SitesBLAST
Comparing CA265_RS03475 FitnessBrowser__Pedo557:CA265_RS03475 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)
P00367 Glutamate dehydrogenase 1, mitochondrial; GDH 1; EC 1.4.1.3 from Homo sapiens (Human) (see 9 papers)
52% identity, 98% coverage: 7:471/473 of query aligns to 82:555/558 of P00367
- K147 (= K72) modified: N6-(2-hydroxyisobutyryl)lysine
- C172 (= C97) modified: ADP-ribosylcysteine
- S270 (≠ E194) to C: in HHF6; diminished sensitivity to GTP
- R274 (= R198) to C: in HHF6; diminished sensitivity to GTP; dbSNP:rs56275071
- R318 (≠ K242) to T: in HHF6; diminished sensitivity to GTP
- R322 (≠ E246) to C: in HHF6; diminished sensitivity to GTP; to H: in HHF6; diminished sensitivity to GTP; dbSNP:rs121909737
- S501 (= S417) mutation to A: Reduces activity and inhibition by GTP.
- H507 (≠ N423) to Y: in HHF6; abolishes inhibition by ATP; no effect on activation by ADP; Strongly reduces inhibition by GTP; dbSNP:rs121909730
- R516 (≠ H432) mutation to A: Abolishes activation by ADP.
Sites not aligning to the query:
- 1:53 modified: transit peptide, Mitochondrion
1nqtA Crystal structure of bovine glutamate dehydrogenase-adp complex (see paper)
52% identity, 98% coverage: 7:471/473 of query aligns to 20:493/496 of 1nqtA
P49448 Glutamate dehydrogenase 2, mitochondrial; GDH 2; EC 1.4.1.3 from Homo sapiens (Human) (see 2 papers)
51% identity, 98% coverage: 7:471/473 of query aligns to 82:555/558 of P49448
- C172 (= C97) 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)
52% identity, 98% coverage: 7:471/473 of query aligns to 25:498/501 of 6dhdA
- active site: K126 (= K108), D168 (= D150)
- binding glutamic acid: K90 (= K72), M111 (= M93), K114 (= K96), K126 (= K108), A166 (= A148), V378 (= V361), S381 (= S364)
- binding guanosine-5'-triphosphate: H209 (≠ R190), S213 (≠ E194), R217 (= R198), H258 (= H239), R261 (≠ K242), Y262 (≠ F243), R265 (≠ E246), E292 (≠ F273), H450 (≠ N423)
- binding 1,4-dihydronicotinamide adenine dinucleotide: H85 (= H67), R86 (≠ M68), R94 (= R76), A116 (= A98), D119 (≠ N101), V120 (= V102), D168 (= D150), M169 (≠ Y151), H195 (≠ L176), Q205 (≠ L186), G206 (≠ H187), T215 (= T196), Q250 (= Q231), F252 (≠ L233), G253 (= G234), N254 (= N235), V255 (= V236), E275 (= E256), S276 (≠ F257), A326 (= A309), A348 (= A331), N349 (= N332), N374 (= N357), K387 (= K370), N388 (= N371), H391 (= H374), S393 (≠ A376), K488 (= K461), R491 (≠ V464)
3etgA Glutamate dehydrogenase complexed with gw5074 (see paper)
52% identity, 98% coverage: 7:471/473 of query aligns to 25:498/501 of 3etgA
- active site: K126 (= K108), D168 (= D150)
- binding glutamic acid: K90 (= K72), M111 (= M93), K114 (= K96), A166 (= A148), V378 (= V361), S381 (= S364)
- binding guanosine-5'-triphosphate: H209 (≠ R190), G210 (= G191), S213 (≠ E194), R217 (= R198), R261 (≠ K242), R265 (≠ E246), E292 (≠ F273)
- binding (3E)-3-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-5-iodo-1,3-dihydro-2H-indol-2-one: R146 (= R128), R147 (= R129), M150 (≠ T132)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: D168 (= D150), M169 (≠ Y151), R211 (= R192), T215 (= T196), Q250 (= Q231), G253 (= G234), V255 (= V236), E275 (= E256), S276 (≠ F257), A326 (= A309), G347 (= G330), A348 (= A331), N349 (= N332), N374 (= N357)
3etdA Structure of glutamate dehydrogenase complexed with bithionol (see paper)
