SitesBLAST
Comparing AZOBR_RS22625 FitnessBrowser__azobra:AZOBR_RS22625 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
48% identity, 98% coverage: 3:412/419 of query aligns to 5:415/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K67), M90 (= M88), K105 (= K103), A143 (= A141), D145 (= D143), S351 (= S348)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R71), D145 (= D143), V146 (= V144), Y147 (= Y145), T191 (= T187), Y220 (= Y216), G221 (= G217), N222 (= N218), A223 (= A219), D244 (= D239), S245 (= S240), K264 (= K259), N281 (≠ G278), A295 (= A292), A296 (= A293), I297 (≠ L294), N319 (= N316), N344 (= N341)
8xcsA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADPH, akg and nh4 in the initial stage of reaction
48% identity, 98% coverage: 3:412/419 of query aligns to 4:414/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (= K67), G70 (= G69), M89 (= M88), K92 (= K91), K104 (= K103), A142 (= A141), D144 (= D143), G346 (= G344), S350 (= S348)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R71), K112 (≠ H111), P143 (= P142), D144 (= D143), V145 (= V144), Y146 (= Y145), T190 (= T187), Y219 (= Y216), G220 (= G217), N221 (= N218), A222 (= A219), D243 (= D239), S244 (= S240), K263 (= K259), A295 (= A293), I296 (≠ L294), N318 (= N316)
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction
48% identity, 98% coverage: 3:412/419 of query aligns to 2:412/416 of 8xcoA
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, 97% coverage: 3:407/419 of query aligns to 16:417/424 of P39633
- E27 (= E14) mutation to F: Increase of thermostability 8 degrees Celsius higher than that of the wild-type.
- E93 (= E80) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (= D109) 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 (≠ G131) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (= Y145) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (≠ F221) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ L314) 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)
45% identity, 97% coverage: 3:407/419 of query aligns to 16:420/427 of P50735
- VKA 97:99 (≠ VTT 81:83) mutation Missing: In gudB1; gains glutamate dehydrogenase activity, restores growth on proline, arginine, ornithine.
3aoeB Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
48% identity, 93% coverage: 27:415/419 of query aligns to 38:424/424 of 3aoeB
3aogA Crystal structure of glutamate dehydrogenase (gdhb) from thermus thermophilus (glu bound form)
46% identity, 97% coverage: 10:415/419 of query aligns to 18:421/421 of 3aogA
- active site: K111 (= K103), D151 (= D143)
- binding glutamic acid: A70 (≠ T62), G77 (= G69), M96 (= M88), K111 (= K103), P150 (= P142), D151 (= D143), D164 (= D156), M168 (≠ S160), S354 (= S348), R417 (≠ H411), G418 (= G412), L419 (≠ T413), Y420 (≠ Q414)
6yeiF Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
43% identity, 95% coverage: 15:412/419 of query aligns to 14:408/410 of 6yeiF
- binding 2-oxoglutaric acid: K66 (= K67), G68 (= G69), M87 (= M88), K90 (= K91), K102 (= K103), A140 (= A141), V341 (= V345), S344 (= S348)
- binding potassium ion: S27 (≠ K28), L28 (= L29), I30 (≠ Y31), P31 (≠ A32), F32 (≠ K33)
- binding nicotinamide-adenine-dinucleotide: R70 (= R71), D142 (= D143), M143 (≠ V144), T185 (= T187), F214 (≠ Y216), G215 (= G217), N216 (= N218), V217 (≠ A219), D237 (= D239), I238 (≠ S240), A288 (= A292), A289 (= A293), A311 (= A315), N312 (= N316), N337 (= N341)
6yeiA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
43% identity, 95% coverage: 15:412/419 of query aligns to 13:407/409 of 6yeiA
- binding potassium ion: S26 (≠ K28), L27 (= L29), I29 (≠ Y31), P30 (≠ A32)
- binding nicotinamide-adenine-dinucleotide: T184 (= T187), F213 (≠ Y216), G214 (= G217), N215 (= N218), V216 (≠ A219), D236 (= D239), I237 (≠ S240), A288 (= A293), L289 (= L294), A310 (= A315), N311 (= N316), N336 (= N341)
