SitesBLAST
Comparing WP_011613632.1 NCBI__GCF_000014265.1:WP_011613632.1 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)
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction (see paper)
53% identity, 97% coverage: 6:420/428 of query aligns to 7:415/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K68), M90 (= M89), K105 (= K104), A143 (= A142), D145 (= D144), S351 (= S356)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R72), D145 (= D144), V146 (≠ M145), Y147 (= Y146), T191 (= T188), Y220 (≠ F217), G221 (= G218), N222 (= N219), A223 (= A220), D244 (= D240), S245 (= S241), K264 (= K260), N281 (= N286), A295 (= A300), A296 (= A301), I297 (≠ L302), N319 (= N324), N344 (= N349)
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)
53% identity, 97% coverage: 6:420/428 of query aligns to 6:414/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (= K68), G70 (= G70), M89 (= M89), K92 (= K92), K104 (= K104), A142 (= A142), D144 (= D144), G346 (= G352), S350 (= S356)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R72), K112 (= K112), P143 (= P143), D144 (= D144), V145 (≠ M145), Y146 (= Y146), T190 (= T188), Y219 (≠ F217), G220 (= G218), N221 (= N219), A222 (= A220), D243 (= D240), S244 (= S241), K263 (= K260), 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)
53% identity, 97% coverage: 6:420/428 of query aligns to 4:412/416 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
53% identity, 97% coverage: 6:420/428 of query aligns to 4:412/416 of 8zneA
- binding glutamic acid: M87 (= M89), K90 (= K92), A140 (= A142), D142 (= D144), S348 (= S356)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G216 (= G216), Y217 (≠ F217), G218 (= G218), N219 (= N219), A220 (= A220), D241 (= D240), S242 (= S241), 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)
49% identity, 97% coverage: 4:420/428 of query aligns to 16:422/424 of P39633
- E27 (≠ R15) mutation to F: Increase of thermostability 8 degrees Celsius higher than that of the wild-type.
- E93 (= E81) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (≠ N110) 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 (≠ D132) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (= Y146) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (≠ A222) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (= A322) 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)
48% identity, 95% coverage: 13:420/428 of query aligns to 25:425/427 of P50735
- VKA 97:99 (vs. gap) mutation Missing: In gudB1; gains glutamate dehydrogenase activity, restores growth on proline, arginine, ornithine.
4xgiA Crystal structure of glutamate dehydrogenase from burkholderia thailandensis
44% identity, 97% coverage: 11:425/428 of query aligns to 19:415/416 of 4xgiA
- active site: K112 (= K104), D152 (= D144)
- binding 2-oxoglutaric acid: K76 (= K68), G78 (= G70), M97 (= M89), K100 (= K92), K112 (= K104), A150 (= A142), R192 (= R184), S355 (= S356)
- binding nicotinamide-adenine-dinucleotide: R80 (= R72), D152 (= D144), V153 (≠ M145), T196 (= T188), G224 (= G216), G226 (= G218), N227 (= N219), V228 (≠ A220), D248 (= D240), H249 (≠ S241), A299 (= A300), A300 (= A301), A322 (= A323), N323 (= N324), N348 (= N349)
3aogA Crystal structure of glutamate dehydrogenase (gdhb) from thermus thermophilus (glu bound form)
45% identity, 97% coverage: 10:425/428 of query aligns to 17:420/421 of 3aogA
- active site: K111 (= K104), D151 (= D144)
- binding glutamic acid: A70 (≠ T63), G77 (= G70), M96 (= M89), K111 (= K104), P150 (= P143), D151 (= D144), D164 (= D157), M168 (≠ I161), S354 (= S356), R417 (= R422), G418 (≠ A423), L419 (≠ F424), Y420 (= Y425)
3aoeB Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
45% identity, 97% coverage: 10:425/428 of query aligns to 20:423/424 of 3aoeB
8owmC Crystal structure of glutamate dehydrogenase 2 from arabidopsis thaliana binding ca, NAD and 2,2-dihydroxyglutarate (see paper)
43% identity, 97% coverage: 10:423/428 of query aligns to 10:413/413 of 8owmC
- binding calcium ion: S29 (≠ R29), I32 (≠ Y32)
- binding nicotinamide-adenine-dinucleotide: D144 (= D144), M145 (= M145), R183 (= R184), T187 (= T188), F216 (= F217), G217 (= G218), N218 (= N219), V219 (≠ A220), D239 (= D240), I240 (≠ S241), C290 (≠ A300), A291 (= A301), A313 (= A323), N314 (= N324), N339 (= N349)
- binding 2,2-bis(oxidanyl)pentanedioic acid: K68 (= K68), G70 (= G70), M89 (= M89), K92 (= K92), K104 (= K104), A142 (= A142), R183 (= R184), N314 (= N324), V343 (= V353), S346 (= S356)
