SitesBLAST
Comparing HSERO_RS19260 FitnessBrowser__HerbieS:HSERO_RS19260 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, 98% coverage: 9:430/430 of query aligns to 2:416/416 of 4xgiA
- active site: K112 (= K119), D152 (= D159)
- binding 2-oxoglutaric acid: K76 (= K83), G78 (= G85), M97 (= M104), K100 (= K107), K112 (= K119), A150 (= A157), R192 (= R199), S355 (= S363)
- binding nicotinamide-adenine-dinucleotide: R80 (= R87), D152 (= D159), V153 (= V160), T196 (= T203), G224 (= G231), G226 (= G233), N227 (= N234), V228 (= V235), D248 (= D255), H249 (= H256), A299 (= A307), A300 (= A308), A322 (= A330), N323 (= N331), N348 (= N356)
3aoeB Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
67% identity, 98% coverage: 11:430/430 of query aligns to 7:424/424 of 3aoeB
3aogA Crystal structure of glutamate dehydrogenase (gdhb) from thermus thermophilus (glu bound form)
67% identity, 98% coverage: 11:430/430 of query aligns to 4:421/421 of 3aogA
- active site: K111 (= K119), D151 (= D159)
- binding glutamic acid: A70 (≠ S78), G77 (= G85), M96 (= M104), K111 (= K119), P150 (= P158), D151 (= D159), D164 (= D172), M168 (= M176), S354 (= S363), R417 (= R426), G418 (= G427), L419 (= L428), Y420 (= Y429)
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction
49% identity, 95% coverage: 18:427/430 of query aligns to 1:412/416 of 8xcoA
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, 95% coverage: 18:427/430 of query aligns to 3:414/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (= K83), G70 (= G85), M89 (= M104), K92 (= K107), K104 (= K119), A142 (= A157), D144 (= D159), G346 (= G359), S350 (= S363)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R87), K112 (= K127), P143 (= P158), D144 (= D159), V145 (= V160), Y146 (≠ N161), T190 (= T203), Y219 (≠ F232), G220 (= G233), N221 (= N234), A222 (≠ V235), D243 (= D255), S244 (≠ H256), K263 (≠ V275), A295 (= A308), I296 (≠ L309), N318 (= N331)
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction
49% identity, 95% coverage: 18:427/430 of query aligns to 4:415/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K83), M90 (= M104), K105 (= K119), A143 (= A157), D145 (= D159), S351 (= S363)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R87), D145 (= D159), V146 (= V160), Y147 (≠ N161), T191 (= T203), Y220 (≠ F232), G221 (= G233), N222 (= N234), A223 (≠ V235), D244 (= D255), S245 (≠ H256), K264 (≠ V275), N281 (≠ D292), A295 (= A307), A296 (= A308), I297 (≠ L309), N319 (= N331), N344 (= N356)
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)
48% identity, 91% coverage: 35:427/430 of query aligns to 32:422/424 of P39633
- E93 (= E96) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (= D125) 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 (≠ I147) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ N161) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (≠ G237) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ G329) 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.
P50735 Cryptic catabolic NAD-specific glutamate dehydrogenase GudB; NAD-GDH; EC 1.4.1.2 from Bacillus subtilis (strain 168) (see paper)
48% identity, 93% coverage: 28:427/430 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.