52% identity, 98% coverage: 7:471/473 of query aligns to 25:498/501 of 3etdA
- active site: K126 (= K108), D168 (= D150)
- binding 2,2'-sulfanediylbis(4,6-dichlorophenol): R146 (= R128), R146 (= R128), R147 (= R129), D181 (= D163), S185 (vs. gap)
- binding glutamic acid: K90 (= K72), G92 (= G74), M111 (= M93), K114 (= K96), K126 (= K108), A166 (= A148), S381 (= S364)
- binding guanosine-5'-triphosphate: H209 (≠ R190), G210 (= G191), I212 (≠ K193), R217 (= R198), R261 (≠ K242), R265 (≠ E246), E292 (≠ F273), H450 (≠ N423)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R94 (= R76), D168 (= D150), M169 (≠ Y151), R211 (= R192), T215 (= T196), Q250 (= Q231), F252 (≠ L233), G253 (= G234), V255 (= V236), E275 (= E256), S276 (≠ F257), A326 (= A309), A348 (= A331), N349 (= N332), N374 (= N357)
6dhlA Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ecg) (see paper)
52% identity, 98% coverage: 7:471/473 of query aligns to 20:493/496 of 6dhlA
- binding (2R,3S)-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate: H80 (= H67), R81 (≠ M68), C110 (= C97), D114 (≠ N101), V115 (= V102), K382 (= K370), S388 (≠ A376), R391 (= R379), R454 (≠ H432), K483 (= K461)
3eteA Crystal structure of bovine glutamate dehydrogenase complexed with hexachlorophene (see paper)
52% identity, 98% coverage: 7:471/473 of query aligns to 22:495/495 of 3eteA
- active site: K123 (= K108), D165 (= D150)
- binding glutamic acid: K87 (= K72), G89 (= G74), M108 (= M93), K111 (= K96), K123 (= K108), A163 (= A148), R208 (= R192), V375 (= V361), S378 (= S364)
- binding guanosine-5'-triphosphate: I209 (≠ K193), S210 (≠ E194), R214 (= R198), H255 (= H239), R258 (≠ K242), Y259 (≠ F243), K443 (≠ M419), H447 (≠ N423)
- binding 2,2'-methanediylbis(3,4,6-trichlorophenol): T183 (= T167), I184 (≠ M168), Y187 (≠ G171)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R91 (= R76), K131 (= K116), D165 (= D150), M166 (≠ Y151), R208 (= R192), F249 (≠ L233), G250 (= G234), V252 (= V236), E272 (= E256), S273 (≠ F257), A323 (= A309), A345 (= A331), N346 (= N332), N371 (= N357)
8ar7A Bovine glutamate dehydrogenase in ternary complex with the allosteric activators adp and leucine (see paper)
52% identity, 98% coverage: 7:471/473 of query aligns to 21:494/496 of 8ar7A
- binding adenosine-5'-diphosphate: H81 (= H67), A112 (= A98), D115 (≠ N101), V116 (= V102), H205 (≠ R190), K383 (= K370), S389 (≠ A376), R392 (= R379), R455 (≠ H432), K484 (= K461), V488 (≠ S465)
- binding potassium ion: I47 (≠ Q34), I48 (= I35), K49 (= K36), P50 (≠ T37), C51 (= C38), N52 (= N39), H78 (= H64), S79 (= S65)
- binding leucine: G493 (= G470), V494 (= V471)
Sites not aligning to the query:
6dhmA Bovine glutamate dehydrogenase complexed with zinc (see paper)
52% identity, 97% coverage: 7:466/473 of query aligns to 25:493/495 of 6dhmA
- binding glutamic acid: K90 (= K72), G92 (= G74), M111 (= M93), K114 (= K96), A166 (= A148), D168 (= D150), R211 (= R192), V378 (= V361), S381 (= S364)
- binding guanosine-5'-triphosphate: H209 (≠ R190), S213 (≠ E194), H258 (= H239), R261 (≠ K242), Y262 (≠ F243), R265 (≠ E246), K289 (≠ D270), E292 (≠ F273), K446 (≠ M419), H450 (≠ N423)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: D168 (= D150), M169 (≠ Y151), S170 (≠ G152), R211 (= R192), Q250 (= Q231), G251 (= G232), F252 (≠ L233), G253 (= G234), N254 (= N235), V255 (= V236), E275 (= E256), S276 (≠ F257), A326 (= A309), G347 (= G330), A348 (= A331), N349 (= N332), N374 (= N357)
