SitesBLAST
Comparing WP_084932394.1 NCBI__GCF_002095475.1:WP_084932394.1 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
63% identity, 99% coverage: 5:423/423 of query aligns to 4:416/416 of 4xgiA
- active site: K112 (= K113), D152 (= D153)
- binding 2-oxoglutaric acid: K76 (= K77), G78 (= G79), M97 (= M98), K100 (= K101), K112 (= K113), A150 (= A151), R192 (= R193), S355 (= S356)
- binding nicotinamide-adenine-dinucleotide: R80 (= R81), D152 (= D153), V153 (= V154), T196 (= T197), G224 (= G225), G226 (= G227), N227 (= N228), V228 (= V229), D248 (= D249), H249 (= H250), A299 (= A300), A300 (= A301), A322 (= A323), N323 (= N324), N348 (= N349)
3aoeB Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
61% identity, 99% coverage: 4:423/423 of query aligns to 6:424/424 of 3aoeB
3aogA Crystal structure of glutamate dehydrogenase (gdhb) from thermus thermophilus (glu bound form)
61% identity, 99% coverage: 4:423/423 of query aligns to 3:421/421 of 3aogA
- active site: K111 (= K113), D151 (= D153)
- binding glutamic acid: A70 (≠ S72), G77 (= G79), M96 (= M98), K111 (= K113), P150 (= P152), D151 (= D153), D164 (= D166), M168 (= M170), S354 (= S356), R417 (= R419), G418 (= G420), L419 (= L421), Y420 (= Y422)
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)
46% identity, 95% coverage: 19:420/423 of query aligns to 10:414/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (= K77), G70 (= G79), M89 (= M98), K92 (= K101), K104 (= K113), A142 (= A151), D144 (= D153), G346 (= G352), S350 (= S356)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R81), K112 (≠ R121), P143 (= P152), D144 (= D153), V145 (= V154), Y146 (≠ G155), T190 (= T197), Y219 (≠ F226), G220 (= G227), N221 (= N228), A222 (≠ V229), D243 (= D249), S244 (≠ H250), K263 (≠ Q269), A295 (= A301), I296 (≠ L302), N318 (= N324)
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction (see paper)
46% identity, 95% coverage: 19:420/423 of query aligns to 8:412/416 of 8xcoA
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction (see paper)
46% identity, 95% coverage: 19:420/423 of query aligns to 11:415/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K77), M90 (= M98), K105 (= K113), A143 (= A151), D145 (= D153), S351 (= S356)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R81), D145 (= D153), V146 (= V154), Y147 (≠ G155), T191 (= T197), Y220 (≠ F226), G221 (= G227), N222 (= N228), A223 (≠ V229), D244 (= D249), S245 (≠ H250), K264 (≠ Q269), N281 (≠ H286), A295 (= A300), A296 (= A301), I297 (≠ L302), N319 (= N324), N344 (= N349)
8zneA Cryo-em structure of w89f mutated glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction
46% identity, 95% coverage: 19:420/423 of query aligns to 8:412/416 of 8zneA
- binding glutamic acid: M87 (= M98), K90 (= K101), A140 (= A151), D142 (= D153), S348 (= S356)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G216 (= G225), Y217 (≠ F226), G218 (= G227), N219 (= N228), A220 (≠ V229), D241 (= D249), S242 (≠ H250), A293 (= A301), I294 (≠ L302)
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, 96% coverage: 17:420/423 of query aligns to 23:422/424 of P39633
- E27 (≠ Q21) mutation to F: Increase of thermostability 8 degrees Celsius higher than that of the wild-type.
- E93 (= E90) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (= D119) 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 (≠ S141) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ G155) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (= S231) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ G322) 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)
44% identity, 98% coverage: 6:420/423 of query aligns to 9:425/427 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)
45% identity, 91% coverage: 37:422/423 of query aligns to 30:421/421 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.