6yehA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in apo form (see paper)
43% identity, 96% coverage: 10:420/428 of query aligns to 7:407/410 of 6yehA
6yeiF Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
43% identity, 96% coverage: 10:420/428 of query aligns to 8:408/410 of 6yeiF
- binding 2-oxoglutaric acid: K66 (= K68), G68 (= G70), M87 (= M89), K90 (= K92), K102 (= K104), A140 (= A142), V341 (= V353), S344 (= S356)
- binding potassium ion: S27 (≠ R29), L28 (= L30), I30 (≠ Y32), P31 (= P33), F32 (≠ K34)
- binding nicotinamide-adenine-dinucleotide: R70 (= R72), D142 (= D144), M143 (= M145), T185 (= T188), F214 (= F217), G215 (= G218), N216 (= N219), V217 (≠ A220), D237 (= D240), I238 (≠ S241), A288 (= A300), A289 (= A301), A311 (= A323), N312 (= N324), N337 (= N349)
6yeiA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
43% identity, 96% coverage: 10:420/428 of query aligns to 7:407/409 of 6yeiA
- binding potassium ion: S26 (≠ R29), L27 (= L30), I29 (≠ Y32), P30 (= P33)
- binding nicotinamide-adenine-dinucleotide: T184 (= T188), F213 (= F217), G214 (= G218), N215 (= N219), V216 (≠ A220), D236 (= D240), I237 (≠ S241), A288 (= A301), L289 (= L302), A310 (= A323), N311 (= N324), N336 (= N349)
P28997 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Peptoniphilus asaccharolyticus (Peptostreptococcus asaccharolyticus) (see 2 papers)
41% identity, 98% coverage: 1:420/428 of query aligns to 1:419/421 of P28997
- E243 (≠ D240) 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)
41% identity, 98% coverage: 1:420/428 of query aligns to 6:418/420 of P80053
- K254 (≠ Q249) modified: N6-methyllysine
- K260 (= K264) modified: N6-methyllysine
- K372 (≠ Q376) modified: N6-methyllysine
- K391 (≠ E395) modified: N6-methyllysine
- K392 (≠ L396) 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)
43% identity, 95% coverage: 13:420/428 of query aligns to 4:416/418 of 1v9lA
- active site: K102 (= K104), D142 (= D144)
- binding nicotinamide-adenine-dinucleotide: T186 (= T188), Q213 (= Q215), G216 (= G218), N217 (= N219), V218 (≠ A220), D238 (= D240), I239 (≠ S241), A296 (= A301), I297 (≠ L302), A318 (= A323), N319 (= N324), N344 (= N349)
8karA Glutamate dehydrogenase-akg
41% identity, 98% coverage: 2:420/428 of query aligns to 1:412/414 of 8karA
- binding 2-oxoglutaric acid: K67 (= K68), G69 (= G70), M88 (= M89), K91 (= K92), K103 (= K104), A141 (= A142), N314 (= N324), G342 (= G352), V343 (= V353), S346 (= S356)
- binding nicotinamide-adenine-dinucleotide: R71 (= R72), D143 (= D144), I144 (≠ M145), R183 (= R184), T187 (= T188), F216 (= F217), G217 (= G218), N218 (= N219), V219 (≠ A220), D239 (= D240), I240 (≠ S241), N276 (= N286), A291 (= A301), A313 (= A323), N314 (= N324), N339 (= N349)
8kaoC Glutamate dehydrogenase-69o
42% identity, 96% coverage: 11:420/428 of query aligns to 8:410/412 of 8kaoC
- binding 2-oxopentanoic acid: G66 (= G69), G67 (= G70), M86 (= M89), K89 (= K92), K101 (= K104), A139 (= A142), N312 (= N324), N337 (= N349), V341 (= V353), S344 (= S356)
- binding nicotinamide-adenine-dinucleotide: P140 (= P143), D141 (= D144), I142 (≠ M145), T185 (= T188), F214 (= F217), G215 (= G218), N216 (= N219), V217 (≠ A220), D237 (= D240), I238 (≠ S241), N274 (= N286), A289 (= A301), A311 (= A323), N312 (= N324)
3aoeF Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
36% identity, 98% coverage: 4:421/428 of query aligns to 11:415/417 of 3aoeF
Sites not aligning to the query:
6dhlA Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ecg) (see paper)
41% identity, 85% coverage: 1:363/428 of query aligns to 7:383/496 of 6dhlA
- binding (2R,3S)-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate: H80 (≠ T63), R81 (= R64), C110 (= C93), D114 (≠ S97), V115 (≠ L98), K382 (≠ Q362)
Sites not aligning to the query:
Query Sequence
>WP_011613632.1 NCBI__GCF_000014265.1:WP_011613632.1
MSDSLFDDASRRLERALQYVSLSEDTKERLKYPKATLIVSIPVRMDDGSLRVFQGYRVRY
DDTRGPTKGGIRYHPNVSIDEVKSLAFWMTFKCAVVSLPFGGAKGGITVNPKELSRMELE
RLSRGYIDAIADFIGPDTDIPAPDMYTNPMIMGWMMDEYSIIRRQLSPAVITGKPVSIGG
SLGRNTATAMGAFFAIETIMPKFEYTPEKTTVAIQGFGNAGAFLAELLCLHGYKVVAVSD
SQGGIYSAQGLDIPSIRQYKEVNKQIQAVYCKDSVCNIVEHTVLTNEELLALDVDILIPA
ALENQITEENVKDIQAKFIFEAANGPTTSGADKILEDRGVYVFPDILINAGGVTVSYFEW
VQNRSGLYWTLDEVNQKLKAKMVAETENIWQISQELSISMRTAAYVHGLDRLGQAINAKG
TRAFYAKR
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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