- binding zinc ion: H209 (≠ R190), H450 (≠ N423)
P00366 Glutamate dehydrogenase 1, mitochondrial; GDH 1; EC 1.4.1.3 from Bos taurus (Bovine) (see 4 papers)
51% identity, 98% coverage: 7:471/473 of query aligns to 82:555/558 of P00366
- K84 (= K9) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- K90 (= K16) modified: N6-acetyllysine
- K110 (= K36) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- QHR 141:143 (≠ HHM 66:68) binding
- K147 (= K72) binding
- K162 (≠ M87) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- K171 (= K96) binding
- D176 (≠ N101) binding
- K183 (= K108) modified: N6-acetyllysine; alternate
- K191 (= K116) modified: N6-acetyllysine; alternate
- H252 (≠ L176) binding
- H266 (≠ R190) binding
- S270 (≠ E194) binding
- Y319 (≠ F243) binding
- R322 (≠ E246) binding
- K363 (≠ G287) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- K365 (= K289) modified: N6-acetyllysine; alternate
- K386 (≠ N312) modified: N6-acetyllysine
- K399 (= K325) modified: N6-acetyllysine
- K415 (≠ T341) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- S438 (= S364) binding
- N444 (≠ K370) binding
- S450 (≠ A376) binding
- K457 (≠ R383) modified: N6-acetyllysine; alternate; modified: N6-malonyllysine; alternate; modified: N6-succinyllysine; alternate
- K480 (= K402) modified: N6-acetyllysine; alternate
- K503 (≠ M419) modified: N6-acetyllysine; alternate; modified: N6-malonyllysine; alternate; modified: N6-succinyllysine; alternate
- R516 (≠ H432) binding
- K527 (≠ N443) modified: N6-acetyllysine; alternate; modified: N6-malonyllysine; alternate; modified: N6-succinyllysine; alternate
- K545 (= K461) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
Sites not aligning to the query:
- 1:57 modified: transit peptide, Mitochondrion
1hwyA Bovine glutamate dehydrogenase complexed with NAD and 2-oxoglutarate (see paper)
51% identity, 98% coverage: 7:471/473 of query aligns to 25:498/501 of 1hwyA
- active site: K126 (= K108), N168 (≠ D150)
- binding 2-oxoglutaric acid: K90 (= K72), M111 (= M93), K114 (= K96), A166 (= A148), R211 (= R192), V378 (= V361), S381 (= S364)
- binding nicotinamide-adenine-dinucleotide: R86 (≠ M68), T87 (≠ S69), C115 (= C97), A116 (= A98), D119 (≠ N101), V120 (= V102), P121 (= P103), N168 (≠ D150), M169 (≠ Y151), H195 (≠ L176), Q205 (≠ L186), G206 (≠ H187), T215 (= T196), G251 (= G232), F252 (≠ L233), G253 (= G234), N254 (= N235), V255 (= V236), E275 (= E256), S276 (≠ F257), A326 (= A309), A348 (= A331), N349 (= N332), N374 (= N357), K387 (= K370), H391 (= H374), V392 (= V375), S393 (≠ A376), K488 (= K461)
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction
41% identity, 79% coverage: 11:383/473 of query aligns to 4:367/416 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
41% identity, 79% coverage: 11:383/473 of query aligns to 6:369/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (= K72), G70 (= G74), M89 (= M93), K92 (= K96), K104 (= K108), A142 (= A148), D144 (= D150), G346 (= G360), S350 (= S364)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R76), K112 (= K116), P143 (= P149), D144 (= D150), V145 (≠ Y151), Y146 (≠ G152), T190 (= T196), Y219 (≠ L233), G220 (= G234), N221 (= N235), A222 (≠ V236), D243 (≠ E256), S244 (≠ F257), K263 (≠ R276), A295 (= A309), I296 (≠ L310), N318 (= N332)