6yehA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in apo form (see paper)
43% identity, 95% coverage: 15:412/419 of query aligns to 13:407/410 of 6yehA
8owmC Crystal structure of glutamate dehydrogenase 2 from arabidopsis thaliana binding ca, NAD and 2,2-dihydroxyglutarate (see paper)
41% identity, 98% coverage: 3:412/419 of query aligns to 4:410/413 of 8owmC
- binding calcium ion: S29 (≠ K28), I32 (≠ Y31)
- binding nicotinamide-adenine-dinucleotide: D144 (= D143), M145 (≠ V144), R183 (= R183), T187 (= T187), F216 (≠ Y216), G217 (= G217), N218 (= N218), V219 (≠ A219), D239 (= D239), I240 (≠ S240), C290 (≠ A292), A291 (= A293), A313 (= A315), N314 (= N316), N339 (= N341)
- binding 2,2-bis(oxidanyl)pentanedioic acid: K68 (= K67), G70 (= G69), M89 (= M88), K92 (= K91), K104 (= K103), A142 (= A141), R183 (= R183), N314 (= N316), V343 (= V345), S346 (= S348)
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: 1:412/419 of query aligns to 2:418/420 of P80053
- M2 (= M1) modified: N-acetylmethionine
- K254 (≠ D248) modified: N6-methyllysine
- K260 (≠ A254) modified: N6-methyllysine
- K372 (≠ E368) modified: N6-methyllysine
- K391 (≠ T387) modified: N6-methyllysine
- K392 (= K388) modified: N6-methyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4xgiA Crystal structure of glutamate dehydrogenase from burkholderia thailandensis
41% identity, 97% coverage: 9:415/419 of query aligns to 18:416/416 of 4xgiA
- active site: K112 (= K103), D152 (= D143)
- binding 2-oxoglutaric acid: K76 (= K67), G78 (= G69), M97 (= M88), K100 (= K91), K112 (= K103), A150 (= A141), R192 (= R183), S355 (= S348)
- binding nicotinamide-adenine-dinucleotide: R80 (= R71), D152 (= D143), V153 (= V144), T196 (= T187), G224 (= G215), G226 (= G217), N227 (= N218), V228 (≠ A219), D248 (= D239), H249 (≠ S240), A299 (= A292), A300 (= A293), A322 (= A315), N323 (= N316), N348 (= N341)
1v9lA L-glutamate dehydrogenase from pyrobaculum islandicum complexed with NAD (see paper)
43% identity, 92% coverage: 29:412/419 of query aligns to 28:416/418 of 1v9lA
- active site: K102 (= K103), D142 (= D143)
- binding nicotinamide-adenine-dinucleotide: T186 (= T187), Q213 (= Q214), G216 (= G217), N217 (= N218), V218 (≠ A219), D238 (= D239), I239 (≠ S240), A296 (= A293), I297 (≠ L294), A318 (= A315), N319 (= N316), N344 (= N341)
P28997 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Peptoniphilus asaccharolyticus (Peptostreptococcus asaccharolyticus) (see 2 papers)
36% identity, 97% coverage: 5:412/419 of query aligns to 8:419/421 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.
P49448 Glutamate dehydrogenase 2, mitochondrial; GDH 2; EC 1.4.1.3 from Homo sapiens (Human) (see 2 papers)
37% identity, 88% coverage: 25:392/419 of query aligns to 105:487/558 of P49448
- C172 (= C92) modified: ADP-ribosylcysteine
Sites not aligning to the query:
- 1:53 modified: transit peptide, Mitochondrion
1nqtA Crystal structure of bovine glutamate dehydrogenase-adp complex (see paper)
36% identity, 93% coverage: 2:392/419 of query aligns to 21:425/496 of 1nqtA
Sites not aligning to the query:
P00367 Glutamate dehydrogenase 1, mitochondrial; GDH 1; EC 1.4.1.3 from Homo sapiens (Human) (see 9 papers)
36% identity, 93% coverage: 2:392/419 of query aligns to 83:487/558 of P00367
- K147 (= K67) modified: N6-(2-hydroxyisobutyryl)lysine
- C172 (= C92) modified: ADP-ribosylcysteine
- S270 (≠ D185) to C: in HHF6; diminished sensitivity to GTP
- R274 (= R189) to C: in HHF6; diminished sensitivity to GTP; dbSNP:rs56275071
- R318 (= R225) to T: in HHF6; diminished sensitivity to GTP
- R322 (≠ A229) to C: in HHF6; diminished sensitivity to GTP; to H: in HHF6; diminished sensitivity to GTP; dbSNP:rs121909737
Sites not aligning to the query:
- 1:53 modified: transit peptide, Mitochondrion
- 501 S→A: Reduces activity and inhibition by GTP.
