SitesBLAST
Comparing PP_0675 FitnessBrowser__Putida:PP_0675 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)
P00370 NADP-specific glutamate dehydrogenase; NADP-GDH; EC 1.4.1.4 from Escherichia coli (strain K12) (see 2 papers)
66% identity, 99% coverage: 7:449/449 of query aligns to 6:447/447 of P00370
- K92 (= K93) mutation to S: Complete loss of dehydrogenase activity.
- K128 (= K129) mutation to H: Reduces catalytic activity and increases pH optima for activity. Increases relative activity with amino acid substrates other than glutamate, especially L-norvaline.; mutation to R: Reduced catalytic activity and increases pH optima for activity. NADP-specific glutamate dehydrogenase.
5gudA Glutamate dehydrogenase from corynebacterium glutamicum (alpha- iminoglutarate/NADP+ complex) (see paper)
59% identity, 100% coverage: 3:449/449 of query aligns to 2:447/447 of 5gudA
- active site: K128 (= K129), D168 (= D169)
- binding (2Z)-2-iminopentanedioic acid: K92 (= K93), G93 (= G94), G94 (= G95), Q113 (= Q114), K116 (= K117), K128 (= K129), A166 (= A167), R208 (= R208), V376 (= V378), S379 (= S381)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K136 (= K137), D168 (= D169), I169 (= I170), R208 (= R208), T212 (= T212), S241 (= S241), G242 (= G242), N243 (= N243), V244 (= V244), D264 (= D264), S265 (= S265), R290 (= R293), A321 (= A323), T322 (= T324), G345 (= G347), A346 (= A348), N347 (= N349), N372 (= N374)
5ijzA Crystal structure of glutamate dehydrogenase(gdh) from corynebacterium glutamicum (see paper)
59% identity, 100% coverage: 3:449/449 of query aligns to 2:447/447 of 5ijzA
- active site: K128 (= K129), D168 (= D169)
- binding 2-oxoglutaric acid: K92 (= K93), G93 (= G94), G94 (= G95), Q113 (= Q114), K116 (= K117), K128 (= K129), A166 (= A167), R208 (= R208), V376 (= V378), S379 (= S381)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K136 (= K137), D168 (= D169), I169 (= I170), T212 (= T212), S241 (= S241), G242 (= G242), N243 (= N243), V244 (= V244), D264 (= D264), S265 (= S265), R290 (= R293), A321 (= A323), T322 (= T324), A346 (= A348), N347 (= N349), N372 (= N374)
5gudE Glutamate dehydrogenase from corynebacterium glutamicum (alpha- iminoglutarate/NADP+ complex) (see paper)
59% identity, 100% coverage: 3:449/449 of query aligns to 15:460/460 of 5gudE
- active site: K141 (= K129), D181 (= D169)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: T225 (= T212), S254 (= S241), G255 (= G242), N256 (= N243), V257 (= V244), D277 (= D264), S278 (= S265), R303 (= R293), A334 (= A323), T335 (= T324), A359 (= A348), N360 (= N349)
P24295 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Clostridium symbiosum (Bacteroides symbiosus) (see 4 papers)
54% identity, 99% coverage: 4:448/449 of query aligns to 1:448/450 of P24295
- M1 (= M4) modified: Initiator methionine, Removed
- K90 (= K93) binding ; mutation to L: Increased substrate activity for methionine and norleucine but negligible activity with either glutamate or leucine. Dramatic reduction in the dehydrogenase activity with glutamate as the substrate; when associated with V-381.
- Q111 (= Q114) binding
- K114 (= K117) binding
- K126 (= K129) active site, Proton donor
- G165 (= G168) binding
- D166 (= D169) mutation to S: Dramatic reduction in the dehydrogenase activity. Specific activity is decreased 1000-fold in the reductive amination reaction and 100000-fold for oxidative deamination.
- S381 (= S381) binding ; mutation to V: Dramatic reduction in the dehydrogenase activity with glutamate as the substrate; when associated with L-90.
