SitesBLAST
Comparing Echvi_1535 FitnessBrowser__Cola:Echvi_1535 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)
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)
46% identity, 94% coverage: 26:423/425 of query aligns to 28:422/424 of P39633
- E93 (= E91) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (≠ N120) 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 (≠ D142) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ G156) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (= S232) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ G325) 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.
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction
49% identity, 96% coverage: 14:423/425 of query aligns to 2:412/416 of 8xcoA
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction
49% identity, 96% coverage: 14:423/425 of query aligns to 5:415/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K78), M90 (= M99), K105 (= K114), A143 (= A152), D145 (= D154), S351 (= S359)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R82), D145 (= D154), V146 (≠ M155), Y147 (≠ G156), T191 (= T198), Y220 (≠ F227), G221 (= G228), N222 (= N229), A223 (≠ V230), D244 (= D250), S245 (≠ I251), K264 (≠ R270), N281 (≠ D288), A295 (= A303), A296 (= A304), I297 (≠ V305), N319 (= N327), N344 (= N352)
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, 96% coverage: 14:423/425 of query aligns to 4:414/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (= K78), G70 (= G80), M89 (= M99), K92 (= K102), K104 (= K114), A142 (= A152), D144 (= D154), G346 (= G355), S350 (= S359)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R82), K112 (≠ R122), P143 (= P153), D144 (= D154), V145 (≠ M155), Y146 (≠ G156), T190 (= T198), Y219 (≠ F227), G220 (= G228), N221 (= N229), A222 (≠ V230), D243 (= D250), S244 (≠ I251), K263 (≠ R270), A295 (= A304), I296 (≠ V305), N318 (= N327)
P50735 Cryptic catabolic NAD-specific glutamate dehydrogenase GudB; NAD-GDH; EC 1.4.1.2 from Bacillus subtilis (strain 168) (see paper)
45% identity, 97% coverage: 10:423/425 of query aligns to 12:425/427 of P50735
- VKA 97:99 (≠ VRA 92:94) mutation Missing: In gudB1; gains glutamate dehydrogenase activity, restores growth on proline, arginine, ornithine.
6yeiA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
47% identity, 96% coverage: 14:423/425 of query aligns to 1:407/409 of 6yeiA
- binding potassium ion: S26 (≠ V39), L27 (= L40), I29 (≠ N42), P30 (= P43)
- binding nicotinamide-adenine-dinucleotide: T184 (= T198), F213 (= F227), G214 (= G228), N215 (= N229), V216 (= V230), D236 (= D250), I237 (= I251), A288 (= A304), L289 (≠ V305), A310 (= A326), N311 (= N327), N336 (= N352)
3aogA Crystal structure of glutamate dehydrogenase (gdhb) from thermus thermophilus (glu bound form)
48% identity, 96% coverage: 15:423/425 of query aligns to 12:418/421 of 3aogA
- active site: K111 (= K114), D151 (= D154)
- binding glutamic acid: A70 (≠ I73), G77 (= G80), M96 (= M99), K111 (= K114), P150 (= P153), D151 (= D154), D164 (= D167), M168 (≠ K171), S354 (= S359), R417 (= R422), G418 (= G423)
Sites not aligning to the query:
6yehA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in apo form (see paper)
47% identity, 96% coverage: 14:423/425 of query aligns to 1:407/410 of 6yehA
6yeiF Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
47% identity, 96% coverage: 14:423/425 of query aligns to 2:408/410 of 6yeiF
- binding 2-oxoglutaric acid: K66 (= K78), G68 (= G80), M87 (= M99), K90 (= K102), K102 (= K114), A140 (= A152), V341 (= V356), S344 (= S359)
- binding potassium ion: S27 (≠ V39), L28 (= L40), I30 (≠ N42), P31 (= P43), F32 (≠ A44)
