SitesBLAST
Comparing RR42_RS02570 FitnessBrowser__Cup4G11:RR42_RS02570 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)
4xgiA Crystal structure of glutamate dehydrogenase from burkholderia thailandensis
75% identity, 97% coverage: 15:435/435 of query aligns to 1:416/416 of 4xgiA
- active site: K112 (= K126), D152 (= D166)
- binding 2-oxoglutaric acid: K76 (= K90), G78 (= G92), M97 (= M111), K100 (= K114), K112 (= K126), A150 (= A164), R192 (= R206), S355 (= S368)
- binding nicotinamide-adenine-dinucleotide: R80 (= R94), D152 (= D166), V153 (= V167), T196 (= T210), G224 (= G238), G226 (= G240), N227 (= N241), V228 (= V242), D248 (= D262), H249 (= H263), A299 (= A312), A300 (= A313), A322 (= A335), N323 (= N336), N348 (= N361)
3aoeB Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
65% identity, 96% coverage: 18:435/435 of query aligns to 7:424/424 of 3aoeB
3aogA Crystal structure of glutamate dehydrogenase (gdhb) from thermus thermophilus (glu bound form)
65% identity, 96% coverage: 18:435/435 of query aligns to 4:421/421 of 3aogA
- active site: K111 (= K126), D151 (= D166)
- binding glutamic acid: A70 (≠ S85), G77 (= G92), M96 (= M111), K111 (= K126), P150 (= P165), D151 (= D166), D164 (= D179), M168 (= M183), S354 (= S368), R417 (= R431), G418 (= G432), L419 (= L433), Y420 (= Y434)
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)
49% identity, 90% coverage: 42:432/435 of query aligns to 32:422/424 of P39633
- E93 (= E103) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (= D132) 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 (≠ F154) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ N168) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (≠ A244) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ G334) 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
49% identity, 94% coverage: 25:432/435 of query aligns to 4:415/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K90), M90 (= M111), K105 (= K126), A143 (= A164), D145 (= D166), S351 (= S368)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R94), D145 (= D166), V146 (= V167), Y147 (≠ N168), T191 (= T210), Y220 (≠ F239), G221 (= G240), N222 (= N241), A223 (≠ V242), D244 (= D262), S245 (≠ H263), K264 (≠ A282), N281 (≠ A298), A295 (= A312), A296 (= A313), I297 (≠ L314), N319 (= N336), N344 (= N361)
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: 25:432/435 of query aligns to 3:414/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (= K90), G70 (= G92), M89 (= M111), K92 (= K114), K104 (= K126), A142 (= A164), D144 (= D166), G346 (= G364), S350 (= S368)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R94), K112 (≠ R134), P143 (= P165), D144 (= D166), V145 (= V167), Y146 (≠ N168), T190 (= T210), Y219 (≠ F239), G220 (= G240), N221 (= N241), A222 (≠ V242), D243 (= D262), S244 (≠ H263), K263 (≠ A282), A295 (= A313), I296 (≠ L314), N318 (= N336)
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction
49% identity, 94% coverage: 25:432/435 of query aligns to 1:412/416 of 8xcoA
P50735 Cryptic catabolic NAD-specific glutamate dehydrogenase GudB; NAD-GDH; EC 1.4.1.2 from Bacillus subtilis (strain 168) (see paper)
49% identity, 90% coverage: 42:432/435 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.