- 507 H → Y: in HHF6; abolishes inhibition by ATP; no effect on activation by ADP; Strongly reduces inhibition by GTP; dbSNP:rs121909730
- 516 R→A: Abolishes activation by ADP.
P00366 Glutamate dehydrogenase 1, mitochondrial; GDH 1; EC 1.4.1.3 from Bos taurus (Bovine) (see 4 papers)
36% identity, 93% coverage: 2:392/419 of query aligns to 83:487/558 of P00366
- K84 (≠ D3) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- K90 (≠ L9) modified: N6-acetyllysine
- K110 (= K30) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- QHR 141:143 (≠ DTR 61:63) binding
- K147 (= K67) binding
- K162 (≠ T82) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- K171 (= K91) binding
- D176 (≠ N96) binding
- K183 (= K103) modified: N6-acetyllysine; alternate
- K191 (≠ H111) modified: N6-acetyllysine; alternate
- H252 (≠ P167) binding
- H266 (≠ L181) binding
- S270 (≠ D185) binding
- Y319 (≠ L226) binding
- R322 (≠ A229) binding
- K363 (≠ G270) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- K365 (≠ R274) modified: N6-acetyllysine; alternate
- K386 (≠ D296) modified: N6-acetyllysine
- K399 (≠ R309) modified: N6-acetyllysine
- K415 (≠ R325) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- S438 (= S348) binding
- N444 (≠ Q354) binding
- S450 (vs. gap) binding
- K457 (≠ Y360) modified: N6-acetyllysine; alternate; modified: N6-malonyllysine; alternate; modified: N6-succinyllysine; alternate
- K480 (≠ D383) modified: N6-acetyllysine; alternate
Sites not aligning to the query:
- 1:57 modified: transit peptide, Mitochondrion
- 503 modified: N6-acetyllysine; alternate; modified: N6-malonyllysine; alternate; modified: N6-succinyllysine; alternate
- 516 binding
- 527 modified: N6-acetyllysine; alternate; modified: N6-malonyllysine; alternate; modified: N6-succinyllysine; alternate
- 545 modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
6dhmA Bovine glutamate dehydrogenase complexed with zinc (see paper)
36% identity, 93% coverage: 2:392/419 of query aligns to 26:430/495 of 6dhmA
- binding glutamic acid: K90 (= K67), G92 (= G69), M111 (= M88), K114 (= K91), A166 (= A141), D168 (= D143), R211 (= R183), V378 (= V345), S381 (= S348)
- binding guanosine-5'-triphosphate: H209 (≠ L181), S213 (≠ D185), H258 (= H222), R261 (= R225), Y262 (≠ L226), R265 (≠ A229), K289 (≠ Q253), E292 (≠ Q256)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: D168 (= D143), M169 (≠ V144), S170 (≠ Y145), R211 (= R183), Q250 (= Q214), G251 (= G215), F252 (≠ Y216), G253 (= G217), N254 (= N218), V255 (≠ A219), E275 (≠ D239), S276 (= S240), A326 (= A293), G347 (≠ L314), A348 (= A315), N349 (= N316), N374 (= N341)
- binding zinc ion: H209 (≠ L181)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS22625 FitnessBrowser__azobra:AZOBR_RS22625
MDDLLSGALSRLDEAAKHVEVDSEVLEKLKYAKETLSVRLSVRMDDGSRRSFPAWRCRYD
DTRGPTKGGIRFHPSSNVEEVTTLAFWMTFKCAVMNLPYGGGKGAVKVDPHSLSKSELER
LSRAYVQAFAGMIGPDRDIPAPDVYTNSMIMGWMADEYSSIVRQPSPAVITGKPLPLGGS
LGRDDATARGGYYLIKHLEEDLRLSGSARRVVIQGYGNAGFHIARLLHADGYRIVGLSDS
RGAIVCEDGLDPQAVQTAKEHGGSVTAYTGNGARAVTGDELLGTPCEILVPAALEDQIHK
GNAGLIKARVVLELANGPVTPDADRILNEAGVIVLPDILANAGGVTVSYFEWVQNRQGYY
WGLDEIHERLRVIMETEGRRVWDMGTTKDIPMRTAAYAHALERLSKAIAAHGTQPFFVG
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