- binding nicotinamide-adenine-dinucleotide: R70 (= R82), D142 (= D154), M143 (= M155), T185 (= T198), F214 (= F227), G215 (= G228), N216 (= N229), V217 (= V230), D237 (= D250), I238 (= I251), A288 (= A303), A289 (= A304), A311 (= A326), N312 (= N327), N337 (= N352)
3aoeB Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
48% identity, 96% coverage: 15:423/425 of query aligns to 15:421/424 of 3aoeB
Sites not aligning to the query:
8owmC Crystal structure of glutamate dehydrogenase 2 from arabidopsis thaliana binding ca, NAD and 2,2-dihydroxyglutarate (see paper)
46% identity, 96% coverage: 14:423/425 of query aligns to 4:410/413 of 8owmC
- binding calcium ion: S29 (≠ V39), I32 (≠ N42)
- binding nicotinamide-adenine-dinucleotide: D144 (= D154), M145 (= M155), R183 (= R194), T187 (= T198), F216 (= F227), G217 (= G228), N218 (= N229), V219 (= V230), D239 (= D250), I240 (= I251), C290 (≠ A303), A291 (= A304), A313 (= A326), N314 (= N327), N339 (= N352)
- binding 2,2-bis(oxidanyl)pentanedioic acid: K68 (= K78), G70 (= G80), M89 (= M99), K92 (= K102), K104 (= K114), A142 (= A152), R183 (= R194), N314 (= N327), V343 (= V356), S346 (= S359)
4xgiA Crystal structure of glutamate dehydrogenase from burkholderia thailandensis
46% identity, 97% coverage: 11:423/425 of query aligns to 9:413/416 of 4xgiA
- active site: K112 (= K114), D152 (= D154)
- binding 2-oxoglutaric acid: K76 (= K78), G78 (= G80), M97 (= M99), K100 (= K102), K112 (= K114), A150 (= A152), R192 (= R194), S355 (= S359)
- binding nicotinamide-adenine-dinucleotide: R80 (= R82), D152 (= D154), V153 (≠ M155), T196 (= T198), G224 (= G226), G226 (= G228), N227 (= N229), V228 (= V230), D248 (= D250), H249 (≠ I251), A299 (= A303), A300 (= A304), A322 (= A326), N323 (= N327), N348 (= N352)
P28997 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Peptoniphilus asaccharolyticus (Peptostreptococcus asaccharolyticus) (see 2 papers)
43% identity, 98% coverage: 9:425/425 of query aligns to 1:421/421 of P28997
- E243 (≠ D250) 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 (≠ I251) 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.
1v9lA L-glutamate dehydrogenase from pyrobaculum islandicum complexed with NAD (see paper)
43% identity, 96% coverage: 16:423/425 of query aligns to 4:416/418 of 1v9lA
- active site: K102 (= K114), D142 (= D154)
- binding nicotinamide-adenine-dinucleotide: T186 (= T198), Q213 (= Q225), G216 (= G228), N217 (= N229), V218 (= V230), D238 (= D250), I239 (= I251), A296 (= A304), I297 (≠ V305), A318 (= A326), N319 (= N327), N344 (= N352)
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: 28:423/425 of query aligns to 23:418/420 of P80053
- K254 (≠ N259) modified: N6-methyllysine
- K260 (= K265) modified: N6-methyllysine
- K372 (≠ R379) modified: N6-methyllysine
- K391 (= K398) modified: N6-methyllysine
- K392 (vs. gap) modified: N6-methyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylmethionine
6dhlA Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ecg) (see paper)
39% identity, 89% coverage: 43:420/425 of query aligns to 49:489/496 of 6dhlA
- binding (2R,3S)-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate: H80 (≠ I73), R81 (≠ L74), C110 (= C103), D114 (= D107), V115 (≠ I108), K382 (≠ Q365), S388 (vs. gap), R391 (= R367), R454 (≠ E387), K483 (= K414)
3eteA Crystal structure of bovine glutamate dehydrogenase complexed with hexachlorophene (see paper)
39% identity, 89% coverage: 43:420/425 of query aligns to 51:491/495 of 3eteA
- active site: K123 (= K114), D165 (= D154)
- binding glutamic acid: K87 (= K78), G89 (= G80), M108 (= M99), K111 (= K102), K123 (= K114), A163 (= A152), R208 (= R194), V375 (= V356), S378 (= S359)