6yehA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in apo form (see paper)
47% identity, 90% coverage: 42:432/435 of query aligns to 17:407/410 of 6yehA
6yeiF Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
47% identity, 90% coverage: 42:432/435 of query aligns to 18:408/410 of 6yeiF
- binding 2-oxoglutaric acid: K66 (= K90), G68 (= G92), M87 (= M111), K90 (= K114), K102 (= K126), A140 (= A164), V341 (= V365), S344 (= S368)
- binding potassium ion: S27 (≠ T51), L28 (= L52), I30 (≠ R54), P31 (= P55), F32 (≠ K56)
- binding nicotinamide-adenine-dinucleotide: R70 (= R94), D142 (= D166), M143 (≠ V167), T185 (= T210), F214 (= F239), G215 (= G240), N216 (= N241), V217 (= V242), D237 (= D262), I238 (≠ H263), A288 (= A312), A289 (= A313), A311 (= A335), N312 (= N336), N337 (= N361)
6yeiA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
47% identity, 90% coverage: 42:432/435 of query aligns to 17:407/409 of 6yeiA
- binding potassium ion: S26 (≠ T51), L27 (= L52), I29 (≠ R54), P30 (= P55)
- binding nicotinamide-adenine-dinucleotide: T184 (= T210), F213 (= F239), G214 (= G240), N215 (= N241), V216 (= V242), D236 (= D262), I237 (≠ H263), A288 (= A313), L289 (= L314), A310 (= A335), N311 (= N336), N336 (= N361)
8owmC Crystal structure of glutamate dehydrogenase 2 from arabidopsis thaliana binding ca, NAD and 2,2-dihydroxyglutarate (see paper)
45% identity, 90% coverage: 42:432/435 of query aligns to 20:410/413 of 8owmC
- binding calcium ion: S29 (≠ T51), I32 (≠ R54)
- binding nicotinamide-adenine-dinucleotide: D144 (= D166), M145 (≠ V167), R183 (= R206), T187 (= T210), F216 (= F239), G217 (= G240), N218 (= N241), V219 (= V242), D239 (= D262), I240 (≠ H263), C290 (≠ A312), A291 (= A313), A313 (= A335), N314 (= N336), N339 (= N361)
- binding 2,2-bis(oxidanyl)pentanedioic acid: K68 (= K90), G70 (= G92), M89 (= M111), K92 (= K114), K104 (= K126), A142 (= A164), R183 (= R206), N314 (= N336), V343 (= V365), S346 (= S368)
P28997 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Peptoniphilus asaccharolyticus (Peptostreptococcus asaccharolyticus) (see 2 papers)
44% identity, 95% coverage: 23:434/435 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)
43% identity, 93% coverage: 30:433/435 of query aligns to 10:419/420 of P80053
- K254 (≠ A271) modified: N6-methyllysine
- K260 (≠ A277) modified: N6-methyllysine
- K372 (≠ Q388) modified: N6-methyllysine
- K391 (≠ D407) modified: N6-methyllysine
- K392 (≠ N408) modified: N6-methyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylmethionine
3aoeF Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
41% identity, 97% coverage: 16:435/435 of query aligns to 1:417/417 of 3aoeF
1v9lA L-glutamate dehydrogenase from pyrobaculum islandicum complexed with NAD (see paper)
45% identity, 88% coverage: 50:432/435 of query aligns to 26:416/418 of 1v9lA
- active site: K102 (= K126), D142 (= D166)
- binding nicotinamide-adenine-dinucleotide: T186 (= T210), Q213 (= Q237), G216 (= G240), N217 (= N241), V218 (= V242), D238 (= D262), I239 (≠ H263), A296 (= A313), I297 (≠ L314), A318 (= A335), N319 (= N336), N344 (= N361)
6dhmA Bovine glutamate dehydrogenase complexed with zinc (see paper)
45% identity, 80% coverage: 49:398/435 of query aligns to 49:417/495 of 6dhmA
- binding glutamic acid: K90 (= K90), G92 (= G92), M111 (= M111), K114 (= K114), A166 (= A164), D168 (= D166), R211 (= R206), V378 (= V365), S381 (= S368)
- binding guanosine-5'-triphosphate: H209 (≠ L204), S213 (≠ E208), H258 (≠ V245), R261 (≠ K248), Y262 (≠ L249), R265 (≠ E252), K289 (≠ P276), E292 (≠ M279)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: D168 (= D166), M169 (≠ V167), S170 (≠ N168), R211 (= R206), Q250 (= Q237), G251 (= G238), F252 (= F239), G253 (= G240), N254 (= N241), V255 (= V242), E275 (≠ D262), S276 (≠ H263), A326 (= A313), G347 (= G334), A348 (= A335), N349 (= N336), N374 (= N361)
