SitesBLAST
Comparing WP_092481889.1 NCBI__GCF_900115975.1:WP_092481889.1 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)
8xcsA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADPH, akg and nh4 in the initial stage of reaction (see paper)
57% identity, 98% coverage: 4:417/421 of query aligns to 2:416/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (= K70), G70 (= G72), M89 (= M91), K92 (= K94), K104 (= K106), A142 (= A144), D144 (= D146), G346 (= G346), S350 (= S350)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R74), K112 (= K114), P143 (= P145), D144 (= D146), V145 (= V147), Y146 (≠ G148), T190 (= T190), Y219 (≠ F219), G220 (= G220), N221 (= N221), A222 (≠ V222), D243 (= D243), S244 (= S244), K263 (= K263), A295 (= A295), I296 (≠ L296), N318 (= N318)
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction (see paper)
57% identity, 98% coverage: 4:417/421 of query aligns to 3:417/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K70), M90 (= M91), K105 (= K106), A143 (= A144), D145 (= D146), S351 (= S350)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R74), D145 (= D146), V146 (= V147), Y147 (≠ G148), T191 (= T190), Y220 (≠ F219), G221 (= G220), N222 (= N221), A223 (≠ V222), D244 (= D243), S245 (= S244), K264 (= K263), N281 (≠ T280), A295 (= A294), A296 (= A295), I297 (≠ L296), N319 (= N318), N344 (= N343)
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction (see paper)
57% identity, 98% coverage: 5:417/421 of query aligns to 1:414/416 of 8xcoA
8zneA Cryo-em structure of w89f mutated glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction
57% identity, 98% coverage: 5:417/421 of query aligns to 1:414/416 of 8zneA
- binding glutamic acid: M87 (= M91), K90 (= K94), A140 (= A144), D142 (= D146), S348 (= S350)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G216 (= G218), Y217 (≠ F219), G218 (= G220), N219 (= N221), A220 (≠ V222), D241 (= D243), S242 (= S244), A293 (= A295), I294 (≠ L296)
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)
52% identity, 99% coverage: 3:417/421 of query aligns to 13:424/424 of P39633
- E27 (≠ D17) mutation to F: Increase of thermostability 8 degrees Celsius higher than that of the wild-type.
- E93 (= E83) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (≠ N112) 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 (≠ P134) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ G148) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (= S224) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ G316) mutation to R: No effect.
P50735 Cryptic catabolic NAD-specific glutamate dehydrogenase GudB; NAD-GDH; EC 1.4.1.2 from Bacillus subtilis (strain 168) (see paper)
54% identity, 98% coverage: 4:417/421 of query aligns to 14:427/427 of P50735
- VKA 97:99 (vs. gap) mutation Missing: In gudB1; gains glutamate dehydrogenase activity, restores growth on proline, arginine, ornithine.
P28997 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Peptoniphilus asaccharolyticus (Peptostreptococcus asaccharolyticus) (see 2 papers)
52% identity, 99% coverage: 1:416/421 of query aligns to 1:420/421 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.