- binding guanosine-5'-triphosphate: I209 (≠ T195), S210 (≠ E196), R214 (= R200), H255 (≠ W233), R258 (≠ A236), Y259 (≠ L237), K443 (vs. gap), H447 (vs. gap)
- binding 2,2'-methanediylbis(3,4,6-trichlorophenol): T183 (≠ A172), I184 (≠ K173), Y187 (vs. gap)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R91 (= R82), K131 (≠ R122), D165 (= D154), M166 (= M155), R208 (= R194), F249 (= F227), G250 (= G228), V252 (= V230), E272 (≠ D250), S273 (≠ I251), A323 (= A304), A345 (= A326), N346 (= N327), N371 (= N352)
6dhdA Bovine glutamate dehydrogenase complexed with nadh, gtp, glutamate (see paper)
39% identity, 89% coverage: 43:420/425 of query aligns to 54:494/501 of 6dhdA
- active site: K126 (= K114), D168 (= D154)
- binding glutamic acid: K90 (= K78), M111 (= M99), K114 (= K102), K126 (= K114), A166 (= A152), V378 (= V356), S381 (= S359)
- binding guanosine-5'-triphosphate: H209 (≠ L192), S213 (≠ E196), R217 (= R200), H258 (≠ W233), R261 (≠ A236), Y262 (≠ L237), R265 (≠ E240), E292 (≠ I267), H450 (vs. gap)
- binding 1,4-dihydronicotinamide adenine dinucleotide: H85 (≠ I73), R86 (≠ L74), R94 (= R82), A116 (= A104), D119 (= D107), V120 (≠ I108), D168 (= D154), M169 (= M155), H195 (≠ N178), Q205 (≠ L188), G206 (= G189), T215 (= T198), Q250 (= Q225), F252 (= F227), G253 (= G228), N254 (= N229), V255 (= V230), E275 (≠ D250), S276 (≠ I251), A326 (= A304), A348 (= A326), N349 (= N327), N374 (= N352), K387 (≠ Q365), N388 (= N366), H391 (vs. gap), S393 (vs. gap), K488 (= K414), R491 (≠ Q417)
3etgA Glutamate dehydrogenase complexed with gw5074 (see paper)
39% identity, 89% coverage: 43:420/425 of query aligns to 54:494/501 of 3etgA
- active site: K126 (= K114), D168 (= D154)
- binding glutamic acid: K90 (= K78), M111 (= M99), K114 (= K102), A166 (= A152), V378 (= V356), S381 (= S359)
- binding guanosine-5'-triphosphate: H209 (≠ L192), G210 (= G193), S213 (≠ E196), R217 (= R200), R261 (≠ A236), R265 (≠ E240), E292 (≠ I267)
- binding (3E)-3-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-5-iodo-1,3-dihydro-2H-indol-2-one: R146 (= R134), R147 (≠ A135), M150 (vs. gap)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: D168 (= D154), M169 (= M155), R211 (= R194), T215 (= T198), Q250 (= Q225), G253 (= G228), V255 (= V230), E275 (≠ D250), S276 (≠ I251), A326 (= A304), G347 (= G325), A348 (= A326), N349 (= N327), N374 (= N352)
3etdA Structure of glutamate dehydrogenase complexed with bithionol (see paper)
39% identity, 89% coverage: 43:420/425 of query aligns to 54:494/501 of 3etdA
- active site: K126 (= K114), D168 (= D154)
- binding 2,2'-sulfanediylbis(4,6-dichlorophenol): R146 (= R134), R146 (= R134), R147 (≠ A135), D181 (= D167), S185 (≠ K171)
- binding glutamic acid: K90 (= K78), G92 (= G80), M111 (= M99), K114 (= K102), K126 (= K114), A166 (= A152), S381 (= S359)
- binding guanosine-5'-triphosphate: H209 (≠ L192), G210 (= G193), I212 (≠ T195), R217 (= R200), R261 (≠ A236), R265 (≠ E240), E292 (≠ I267), H450 (vs. gap)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R94 (= R82), D168 (= D154), M169 (= M155), R211 (= R194), T215 (= T198), Q250 (= Q225), F252 (= F227), G253 (= G228), V255 (= V230), E275 (≠ D250), S276 (≠ I251), A326 (= A304), A348 (= A326), N349 (= N327), N374 (= N352)
Query Sequence
>Echvi_1535 FitnessBrowser__Cola:Echvi_1535
MAYIEPAPIKDKENPLESMMERFNIAAEKLGLSEEVYNVLKNPAKQVIVSLPITMDNGKI
KVFEGIRVVHSNILGPAKGGIRFAPDVHIDEVRALAAWMTWKCAVVDIPYGGGKGGVRCN
PREMSPGEIERLVRAYTLAMIDVFGPDKDIPAPDMGTGPKEMAWLMDEYSKAKGTTVNAV
VTGKPLVLGGSLGRTEATGRGVMVSALAAMEKLKINPFQATCAVQGFGNVGSWASALLEE
RGLKVVAVSDISGAYYNANGINIQKAIAYRDGNKGTLEGFDGAEKLSDPMELLELKVDVL
VPAAVEDVITKANVDKINARLIVEGANGPTSFNADKIINDKGIMVVPDILANAGGVTVSY
FEWVQNRLGYKWTAERVNRRSDRIMKEAFDQVYKVSVKHGVPMRIAAYIVAIDKVAQTYQ
FRGGF
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