SitesBLAST
Comparing 8500598 FitnessBrowser__Miya:8500598 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)
Q54VI3 Glutamate dehydrogenase 2; NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Dictyostelium discoideum (Social amoeba) (see paper)
31% identity, 54% coverage: 408:952/1017 of query aligns to 477:1024/1042 of Q54VI3
- R763 (≠ Q708) modified: ADP-ribosylarginine; by Legionella Lart1; mutation to A: Abolishes ADP-ribosylation by Lart1.
1v9lA L-glutamate dehydrogenase from pyrobaculum islandicum complexed with NAD (see paper)
30% identity, 35% coverage: 475:831/1017 of query aligns to 53:367/418 of 1v9lA
- active site: K102 (= K530), D142 (= D583)
- binding nicotinamide-adenine-dinucleotide: T186 (= T626), Q213 (≠ T655), G216 (= G660), N217 (≠ D661), V218 (= V662), D238 (= D685), I239 (≠ G686), A296 (≠ G754), I297 (≠ R756), A318 (= A784), N319 (= N785), N344 (= N810)
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)
26% identity, 35% coverage: 490:840/1017 of query aligns to 76:383/424 of P39633
- E93 (= E509) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (≠ G536) 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 (≠ D554) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ N585) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (≠ G664) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ G783) 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)
24% identity, 34% coverage: 475:820/1017 of query aligns to 67:364/427 of P50735
- VKA 97:99 (≠ VKG 510:512) mutation Missing: In gudB1; gains glutamate dehydrogenase activity, restores growth on proline, arginine, ornithine.
6yehA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in apo form (see paper)
26% identity, 34% coverage: 474:820/1017 of query aligns to 51:346/410 of 6yehA
Sites not aligning to the query:
6yeiF Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
26% identity, 34% coverage: 474:820/1017 of query aligns to 52:347/410 of 6yeiF
- binding 2-oxoglutaric acid: K66 (≠ R485), G68 (= G487), M87 (≠ Q517), K90 (= K520), K102 (= K530), A140 (= A564), V341 (= V814), S344 (= S817)
- binding nicotinamide-adenine-dinucleotide: R70 (= R489), D142 (= D583), M143 (≠ E584), T185 (= T626), F214 (≠ K659), G215 (= G660), N216 (≠ D661), V217 (= V662), D237 (= D685), I238 (≠ G686), A288 (= A753), A289 (vs. gap), A311 (= A784), N312 (= N785), N337 (= N810)
Sites not aligning to the query:
6yeiA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
26% identity, 34% coverage: 474:820/1017 of query aligns to 51:346/409 of 6yeiA
- binding nicotinamide-adenine-dinucleotide: T184 (= T626), F213 (≠ K659), G214 (= G660), N215 (≠ D661), V216 (= V662), D236 (= D685), I237 (≠ G686), A288 (vs. gap), L289 (vs. gap), A310 (= A784), N311 (= N785), N336 (= N810)
Sites not aligning to the query:
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction
25% identity, 36% coverage: 475:838/1017 of query aligns to 56:375/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (≠ R485), M90 (≠ Y515), K105 (= K530), A143 (= A564), D145 (= D583), S351 (= S817)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R489), D145 (= D583), V146 (≠ E584), Y147 (≠ N585), T191 (= T626), Y220 (≠ K659), G221 (= G660), N222 (≠ D661), A223 (≠ V662), D244 (= D685), S245 (≠ G686), K264 (≠ A717), N281 (= N739), A295 (= A753), A296 (≠ G754), I297 (≠ G755), N319 (= N785), N344 (= N810)