6yeiF Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
49% identity, 91% coverage: 35:427/430 of query aligns to 18:408/410 of 6yeiF
- binding 2-oxoglutaric acid: K66 (= K83), G68 (= G85), M87 (= M104), K90 (= K107), K102 (= K119), A140 (= A157), V341 (= V360), S344 (= S363)
- binding potassium ion: S27 (≠ T44), L28 (= L45), I30 (≠ R47), P31 (= P48), F32 (≠ K49)
- binding nicotinamide-adenine-dinucleotide: R70 (= R87), D142 (= D159), M143 (≠ V160), T185 (= T203), F214 (= F232), G215 (= G233), N216 (= N234), V217 (= V235), D237 (= D255), I238 (≠ H256), A288 (= A307), A289 (= A308), A311 (= A330), N312 (= N331), N337 (= N356)
6yeiA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
49% identity, 91% coverage: 35:427/430 of query aligns to 17:407/409 of 6yeiA
- binding potassium ion: S26 (≠ T44), L27 (= L45), I29 (≠ R47), P30 (= P48)
- binding nicotinamide-adenine-dinucleotide: T184 (= T203), F213 (= F232), G214 (= G233), N215 (= N234), V216 (= V235), D236 (= D255), I237 (≠ H256), A288 (= A308), L289 (= L309), A310 (= A330), N311 (= N331), N336 (= N356)
6yehA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in apo form (see paper)
49% identity, 91% coverage: 35:427/430 of query aligns to 17:407/410 of 6yehA
8owmC Crystal structure of glutamate dehydrogenase 2 from arabidopsis thaliana binding ca, NAD and 2,2-dihydroxyglutarate (see paper)
46% identity, 91% coverage: 35:427/430 of query aligns to 20:410/413 of 8owmC
- binding calcium ion: S29 (≠ T44), I32 (≠ R47)
- binding nicotinamide-adenine-dinucleotide: D144 (= D159), M145 (≠ V160), R183 (= R199), T187 (= T203), F216 (= F232), G217 (= G233), N218 (= N234), V219 (= V235), D239 (= D255), I240 (≠ H256), C290 (≠ A307), A291 (= A308), A313 (= A330), N314 (= N331), N339 (= N356)
- binding 2,2-bis(oxidanyl)pentanedioic acid: K68 (= K83), G70 (= G85), M89 (= M104), K92 (= K107), K104 (= K119), A142 (= A157), R183 (= R199), N314 (= N331), V343 (= V360), S346 (= S363)
P28997 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Peptoniphilus asaccharolyticus (Peptostreptococcus asaccharolyticus) (see 2 papers)
44% identity, 94% coverage: 26:429/430 of query aligns to 13:421/421 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)
44% identity, 94% coverage: 23:428/430 of query aligns to 10:419/420 of P80053
- K254 (≠ G264) modified: N6-methyllysine
- K260 (≠ A270) modified: N6-methyllysine
- K372 (≠ L383) modified: N6-methyllysine
- K391 (≠ E402) modified: N6-methyllysine
- K392 (= K403) 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)
42% identity, 98% coverage: 11:430/430 of query aligns to 3:417/417 of 3aoeF
1v9lA L-glutamate dehydrogenase from pyrobaculum islandicum complexed with NAD (see paper)
45% identity, 90% coverage: 43:427/430 of query aligns to 26:416/418 of 1v9lA
- active site: K102 (= K119), D142 (= D159)
- binding nicotinamide-adenine-dinucleotide: T186 (= T203), Q213 (= Q230), G216 (= G233), N217 (= N234), V218 (= V235), D238 (= D255), I239 (≠ H256), A296 (= A308), I297 (≠ L309), A318 (= A330), N319 (= N331), N344 (= N356)
P49448 Glutamate dehydrogenase 2, mitochondrial; GDH 2; EC 1.4.1.3 from Homo sapiens (Human) (see 2 papers)
42% identity, 82% coverage: 42:393/430 of query aligns to 106:474/558 of P49448
- C172 (≠ N108) modified: ADP-ribosylcysteine
Sites not aligning to the query:
- 1:53 modified: transit peptide, Mitochondrion