1bgvA Glutamate dehydrogenase (see paper)
54% identity, 98% coverage: 8:448/449 of query aligns to 4:447/449 of 1bgvA
P00369 NADP-specific glutamate dehydrogenase; NADP-GDH; NADP-dependent glutamate dehydrogenase; EC 1.4.1.4 from Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) (see paper)
56% identity, 95% coverage: 20:447/449 of query aligns to 5:448/454 of P00369
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
7ecsA Crystal structure of aspergillus terreus glutamate dehydrogenase (atgdh) complexed with malonate and NADPH (see paper)
56% identity, 95% coverage: 20:447/449 of query aligns to 5:457/460 of 7ecsA
- binding malonate ion: G79 (= G94), G80 (= G95), Q99 (= Q114), K102 (= K117), K114 (= K129), S326 (≠ G329), G327 (≠ A330), E328 (= E331), T350 (= T353), A352 (≠ E355)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K122 (= K137), D154 (= D169), I155 (= I170), R193 (= R208), T197 (= T212), S229 (= S241), G230 (= G242), N231 (= N243), V232 (= V244), D252 (= D264), S253 (= S265), K279 (= K287), A320 (= A323), T321 (= T324), G344 (= G347), S345 (≠ A348), N346 (= N349), N379 (= N374)
7ecrA Crystal structure of aspergillus terreus glutamate dehydrogenase (atgdh) complexed with succinate and adp-ribose (see paper)
56% identity, 95% coverage: 20:447/449 of query aligns to 5:457/460 of 7ecrA
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4r,5r)-3,4,5-trihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: K122 (= K137), D154 (= D169), I155 (= I170), S229 (= S241), G230 (= G242), N231 (= N243), V232 (= V244), D252 (= D264), S253 (= S265), K279 (= K287), A320 (= A323), T321 (= T324), G344 (= G347), S345 (≠ A348), N346 (= N349), N379 (= N374)
7f79C Crystal structure of glutamate dehydrogenase 3 from candida albicans in complex with alpha-ketoglutarate and NADPH (see paper)
51% identity, 96% coverage: 20:449/449 of query aligns to 6:457/458 of 7f79C
- binding 2-oxoglutaric acid: K79 (= K93), G80 (= G94), G81 (= G95), Q100 (= Q114), K103 (= K117), K115 (= K129), V380 (= V378), S383 (= S381)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R83 (= R97), H85 (= H99), K123 (= K137), D155 (= D169), I156 (= I170), R194 (= R208), T198 (= T212), S230 (= S241), G231 (= G242), N232 (= N243), V233 (= V244), D253 (= D264), S254 (= S265), K276 (vs. gap), A321 (= A323), T322 (= T324), G345 (= G347), S346 (≠ A348), N347 (= N349), N376 (= N374)
5xwcA Crystal structure of aspergillus niger glutamate dehydrogenase complexed with alpha-iminoglutarate, 2-amino-2-hydroxyglutarate and NADP (see paper)
54% identity, 95% coverage: 20:447/449 of query aligns to 4:456/459 of 5xwcA
- binding (2Z)-2-iminopentanedioic acid: K77 (= K93), G78 (= G94), Q98 (= Q114), K101 (= K117), K113 (= K129), A151 (= A167), R192 (= R208), V382 (= V378), S385 (= S381)
- binding (2S)-2-azanyl-2-oxidanyl-pentanedioic acid: K77 (= K93), G78 (= G94), G79 (= G95), Q98 (= Q114), K101 (= K117), K113 (= K129), A151 (= A167), D153 (= D169), R192 (= R208), V382 (= V378), S385 (= S381)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H83 (= H99), K121 (= K137), D153 (= D169), I154 (= I170), R192 (= R208), T196 (= T212), S228 (= S241), G229 (= G242), N230 (= N243), V231 (= V244), D251 (= D264), S252 (= S265), A319 (= A323), T320 (= T324), G343 (= G347), S344 (≠ A348), N345 (= N349), N378 (= N374)
5xw0A Crystal structure of aspergillus niger glutamate dehydrogenase complexed with isophthalate and NADPH (see paper)
54% identity, 95% coverage: 20:447/449 of query aligns to 4:456/459 of 5xw0A
- binding benzene-1,3-dicarboxylic acid: K77 (= K93), G78 (= G94), Q98 (= Q114), K101 (= K117), K113 (= K129), A151 (= A167), G152 (= G168), D153 (= D169), R192 (= R208), S385 (= S381)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H83 (= H99), K121 (= K137), D153 (= D169), I154 (= I170), R192 (= R208), T196 (= T212), S228 (= S241), G229 (= G242), N230 (= N243), V231 (= V244), D251 (= D264), S252 (= S265), A319 (= A323), T320 (= T324), G343 (= G347), S344 (≠ A348), N345 (= N349), N378 (= N374)