8xcsA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADPH, akg and nh4 in the initial stage of reaction
25% identity, 36% coverage: 475:838/1017 of query aligns to 55:374/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (≠ R485), G70 (= G487), M89 (≠ Y515), K92 (≠ Q518), K104 (= K530), A142 (= A564), D144 (= D583), G346 (= G813), S350 (= S817)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R489), K112 (≠ L538), P143 (= P582), D144 (= D583), V145 (≠ E584), Y146 (≠ N585), T190 (= T626), Y219 (≠ K659), G220 (= G660), N221 (≠ D661), A222 (≠ V662), D243 (= D685), S244 (≠ G686), K263 (≠ A717), A295 (≠ G754), I296 (≠ G755), N318 (= N785)
P49448 Glutamate dehydrogenase 2, mitochondrial; GDH 2; EC 1.4.1.3 from Homo sapiens (Human) (see 2 papers)
25% identity, 34% coverage: 477:825/1017 of query aligns to 139:446/558 of P49448
- C172 (≠ N521) modified: ADP-ribosylcysteine
Sites not aligning to the query:
- 1:53 modified: transit peptide, Mitochondrion
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction
25% identity, 36% coverage: 475:838/1017 of query aligns to 53:372/416 of 8xcoA
6dhdA Bovine glutamate dehydrogenase complexed with nadh, gtp, glutamate (see paper)
24% identity, 34% coverage: 477:825/1017 of query aligns to 82:389/501 of 6dhdA
- active site: K126 (= K530), D168 (= D583)
- binding glutamic acid: K90 (≠ R485), M111 (≠ Q517), K114 (= K520), K126 (= K530), A166 (= A564), V378 (= V814), S381 (= S817)
- binding guanosine-5'-triphosphate: H209 (= H620), S213 (≠ G624), R217 (≠ I628), H258 (≠ N665), R261 (= R668), Y262 (≠ L669), R265 (≠ E672), E292 (≠ L702)
- binding 1,4-dihydronicotinamide adenine dinucleotide: H85 (≠ Y480), R86 (= R481), R94 (= R489), A116 (≠ K522), D119 (= D523), V120 (≠ I524), D168 (= D583), M169 (≠ E584), H195 (≠ M610), Q205 (vs. gap), G206 (vs. gap), T215 (= T626), Q250 (≠ T655), F252 (≠ K659), G253 (= G660), N254 (≠ D661), V255 (= V662), E275 (≠ D685), S276 (≠ G686), A326 (≠ G754), A348 (= A784), N349 (= N785), N374 (= N810), K387 (≠ G823), N388 (≠ G824)
Sites not aligning to the query:
3etgA Glutamate dehydrogenase complexed with gw5074 (see paper)
24% identity, 34% coverage: 477:825/1017 of query aligns to 82:389/501 of 3etgA
- active site: K126 (= K530), D168 (= D583)
- binding glutamic acid: K90 (≠ R485), M111 (≠ Q517), K114 (= K520), A166 (= A564), V378 (= V814), S381 (= S817)
- binding guanosine-5'-triphosphate: H209 (= H620), G210 (≠ K621), S213 (≠ G624), R217 (≠ I628), R261 (= R668), R265 (≠ E672), E292 (≠ L702)
- binding (3E)-3-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-5-iodo-1,3-dihydro-2H-indol-2-one: R146 (≠ N550), R147 (≠ S551), M150 (vs. gap)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: D168 (= D583), M169 (≠ E584), R211 (≠ Q622), T215 (= T626), Q250 (≠ T655), G253 (= G660), V255 (= V662), E275 (≠ D685), S276 (≠ G686), A326 (≠ G754), G347 (= G783), A348 (= A784), N349 (= N785), N374 (= N810)
3etdA Structure of glutamate dehydrogenase complexed with bithionol (see paper)