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction
41% identity, 79% coverage: 11:383/473 of query aligns to 7:370/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K72), M90 (= M93), K105 (= K108), A143 (= A148), D145 (= D150), S351 (= S364)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R76), D145 (= D150), V146 (≠ Y151), Y147 (≠ G152), T191 (= T196), Y220 (≠ L233), G221 (= G234), N222 (= N235), A223 (≠ V236), D244 (≠ E256), S245 (≠ F257), K264 (≠ R276), N281 (= N293), A295 (= A308), A296 (= A309), I297 (≠ L310), N319 (= N332), N344 (= N357)
4xgiA Crystal structure of glutamate dehydrogenase from burkholderia thailandensis
43% identity, 77% coverage: 5:370/473 of query aligns to 8:361/416 of 4xgiA
- active site: K112 (= K108), D152 (= D150)
- binding 2-oxoglutaric acid: K76 (= K72), G78 (= G74), M97 (= M93), K100 (= K96), K112 (= K108), A150 (= A148), R192 (= R192), S355 (= S364)
- binding nicotinamide-adenine-dinucleotide: R80 (= R76), D152 (= D150), V153 (≠ Y151), T196 (= T196), G224 (= G232), G226 (= G234), N227 (= N235), V228 (= V236), D248 (≠ E256), H249 (≠ F257), A299 (= A308), A300 (= A309), A322 (= A331), N323 (= N332), N348 (= N357)
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)
40% identity, 73% coverage: 27:371/473 of query aligns to 34:365/424 of P39633
- E93 (= E85) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (≠ N114) 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 (≠ N138) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ G152) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (≠ Y238) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ G330) 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)
38% identity, 77% coverage: 6:371/473 of query aligns to 11:368/427 of P50735
- VKA 97:99 (≠ LAA 89:91) mutation Missing: In gudB1; gains glutamate dehydrogenase activity, restores growth on proline, arginine, ornithine.
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)
36% identity, 80% coverage: 32:410/473 of query aligns to 32:398/420 of P80053
- K254 (≠ N265) modified: N6-methyllysine
- K260 (≠ E271) modified: N6-methyllysine
- K372 (≠ R383) modified: N6-methyllysine
- K391 (= K402) modified: N6-methyllysine
- K392 (≠ T403) modified: N6-methyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylmethionine
3aogA Crystal structure of glutamate dehydrogenase (gdhb) from thermus thermophilus (glu bound form)
40% identity, 81% coverage: 15:398/473 of query aligns to 17:382/421 of 3aogA
Sites not aligning to the query:
Query Sequence
>CA265_RS03475 FitnessBrowser__Pedo557:CA265_RS03475
MANLADENKFFADVCKNFDSAAQFTNHPEGLLNQIKTCNSVYRFQFPIRRGNGFEVIDAW
RVEHSHHMSPTKGGIRYSEMVNEDEVMALAALMTYKCAIVNVPFGGAKGGIKINTKQYSV
AELETITRRYTTELIKKNFIGPGIDVPAPDYGSGEREMSWIADTYMTMNPGQLDALGCVT
GKPIALHGIRGRKEATGRGVAYAVRECVEVAEDMAKIGFKAGLGDKRVIVQGLGNVGYHS
AKFLAEFGATIVGLCEFEGAIYNPNGLNVDEVFAHRKNTGSILGFPGAKDFKNSMEGLEQ
DCDIIVPAALENQFTELNIRNIKAKIIAEGANGPTTPEAETIFTEMGGIIIPDMYCNAGG
VTVSYFEWLKNLSHVAFGRMENRYAANSNANLINTLENLTGKTILPEHRLMIVKGASEME
LVNSGLEDTMIHSYHEIRETLMNKPATQTLRTAAFVNSIDKIAVSYMNLGVWP
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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