4xgiA Crystal structure of glutamate dehydrogenase from burkholderia thailandensis
51% identity, 95% coverage: 15:415/421 of query aligns to 21:413/416 of 4xgiA
- active site: K112 (= K106), D152 (= D146)
- binding 2-oxoglutaric acid: K76 (= K70), G78 (= G72), M97 (= M91), K100 (= K94), K112 (= K106), A150 (= A144), R192 (= R186), S355 (= S350)
- binding nicotinamide-adenine-dinucleotide: R80 (= R74), D152 (= D146), V153 (= V147), T196 (= T190), G224 (= G218), G226 (= G220), N227 (= N221), V228 (= V222), D248 (= D243), H249 (≠ S244), A299 (= A294), A300 (= A295), A322 (= A317), N323 (= N318), N348 (= N343)
3aogA Crystal structure of glutamate dehydrogenase (gdhb) from thermus thermophilus (glu bound form)
51% identity, 97% coverage: 8:415/421 of query aligns to 13:418/421 of 3aogA
- active site: K111 (= K106), D151 (= D146)
- binding glutamic acid: A70 (= A65), G77 (= G72), M96 (= M91), K111 (= K106), P150 (= P145), D151 (= D146), D164 (= D159), M168 (≠ R163), S354 (= S350), R417 (= R414), G418 (= G415)
Sites not aligning to the query:
3aoeB Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
51% identity, 97% coverage: 8:415/421 of query aligns to 16:421/424 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)
48% identity, 94% coverage: 22:416/421 of query aligns to 20:411/413 of 8owmC
- binding calcium ion: S29 (≠ I31), I32 (≠ E34)
- binding nicotinamide-adenine-dinucleotide: D144 (= D146), M145 (≠ V147), R183 (= R186), T187 (= T190), F216 (= F219), G217 (= G220), N218 (= N221), V219 (= V222), D239 (= D243), I240 (≠ S244), C290 (≠ A294), A291 (= A295), A313 (= A317), N314 (= N318), N339 (= N343)
- binding 2,2-bis(oxidanyl)pentanedioic acid: K68 (= K70), G70 (= G72), M89 (= M91), K92 (= K94), K104 (= K106), A142 (= A144), R183 (= R186), N314 (= N318), V343 (= V347), S346 (= S350)
8s38A Crystal structure of medicago truncatula glutamate dehydrogenase 2 in complex with citrate and NAD (see paper)
48% identity, 94% coverage: 22:416/421 of query aligns to 14:405/407 of 8s38A
- binding nicotinamide-adenine-dinucleotide: T181 (= T190), F210 (= F219), G211 (= G220), N212 (= N221), V213 (= V222), D233 (= D243), I234 (≠ S244), C284 (≠ A294), A285 (= A295), L286 (= L296), A307 (= A317), N308 (= N318), N333 (= N343)
8s3bA Glutamate dehydrogenase (see paper)
48% identity, 94% coverage: 22:416/421 of query aligns to 17:408/410 of 8s3bA
- binding 3-(1~{H}-1,2,3,4-tetrazol-5-yl)benzoic acid: K65 (= K70), G66 (= G71), G67 (= G72), M86 (= M91), K101 (= K106), A139 (= A144), D141 (= D146), G339 (= G346), S343 (= S350)
- binding calcium ion: S26 (≠ I31), I29 (≠ E34)
- binding nicotinamide-adenine-dinucleotide: T184 (= T190), F213 (= F219), G214 (= G220), N215 (= N221), V216 (= V222), D236 (= D243), I237 (≠ S244), A288 (= A295), A310 (= A317), N311 (= N318), N336 (= N343)
8s38B Crystal structure of medicago truncatula glutamate dehydrogenase 2 in complex with citrate and NAD (see paper)
48% identity, 94% coverage: 22:416/421 of query aligns to 21:412/414 of 8s38B
8s3dA Crystal structure of medicago truncatula glutamate dehydrogenase 2 in complex with 2-amino-2-hydroxyglutarate (reaction intermediate) and NAD (see paper)
48% identity, 94% coverage: 22:416/421 of query aligns to 19:410/412 of 8s3dA
- binding (2S)-2-azanyl-2-oxidanyl-pentanedioic acid: K67 (= K70), G68 (= G71), G69 (= G72), M88 (= M91), K91 (= K94), K103 (= K106), A141 (= A144), R182 (= R186), V342 (= V347), S345 (= S350)
- binding calcium ion: S28 (≠ I31), I31 (≠ E34)