24% identity, 34% coverage: 477:825/1017 of query aligns to 82:389/501 of 3etdA
- active site: K126 (= K530), D168 (= D583)
- binding 2,2'-sulfanediylbis(4,6-dichlorophenol): R146 (≠ N550), R146 (≠ N550), R147 (≠ S551), D181 (≠ E596), S185 (≠ Q600)
- binding glutamic acid: K90 (≠ R485), G92 (= G487), M111 (≠ Q517), K114 (= K520), K126 (= K530), A166 (= A564), S381 (= S817)
- binding guanosine-5'-triphosphate: H209 (= H620), G210 (≠ K621), I212 (≠ Y623), R217 (≠ I628), R261 (= R668), R265 (≠ E672), E292 (≠ L702)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R94 (= R489), D168 (= D583), M169 (≠ E584), R211 (≠ Q622), T215 (= T626), Q250 (≠ T655), F252 (≠ K659), G253 (= G660), V255 (= V662), E275 (≠ D685), S276 (≠ G686), A326 (≠ G754), A348 (= A784), N349 (= N785), N374 (= N810)
Sites not aligning to the query:
6dhmA Bovine glutamate dehydrogenase complexed with zinc (see paper)
24% identity, 34% coverage: 477:825/1017 of query aligns to 82:389/495 of 6dhmA
- binding glutamic acid: K90 (≠ R485), G92 (= G487), M111 (≠ Q517), K114 (= K520), A166 (= A564), D168 (= D583), R211 (≠ Q622), V378 (= V814), S381 (= S817)
- binding guanosine-5'-triphosphate: H209 (= H620), S213 (≠ G624), H258 (≠ N665), R261 (= R668), Y262 (≠ L669), R265 (≠ E672), K289 (≠ A699), E292 (≠ L702)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: D168 (= D583), M169 (≠ E584), S170 (≠ N585), R211 (≠ Q622), Q250 (≠ T655), G251 (= G656), F252 (≠ K659), G253 (= G660), N254 (≠ D661), V255 (= V662), E275 (≠ D685), S276 (≠ G686), A326 (≠ G754), G347 (= G783), A348 (= A784), N349 (= N785), N374 (= N810)
- binding zinc ion: H209 (= H620)
Sites not aligning to the query:
8ar7A Bovine glutamate dehydrogenase in ternary complex with the allosteric activators adp and leucine (see paper)
24% identity, 34% coverage: 477:825/1017 of query aligns to 78:385/496 of 8ar7A
Sites not aligning to the query:
- binding adenosine-5'-diphosphate: 389, 392, 455, 484, 488
- binding potassium ion: 47, 48, 49, 50, 51, 52
- binding leucine: 493, 494, 495
6dhlA Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ecg) (see paper)
24% identity, 34% coverage: 477:825/1017 of query aligns to 77:384/496 of 6dhlA
- binding (2R,3S)-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate: H80 (≠ Y480), R81 (= R481), C110 (≠ N521), D114 (= D523), V115 (≠ I524), K382 (≠ G823)
Sites not aligning to the query:
3eteA Crystal structure of bovine glutamate dehydrogenase complexed with hexachlorophene (see paper)
24% identity, 34% coverage: 477:825/1017 of query aligns to 79:386/495 of 3eteA
- active site: K123 (= K530), D165 (= D583)
- binding glutamic acid: K87 (≠ R485), G89 (= G487), M108 (≠ Q517), K111 (= K520), K123 (= K530), A163 (= A564), R208 (≠ Q622), V375 (= V814), S378 (= S817)
- binding guanosine-5'-triphosphate: I209 (≠ Y623), S210 (≠ G624), R214 (≠ I628), H255 (≠ N665), R258 (= R668), Y259 (≠ L669)
- binding 2,2'-methanediylbis(3,4,6-trichlorophenol): T183 (≠ R601), I184 (≠ G602), Y187 (≠ W605)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R91 (= R489), K131 (≠ L538), D165 (= D583), M166 (≠ E584), R208 (≠ Q622), F249 (≠ K659), G250 (= G660), V252 (= V662), E272 (≠ D685), S273 (≠ G686), A323 (≠ G754), A345 (= A784), N346 (= N785), N371 (= N810)