- binding zinc ion: H209 (≠ L204)
Sites not aligning to the query:
6dhdA Bovine glutamate dehydrogenase complexed with nadh, gtp, glutamate (see paper)
45% identity, 80% coverage: 52:398/435 of query aligns to 52:417/501 of 6dhdA
- active site: K126 (= K126), D168 (= D166)
- binding glutamic acid: K90 (= K90), M111 (= M111), K114 (= K114), K126 (= K126), A166 (= A164), V378 (= V365), S381 (= S368)
- binding guanosine-5'-triphosphate: H209 (≠ L204), S213 (≠ E208), R217 (= R212), H258 (≠ V245), R261 (≠ K248), Y262 (≠ L249), R265 (≠ E252), E292 (≠ M279)
- binding 1,4-dihydronicotinamide adenine dinucleotide: H85 (≠ S85), R86 (= R86), R94 (= R94), A116 (= A116), D119 (≠ N119), V120 (= V120), D168 (= D166), M169 (≠ V167), H195 (≠ T190), Q205 (≠ L200), G206 (= G201), T215 (= T210), Q250 (= Q237), F252 (= F239), G253 (= G240), N254 (= N241), V255 (= V242), E275 (≠ D262), S276 (≠ H263), A326 (= A313), A348 (= A335), N349 (= N336), N374 (= N361), K387 (≠ Q374), N388 (≠ D375), H391 (≠ S378), S393 (vs. gap)
Sites not aligning to the query:
3etgA Glutamate dehydrogenase complexed with gw5074 (see paper)
45% identity, 80% coverage: 52:398/435 of query aligns to 52:417/501 of 3etgA
- active site: K126 (= K126), D168 (= D166)
- binding glutamic acid: K90 (= K90), M111 (= M111), K114 (= K114), A166 (= A164), V378 (= V365), S381 (= S368)
- binding guanosine-5'-triphosphate: H209 (≠ L204), G210 (= G205), S213 (≠ E208), R217 (= R212), R261 (≠ K248), R265 (≠ E252), E292 (≠ M279)
- binding (3E)-3-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-5-iodo-1,3-dihydro-2H-indol-2-one: R146 (= R146), R147 (= R147), M150 (≠ S150)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: D168 (= D166), M169 (≠ V167), R211 (= R206), T215 (= T210), Q250 (= Q237), G253 (= G240), V255 (= V242), E275 (≠ D262), S276 (≠ H263), A326 (= A313), G347 (= G334), A348 (= A335), N349 (= N336), N374 (= N361)
3etdA Structure of glutamate dehydrogenase complexed with bithionol (see paper)
45% identity, 80% coverage: 52:398/435 of query aligns to 52:417/501 of 3etdA
- active site: K126 (= K126), D168 (= D166)
- binding 2,2'-sulfanediylbis(4,6-dichlorophenol): R146 (= R146), R146 (= R146), R147 (= R147), D181 (= D179), S185 (≠ M183)
- binding glutamic acid: K90 (= K90), G92 (= G92), M111 (= M111), K114 (= K114), K126 (= K126), A166 (= A164), S381 (= S368)
- binding guanosine-5'-triphosphate: H209 (≠ L204), G210 (= G205), I212 (≠ R207), R217 (= R212), R261 (≠ K248), R265 (≠ E252), E292 (≠ M279)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R94 (= R94), D168 (= D166), M169 (≠ V167), R211 (= R206), T215 (= T210), Q250 (= Q237), F252 (= F239), G253 (= G240), V255 (= V242), E275 (≠ D262), S276 (≠ H263), A326 (= A313), A348 (= A335), N349 (= N336), N374 (= N361)
Sites not aligning to the query:
Query Sequence
>RR42_RS02570 FitnessBrowser__Cup4G11:RR42_RS02570
MSSAAPSNPAVKNHTLPSYLNADALGPWGIYLQQVDRVTPYLGSLARWVETLKRPKRALV
VDVPIEMDNGTIAHFEGYRVQHNMSRGPGKGGVRFHQDVTLSEVMALSAWMSVKNAAVNV
PYGGAKGGIRVDPRTLSRSELERVTRRYTSEINFIIGPNKDIPAPDVNTNEQVMAWMMDT
YSMNSGSTATGVVTGKPISLGGSLGRREATGRGVFVVGSEAARNLGLEIKGARIAVQGFG
NVGAVAAKLFHEAGAKVVAVQDHRTALYNPAGLDVPAMMEYASHSGTIEGFQGETISAEQ
FWQVDCEILIPAALEGQITAQNAPHIKARMVIEGANGPTTPEADDILRERNILVAPDVIA
NAGGVTVSYFEWVQDFSSFFWTEEEINQRLVRIMQEAFRAIWQVAQDNKVTLRTAAFIVA
CTRILQAREMRGLYP
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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