- binding glycine: P142 (= P145), G171 (= G175), N217 (= N221)
- binding nicotinamide-adenine-dinucleotide: R71 (= R74), D143 (= D146), M144 (≠ V147), R182 (= R186), T186 (= T190), F215 (= F219), G216 (= G220), N217 (= N221), V218 (= V222), D238 (= D243), I239 (≠ S244), C289 (≠ A294), A290 (= A295), A312 (= A317), N313 (= N318), N338 (= N343)
8s3aE Crystal structure of medicago truncatula glutamate dehydrogenase 2 in complex with 2,6-pyridinedicarboxylic acid and NAD (see paper)
48% identity, 94% coverage: 22:416/421 of query aligns to 19:410/412 of 8s3aE
- binding nicotinamide-adenine-dinucleotide: R71 (= R74), D143 (= D146), M144 (≠ V147), R182 (= R186), T186 (= T190), F215 (= F219), G216 (= G220), N217 (= N221), V218 (= V222), D238 (= D243), I239 (≠ S244), C289 (≠ A294), A290 (= A295), A312 (= A317), N313 (= N318), N338 (= N343)
- binding pyridine-2,6-dicarboxylic acid: K67 (= K70), M88 (= M91), K91 (= K94), K103 (= K106), A141 (= A144), P142 (= P145), D143 (= D146), R182 (= R186), N313 (= N318), S345 (= S350)
8s39C Crystal structure of medicago truncatula glutamate dehydrogenase 2 in complex with isophthalic acid and NAD (see paper)
48% identity, 94% coverage: 22:416/421 of query aligns to 20:411/413 of 8s39C
- binding benzene-1,3-dicarboxylic acid: K68 (= K70), M89 (= M91), K92 (= K94), K104 (= K106), A142 (= A144), P143 (= P145), D144 (= D146), R183 (= R186), N314 (= N318), S346 (= S350)
- binding nicotinamide-adenine-dinucleotide: R72 (= R74), D144 (= D146), M145 (≠ V147), R183 (= R186), T187 (= T190), F216 (= F219), G217 (= G220), N218 (= N221), V219 (= V222), D239 (= D243), I240 (≠ S244), A291 (= A295), A313 (= A317), N314 (= N318), N339 (= N343)
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)
47% identity, 95% coverage: 20:417/421 of query aligns to 23:420/420 of P80053
- K254 (≠ N252) modified: N6-methyllysine
- K260 (≠ A258) modified: N6-methyllysine
- K372 (≠ E370) modified: N6-methyllysine
- K391 (= K388) modified: N6-methyllysine
- K392 (≠ E389) 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)
47% identity, 97% coverage: 8:417/421 of query aligns to 4:418/418 of 1v9lA
- active site: K102 (= K106), D142 (= D146)
- binding nicotinamide-adenine-dinucleotide: T186 (= T190), Q213 (= Q217), G216 (= G220), N217 (= N221), V218 (= V222), D238 (= D243), I239 (≠ S244), A296 (= A295), I297 (≠ L296), A318 (= A317), N319 (= N318), N344 (= N343)
6yeiA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
47% identity, 94% coverage: 22:416/421 of query aligns to 17:408/409 of 6yeiA
- binding potassium ion: S26 (≠ I31), L27 (= L32), I29 (≠ E34), P30 (= P35)
- binding nicotinamide-adenine-dinucleotide: T184 (= T190), F213 (= F219), G214 (= G220), N215 (= N221), V216 (= V222), D236 (= D243), I237 (≠ S244), A288 (= A295), L289 (= L296), A310 (= A317), N311 (= N318), N336 (= N343)
Query Sequence
>WP_092481889.1 NCBI__GCF_900115975.1:WP_092481889.1
MSQEINCFEIVQNLIDDCVEKLGLDRTVAEILREPQRVLSVSIPVQMDDGSIKVFKGFRS
QHNNACGPCKGGIRFHPDVSMDEVKALSTWMSLKCAVVNLPYGGGKGGVIVNHKELSPNE
LEQLCRGYIRAIAPVLGADMDVPAPDVGTNGQTMGWMMDEFARYRGYNEFGVITGKPIIV
GGSLGRVEATSRGCVFTIRQAAKATGLELKDATVVVQGFGNVGSIAARLLSREDGCKVLA
VSDSTGAAYDPNGLDIAALEKFKLETGSVVGFPGSKNITTEELLQLECDILVPAALENQI
TGENADKINAKIVAEGANGPTTPEADNILAKRNILVLPDVLANAGGVTVSYFEWVQNQYG
YYWTEEEVNERLERKMVEAFDSVYSLYKEHGDINMRGAAYMVAIKRIYEAMKIRGWLGNK
A
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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