6dhdA Bovine glutamate dehydrogenase complexed with nadh, gtp, glutamate (see paper)
43% identity, 81% coverage: 45:393/430 of query aligns to 52:417/501 of 6dhdA
- active site: K126 (= K119), D168 (= D159)
- binding glutamic acid: K90 (= K83), M111 (= M104), K114 (= K107), K126 (= K119), A166 (= A157), V378 (= V360), S381 (= S363)
- binding guanosine-5'-triphosphate: H209 (≠ L197), S213 (≠ E201), R217 (= R205), H258 (≠ I238), R261 (= R241), Y262 (≠ L242), R265 (≠ E245), E292 (≠ Q272)
- binding 1,4-dihydronicotinamide adenine dinucleotide: H85 (≠ S78), R86 (= R79), R94 (= R87), A116 (= A109), D119 (≠ N112), V120 (= V113), D168 (= D159), M169 (≠ V160), H195 (≠ S183), Q205 (≠ L193), G206 (= G194), T215 (= T203), Q250 (= Q230), F252 (= F232), G253 (= G233), N254 (= N234), V255 (= V235), E275 (≠ D255), S276 (≠ H256), A326 (= A308), A348 (= A330), N349 (= N331), N374 (= N356), K387 (≠ Q369), N388 (≠ D370), H391 (≠ S373), S393 (vs. gap)
Sites not aligning to the query:
3etgA Glutamate dehydrogenase complexed with gw5074 (see paper)
43% identity, 81% coverage: 45:393/430 of query aligns to 52:417/501 of 3etgA
- active site: K126 (= K119), D168 (= D159)
- binding glutamic acid: K90 (= K83), M111 (= M104), K114 (= K107), A166 (= A157), V378 (= V360), S381 (= S363)
- binding guanosine-5'-triphosphate: H209 (≠ L197), G210 (= G198), S213 (≠ E201), R217 (= R205), R261 (= R241), R265 (≠ E245), E292 (≠ Q272)
- binding (3E)-3-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-5-iodo-1,3-dihydro-2H-indol-2-one: R146 (= R139), R147 (= R140), M150 (≠ S143)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: D168 (= D159), M169 (≠ V160), R211 (= R199), T215 (= T203), Q250 (= Q230), G253 (= G233), V255 (= V235), E275 (≠ D255), S276 (≠ H256), A326 (= A308), G347 (= G329), A348 (= A330), N349 (= N331), N374 (= N356)
3etdA Structure of glutamate dehydrogenase complexed with bithionol (see paper)
43% identity, 81% coverage: 45:393/430 of query aligns to 52:417/501 of 3etdA
- active site: K126 (= K119), D168 (= D159)
- binding 2,2'-sulfanediylbis(4,6-dichlorophenol): R146 (= R139), R146 (= R139), R147 (= R140), D181 (= D172), S185 (≠ M176)
- binding glutamic acid: K90 (= K83), G92 (= G85), M111 (= M104), K114 (= K107), K126 (= K119), A166 (= A157), S381 (= S363)
- binding guanosine-5'-triphosphate: H209 (≠ L197), G210 (= G198), I212 (≠ H200), R217 (= R205), R261 (= R241), R265 (≠ E245), E292 (≠ Q272)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R94 (= R87), D168 (= D159), M169 (≠ V160), R211 (= R199), T215 (= T203), Q250 (= Q230), F252 (= F232), G253 (= G233), V255 (= V235), E275 (≠ D255), S276 (≠ H256), A326 (= A308), A348 (= A330), N349 (= N331), N374 (= N356)
Sites not aligning to the query:
Query Sequence
>HSERO_RS19260 FitnessBrowser__HerbieS:HSERO_RS19260
MSNVPNHEVPSYLVPHGIGPWGVYLEQIDRVTPYLGSLARWVETLKRPKRMLVVDVPIER
DDGTIAHFEGYRVQHNTSRGPGKGGVRFHQDVTLSEVMALSAWMTIKNAAVNVPYGGAKG
GIRVDPKTLSRGELQRVTRRYTSEIGIIIGPNKDIPAPDVNTDSQIMAWMMDTYSMNQGS
TSSGVVTGKPISLGGSLGRHEATGRGVFVVGCEAAAKRGLDIKDAKVAVQGFGNVGGIAA
RLFAEAGSKVVAVQDHVTTVFNAGGLDVPALQAYVAKNGSVKGFAGADEITDRAQFWSVD
CDILVPAALEQQITEANANQIKAKIILEGANGPTTPAADDILRDKGVLIVPDVIANAGGV
TVSYFEWVQDFSSFFWTEDEINLRLTRIMREAFAAVWQLADEKKVSLRTAAFIVACTRVL
QAREMRGLYP
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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