5xvxA Crystal structure of aspergillus niger glutamate dehydrogenase complexed with alpha-ketoglutarate and NADPH (see paper)
54% identity, 95% coverage: 20:447/449 of query aligns to 4:456/459 of 5xvxA
- binding 2-oxoglutaric acid: K77 (= K93), Q98 (= Q114), K101 (= K117), K113 (= K129), A151 (= A167), R192 (= R208), V382 (= V378), S385 (= S381)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K121 (= K137), D153 (= D169), I154 (= I170), R192 (= R208), T196 (= T212), S228 (= S241), G229 (= G242), N230 (= N243), V231 (= V244), D251 (= D264), S252 (= S265), A319 (= A323), T320 (= T324), G343 (= G347), S344 (≠ A348), N345 (= N349), N378 (= N374)
5xvvB Crystal structure of forward inhibited aspergillus niger glutamate dehydrogenase with both apo- and alpha ketoglutarate bound subunits (see paper)
54% identity, 95% coverage: 20:447/449 of query aligns to 4:456/459 of 5xvvB
P78804 NADP-specific glutamate dehydrogenase; NADP-GDH; NADP-dependent glutamate dehydrogenase; EC 1.4.1.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
53% identity, 95% coverage: 20:447/449 of query aligns to 4:448/451 of P78804
- S252 (= S265) modified: Phosphoserine
3aoeB Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
34% identity, 89% coverage: 51:448/449 of query aligns to 36:422/424 of 3aoeB
Sites not aligning to the query:
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)
33% identity, 89% coverage: 51:449/449 of query aligns to 38:424/424 of P39633
- E93 (≠ V106) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (= D135) 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 (≠ R157) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ G171) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (≠ Q246) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ G347) 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.
3aogA Crystal structure of glutamate dehydrogenase (gdhb) from thermus thermophilus (glu bound form)
34% identity, 89% coverage: 51:448/449 of query aligns to 33:419/421 of 3aogA
- active site: K111 (= K129), D151 (= D169)
- binding glutamic acid: A70 (= A88), G77 (= G95), M96 (≠ Q114), K111 (= K129), P150 (≠ G168), D151 (= D169), D164 (≠ G182), M168 (vs. gap), S354 (= S381), R417 (≠ Q446), G418 (= G447), L419 (≠ V448)
Sites not aligning to the query:
4xgiA Crystal structure of glutamate dehydrogenase from burkholderia thailandensis
35% identity, 80% coverage: 52:408/449 of query aligns to 35:376/416 of 4xgiA
- active site: K112 (= K129), D152 (= D169)
- binding 2-oxoglutaric acid: K76 (= K93), G78 (= G95), M97 (≠ Q114), K100 (= K117), K112 (= K129), A150 (= A167), R192 (= R208), S355 (= S381)
- binding nicotinamide-adenine-dinucleotide: R80 (= R97), D152 (= D169), V153 (≠ I170), T196 (= T212), G224 (= G240), G226 (= G242), N227 (= N243), V228 (= V244), D248 (= D264), H249 (≠ S265), A299 (≠ C322), A300 (= A323), A322 (= A348), N323 (= N349), N348 (= N374)
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction
34% identity, 89% coverage: 52:449/449 of query aligns to 25:414/416 of 8xcoA
Query Sequence
>PP_0675 FitnessBrowser__Putida:PP_0675
MSTMIESVDNFLARLKQRDPGQPEFHQAVEEVLRTLWPFLEANPHYLQSGILERMVEPER
AVLFRVSWVDDQGKVQVNRGYRIQMSSAIGPYKGGLRFHPSVNLSVLKFLAFEQVFKNSL
TSLPMGGGKGGSDFDPKGKSDAEVMRFCQAFMSELYRHIGADCDVPAGDIGVGAREIGFM
FGQYKRLANQFTSVLTGKGMTYGGSLIRPEATGYGCVYFAEEMLKRQDKRIDGRRVAVSG
SGNVAQYAARKVMDLGGKVISLSDSEGTLYAEAGLTDAQWDALMELKNVKRGRISELAGQ
FGLEFRKGQTPWSLPCDIALPCATQNELGAEDARTLLRNGCICVAEGANMPTTLEAVDIF
LDAGILYAPGKASNAGGVAVSGLEMSQNAMRLLWTAGEVDSKLHNIMQSIHHACVHYGEE
ADGRINYVKGANIAGFVKVADAMLAQGVV
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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