 (≠ V243), D244 (= D263), S245 (≠ H264), K264 (≠ V283), N281 (= N300), A295 (= A314), A296 (= A315), I297 (≠ L316), N319 (= N338), N344 (= N363)
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction
50% identity, 94% coverage: 26:434/437 of query aligns to 1:412/416 of 8xcoA
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)
48% identity, 90% coverage: 43:434/437 of query aligns to 32:422/424 of P39633
- E93 (= E104) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (= D133) 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 (≠ I155) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ N169) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (≠ G245) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ G336) 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)
49% identity, 90% coverage: 43:434/437 of query aligns to 32:425/427 of P50735
- VKA 97:99 (vs. gap) mutation Missing: In gudB1; gains glutamate dehydrogenase activity, restores growth on proline, arginine, ornithine.
8owmC Crystal structure of glutamate dehydrogenase 2 from arabidopsis thaliana binding ca, NAD and 2,2-dihydroxyglutarate (see paper)
45% identity, 92% coverage: 33:434/437 of query aligns to 13:410/413 of 8owmC
- binding calcium ion: S29 (≠ T52), I32 (≠ R55)
- binding nicotinamide-adenine-dinucleotide: D144 (= D167), M145 (≠ V168), R183 (= R207), T187 (= T211), F216 (= F240), G217 (= G241), N218 (= N242), V219 (= V243), D239 (= D263), I240 (≠ H264), C290 (≠ A314), A291 (= A315), A313 (= A337), N314 (= N338), N339 (= N363)
- binding 2,2-bis(oxidanyl)pentanedioic acid: K68 (= K91), G70 (= G93), M89 (= M112), K92 (= K115), K104 (= K127), A142 (= A165), R183 (= R207), N314 (= N338), V343 (= V367), S346 (= S370)
6yeiA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
46% identity, 92% coverage: 34:434/437 of query aligns to 8:407/409 of 6yeiA
- binding potassium ion: S26 (≠ T52), L27 (= L53), I29 (≠ R55), P30 (= P56)
- binding nicotinamide-adenine-dinucleotide: T184 (= T211), F213 (= F240), G214 (= G241), N215 (= N242), V216 (= V243), D236 (= D263), I237 (≠ H264), A288 (= A315), L289 (= L316), A310 (= A337), N311 (= N338), N336 (= N363)
6yeiF Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
46% identity, 92% coverage: 34:434/437 of query aligns to 9:408/410 of 6yeiF
- binding 2-oxoglutaric acid: K66 (= K91), G68 (= G93), M87 (= M112), K90 (= K115), K102 (= K127), A140 (= A165), V341 (= V367), S344 (= S370)
- binding potassium ion: S27 (≠ T52), L28 (= L53), I30 (≠ R55), P31 (= P56), F32 (≠ K57)
- binding nicotinamide-adenine-dinucleotide: R70 (= R95), D142 (= D167), M143 (≠ V168), T185 (= T211), F214 (= F240), G215 (= G241), N216 (= N242), V217 (= V243), D237 (= D263), I238 (≠ H264), A288 (= A314), A289 (= A315), A311 (= A337), N312 (= N338), N337 (= N363)
6yehA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in apo form (see paper)
46% identity, 92% coverage: 34:434/437 of query aligns to 8:407/410 of 6yehA
P28997 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Peptoniphilus asaccharolyticus (Peptostreptococcus asaccharolyticus) (see 2 papers)
45% identity, 95% coverage: 24:436/437 of query aligns to 3:421/421 of P28997
- E243 (vs. gap) Important for nucleotide recognition; mutation to D: Shows a 9-fold relaxation of the strong discrimination against NADPH due to the decrease of binding affinity for NADH and the increase for NADPH.; mutation to K: Severely crippled in its ability to bind to NADH. Decrease of binding affinity for NADH and increase for NADPH.; mutation to R: Decrease of binding affinity for NADH and increase for NADPH.
- W244 (vs. gap) mutation to S: Decrease of binding affinity for NADH and increase for NADPH.
- D245 (vs. gap) mutation to K: Decrease of binding affinity for NADH and increase for NADPH.