3aoeF Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
45% identity, 99% coverage: 5:423/423 of query aligns to 3:417/417 of 3aoeF
6yehA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in apo form (see paper)
44% identity, 93% coverage: 29:420/423 of query aligns to 17:407/410 of 6yehA
6yeiF Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
44% identity, 93% coverage: 29:420/423 of query aligns to 18:408/410 of 6yeiF
- binding 2-oxoglutaric acid: K66 (= K77), G68 (= G79), M87 (= M98), K90 (= K101), K102 (= K113), A140 (= A151), V341 (= V353), S344 (= S356)
- binding potassium ion: S27 (≠ T38), L28 (= L39), I30 (≠ H41), P31 (= P42), F32 (≠ K43)
- binding nicotinamide-adenine-dinucleotide: R70 (= R81), D142 (= D153), M143 (≠ V154), T185 (= T197), F214 (= F226), G215 (= G227), N216 (= N228), V217 (= V229), D237 (= D249), I238 (≠ H250), A288 (= A300), A289 (= A301), A311 (= A323), N312 (= N324), N337 (= N349)
6yeiA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
44% identity, 93% coverage: 29:420/423 of query aligns to 17:407/409 of 6yeiA
- binding potassium ion: S26 (≠ T38), L27 (= L39), I29 (≠ H41), P30 (= P42)
- binding nicotinamide-adenine-dinucleotide: T184 (= T197), F213 (= F226), G214 (= G227), N215 (= N228), V216 (= V229), D236 (= D249), I237 (≠ H250), A288 (= A301), L289 (= L302), A310 (= A323), N311 (= N324), N336 (= N349)
8s38B Crystal structure of medicago truncatula glutamate dehydrogenase 2 in complex with citrate and NAD (see paper)
42% identity, 95% coverage: 21:420/423 of query aligns to 13:411/414 of 8s38B
8s38A Crystal structure of medicago truncatula glutamate dehydrogenase 2 in complex with citrate and NAD (see paper)
42% identity, 95% coverage: 21:420/423 of query aligns to 6:404/407 of 8s38A
- binding nicotinamide-adenine-dinucleotide: T181 (= T197), F210 (= F226), G211 (= G227), N212 (= N228), V213 (= V229), D233 (= D249), I234 (≠ H250), C284 (≠ A300), A285 (= A301), L286 (= L302), A307 (= A323), N308 (= N324), N333 (= N349)
8s3bA Glutamate dehydrogenase (see paper)
42% identity, 95% coverage: 21:420/423 of query aligns to 9:407/410 of 8s3bA
- binding 3-(1~{H}-1,2,3,4-tetrazol-5-yl)benzoic acid: K65 (= K77), G66 (= G78), G67 (= G79), M86 (= M98), K101 (= K113), A139 (= A151), D141 (= D153), G339 (= G352), S343 (= S356)
- binding calcium ion: S26 (≠ T38), I29 (≠ H41)
- binding nicotinamide-adenine-dinucleotide: T184 (= T197), F213 (= F226), G214 (= G227), N215 (= N228), V216 (= V229), D236 (= D249), I237 (≠ H250), A288 (= A301), A310 (= A323), N311 (= N324), N336 (= N349)
8s39C Crystal structure of medicago truncatula glutamate dehydrogenase 2 in complex with isophthalic acid and NAD (see paper)
42% identity, 95% coverage: 21:420/423 of query aligns to 12:410/413 of 8s39C
- binding benzene-1,3-dicarboxylic acid: K68 (= K77), M89 (= M98), K92 (= K101), K104 (= K113), A142 (= A151), P143 (= P152), D144 (= D153), R183 (= R193), N314 (= N324), S346 (= S356)
- binding nicotinamide-adenine-dinucleotide: R72 (= R81), D144 (= D153), M145 (≠ V154), R183 (= R193), T187 (= T197), F216 (= F226), G217 (= G227), N218 (= N228), V219 (= V229), D239 (= D249), I240 (≠ H250), A291 (= A301), A313 (= A323), N314 (= N324), N339 (= N349)
8s3dA Crystal structure of medicago truncatula glutamate dehydrogenase 2 in complex with 2-amino-2-hydroxyglutarate (reaction intermediate) and NAD (see paper)
42% identity, 95% coverage: 21:420/423 of query aligns to 11:409/412 of 8s3dA
- binding (2S)-2-azanyl-2-oxidanyl-pentanedioic acid: K67 (= K77), G68 (= G78), G69 (= G79), M88 (= M98), K91 (= K101), K103 (= K113), A141 (= A151), R182 (= R193), V342 (= V353), S345 (= S356)
- binding calcium ion: S28 (≠ T38), I31 (≠ H41)
- binding glycine: P142 (= P152), G171 (= G182), N217 (= N228)
- binding nicotinamide-adenine-dinucleotide: R71 (= R81), D143 (= D153), M144 (≠ V154), R182 (= R193), T186 (= T197), F215 (= F226), G216 (= G227), N217 (= N228), V218 (= V229), D238 (= D249), I239 (≠ H250), C289 (≠ A300), A290 (= A301), A312 (= A323), N313 (= N324), N338 (= N349)
8s3aE Crystal structure of medicago truncatula glutamate dehydrogenase 2 in complex with 2,6-pyridinedicarboxylic acid and NAD (see paper)
42% identity, 95% coverage: 21:420/423 of query aligns to 11:409/412 of 8s3aE
- binding nicotinamide-adenine-dinucleotide: R71 (= R81), D143 (= D153), M144 (≠ V154), R182 (= R193), T186 (= T197), F215 (= F226), G216 (= G227), N217 (= N228), V218 (= V229), D238 (= D249), I239 (≠ H250), C289 (≠ A300), A290 (= A301), A312 (= A323), N313 (= N324), N338 (= N349)
- binding pyridine-2,6-dicarboxylic acid: K67 (= K77), M88 (= M98), K91 (= K101), K103 (= K113), A141 (= A151), P142 (= P152), D143 (= D153), R182 (= R193), N313 (= N324), S345 (= S356)
Query Sequence
>WP_084932394.1 NCBI__GCF_002095475.1:WP_084932394.1
MSALSYVSEDKNSAWATYLAQVERVLPYLGDLSKWADTLRHPKRALIVDIPLEMDDGSVR
HFEGYRVQHNLSRGPGKGGVRFHPDVTLEEVMALSAWMTVKCAAINLPFGGAKGGVRVDP
RELSRKELERLTRRYTSEIGSIIGPQQDIPAPDVGTNPQVMAWMMDTWSMNVGATSTGVV
TGKPIHLGGSLGRVKATGRGVFVTGRAMAQRINLPLENARVAVQGFGNVGSVAAELFSEA
GALIVAVQDHSATLYNASGIDVAALTEWQQQTGSISGYRGAMSVSHEAFWEQGYDIVVPA
ALEGQITADRARKLVCKLVLEGANGPTLPAADDILKERGITVVPDVICNAGGVTVSYFEW
VQDFSSFFWSEDEINERLDRIMEQALLAVWNKSLELGVTLRTAAYAVACERILEARRERG
LYP
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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