Sites not aligning to the query:
P00366 Glutamate dehydrogenase 1, mitochondrial; GDH 1; EC 1.4.1.3 from Bos taurus (Bovine) (see 4 papers)
24% identity, 34% coverage: 477:825/1017 of query aligns to 139:446/558 of P00366
- QHR 141:143 (≠ RYR 479:481) binding
- K147 (≠ R485) binding
- K162 (= K511) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- K171 (= K520) binding
- D176 (= D523) binding
- K183 (= K530) modified: N6-acetyllysine; alternate
- K191 (≠ L538) modified: N6-acetyllysine; alternate
- H252 (≠ M610) binding
- H266 (= H620) binding
- S270 (≠ G624) binding
- Y319 (≠ L669) binding
- R322 (≠ E672) binding
- K363 (≠ P716) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- K365 (≠ R718) modified: N6-acetyllysine; alternate
- K386 (≠ P757) modified: N6-acetyllysine
- K399 (≠ V780) modified: N6-acetyllysine
- K415 (= K794) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- S438 (= S817) binding
- N444 (≠ G823) binding
Sites not aligning to the query:
- 1:57 modified: transit peptide, Mitochondrion
- 84 modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- 90 modified: N6-acetyllysine
- 110 modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- 450 binding
- 457 modified: N6-acetyllysine; alternate; modified: N6-malonyllysine; alternate; modified: N6-succinyllysine; alternate
- 480 modified: N6-acetyllysine; alternate
- 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
P00367 Glutamate dehydrogenase 1, mitochondrial; GDH 1; EC 1.4.1.3 from Homo sapiens (Human) (see 9 papers)
24% identity, 34% coverage: 477:825/1017 of query aligns to 139:446/558 of P00367
- K147 (≠ R485) modified: N6-(2-hydroxyisobutyryl)lysine
- C172 (≠ N521) modified: ADP-ribosylcysteine
- S270 (≠ G624) to C: in HHF6; diminished sensitivity to GTP
- R274 (≠ I628) to C: in HHF6; diminished sensitivity to GTP; dbSNP:rs56275071
- R318 (= R668) to T: in HHF6; diminished sensitivity to GTP
- R322 (≠ E672) 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.
Query Sequence
>8500598 FitnessBrowser__Miya:8500598
MAESHAKGVEEALSLVKGGLGGIADQVVPWFFANMPDYYLRTHSVTEQVHHLQAIISGRV
VTDNHAVRLASPDGRKITYISPSASRDLHGILAGLLGEHIETARIYTTADGQLGLNEFLL
APQPRAGSLRTAEGDDLFSAALDAMRASGELPETDMTAFAAFLAAANAEYVEKFDPVRAA
RHFRLLREIGGGDDTGLLIEQCSAPTIPAAPAASEATGGTGGVGTVLPAEPCDIRRETRI
VVAMRHPPATGLLLQIARIMRRLDITVHRSYADTFADESGETAIMSFYVSHKGDLILDDS
ALWQNLRKKLRLVKWFAPHELEILADEESWPIKRIMLLQAACGFAHVFLAKDNQWAFSTQ
NVVRIVLARRAETAALVDWFEARFDPTLGDREATARRLEADATDAVNAVADERERAVLLM
IQRFFRHVLRTNYFLDTIYGLSFRLDPEFLPPAYRYEGEELPFGIFFFHAPGGLGFHIRY
RDMARGGVRVVPTRTQEQFELESNRLYDEVKGLAYAQQVKNKDIPEGGAKAVILLGPLGD
VGLAVSSVINSLLDVVLPGQDTPALPGVVDYLGREEIIYCGPDENIQPAHIAWMVERARQ
RGYRWPSAFMSSKAGAGINHKQYGVTSIGVMVFAEEMLRHLGIDPFTQPFTVKLTGGPKG
DVAGNLMRLMFETYGDNARIVAVSDGHGGAWDPDGLDRAELLRLVDAQRSISAFDPARLR
GEGAWVAVSDTPEGVRRRNTLHNTAHADIFIPAGGRPDTINTRNWHDFFDRGGVPTARAV
IEGANLFVAPEARKRLAERGVLVVHGSSANKTGVICSSYEVLGGLVMTDEEFIAHKDRFV
AEVLDILRVRARDEARLLLAEIRRCDGCKALHEISVDVSLEMNAVADALYAALMARGEPV
EADPVLRQVLLGYLPPVLVERFPERIFERIPLRHQYALVAAHTASRIVYAEGAGWLAPLA
RQRDAESVARAWLREDGRIRDLIAAVSRSGLPEAGAVVHLLERGARKRATEEALGLE
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