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)
44% identity, 92% coverage: 33:435/437 of query aligns to 15:419/420 of P80053
- K254 (≠ T272) modified: N6-methyllysine
- K260 (≠ A278) modified: N6-methyllysine
- K372 (≠ Q390) modified: N6-methyllysine
- K391 (≠ E409) modified: N6-methyllysine
- K392 (vs. gap) modified: N6-methyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylmethionine
1v9lA L-glutamate dehydrogenase from pyrobaculum islandicum complexed with NAD (see paper)
45% identity, 88% coverage: 51:434/437 of query aligns to 26:416/418 of 1v9lA
- active site: K102 (= K127), D142 (= D167)
- binding nicotinamide-adenine-dinucleotide: T186 (= T211), Q213 (= Q238), G216 (= G241), N217 (= N242), V218 (= V243), D238 (= D263), I239 (≠ H264), A296 (= A315), I297 (≠ L316), A318 (= A337), N319 (= N338), N344 (= N363)
3aoeF Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
41% identity, 96% coverage: 19:437/437 of query aligns to 3:417/417 of 3aoeF
P49448 Glutamate dehydrogenase 2, mitochondrial; GDH 2; EC 1.4.1.3 from Homo sapiens (Human) (see 2 papers)
44% identity, 76% coverage: 50:379/437 of query aligns to 106:447/558 of P49448
- C172 (≠ N116) modified: ADP-ribosylcysteine
Sites not aligning to the query:
- 1:53 modified: transit peptide, Mitochondrion
6dhmA Bovine glutamate dehydrogenase complexed with zinc (see paper)
44% identity, 76% coverage: 50:379/437 of query aligns to 49:390/495 of 6dhmA
- binding glutamic acid: K90 (= K91), G92 (= G93), M111 (= M112), K114 (= K115), A166 (= A165), D168 (= D167), R211 (= R207), V378 (= V367), S381 (= S370)
- binding guanosine-5'-triphosphate: H209 (≠ L205), S213 (≠ E209), H258 (≠ I246), R261 (= R249), Y262 (≠ L250), R265 (≠ E253), K289 (≠ V277), E292 (≠ L280)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: D168 (= D167), M169 (≠ V168), S170 (≠ N169), R211 (= R207), Q250 (= Q238), G251 (= G239), F252 (= F240), G253 (= G241), N254 (= N242), V255 (= V243), E275 (≠ D263), S276 (≠ H264), A326 (= A315), G347 (= G336), A348 (= A337), N349 (= N338), N374 (= N363)
- binding zinc ion: H209 (≠ L205)
Sites not aligning to the query:
8ar7A Bovine glutamate dehydrogenase in ternary complex with the allosteric activators adp and leucine (see paper)
44% identity, 76% coverage: 50:379/437 of query aligns to 45:386/496 of 8ar7A
- binding adenosine-5'-diphosphate: H81 (≠ S86), A112 (= A117), D115 (≠ N120), V116 (= V121), H205 (≠ L205), K383 (≠ Q376)
- binding potassium ion: I47 (≠ T52), I48 (≠ L53), K49 (= K54), P50 (≠ R55), C51 (≠ P56), N52 (≠ K57), H78 (= H83), S79 (≠ N84)
Sites not aligning to the query:
6dhlA Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ecg) (see paper)
44% identity, 76% coverage: 50:379/437 of query aligns to 44:385/496 of 6dhlA
- binding (2R,3S)-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate: H80 (≠ S86), R81 (= R87), C110 (≠ N116), D114 (≠ N120), V115 (= V121), K382 (≠ Q376)
Sites not aligning to the query:
Query Sequence
>BPHYT_RS16705 FitnessBrowser__BFirm:BPHYT_RS16705
MSSQQQAVQSASTLQSVPSYLNKDDLGPWGNYLRQVDRVAPYLGSLSRWLETLKRPKRIL
IVDVPIELDNGTVAHFEGYRVQHNVSRGPGKGGVRYHQDVTLSEVMALSAWMSVKNAAVN
VPYGGAKGGIRVDPRTLSRGELERVTRRYTSEIGIIIGPNTDIPAPDVNTNEQIMAWMMD
TYSMNQGQTATGVVTGKPITLGGSLGRREATGRGVFVTASEAARRIGVDIEGARIAVQGF
GNVGGIAARLFQEAGSKLVAVQDHTGSLYKSTGIDAVALLEHVAKTGGVGGFPEADSVTN
EEFWTVESDILIPAALENQITEKNASKIKTKIVVEGANGPTTTAADDILHDRGILVIPDV
VANAGGVTVSYFEWVQDFSSFFWTEDEINQRLERVMREAFAAVWQVSSEQKVSVRTAAFI
VACKRILEARELRGLYP
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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