SitesBLAST
Comparing PP_3591 FitnessBrowser__Putida:PP_3591 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
72% identity, 99% coverage: 3:332/332 of query aligns to 7:336/337 of 2cwfB
- active site: H48 (= H44)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H44), H120 (= H116), A122 (= A118), A123 (= A119), L124 (= L120), T160 (= T156), P162 (= P158), F177 (= F173), D178 (= D174), L179 (≠ M175), A180 (= A176), H230 (= H226), K231 (= K227), R303 (= R299), G306 (= G302), R308 (= R304), R309 (= R305)
Q4U331 Delta(1)-pyrroline-2-carboxylate/Delta(1)-piperideine-2-carboxylate reductase; Pyr2C/Pip2C reductase; N-methyl-L-amino acid dehydrogenase; EC 1.5.1.21; EC 1.4.1.17 from Pseudomonas syringae pv. tomato (see paper)
72% identity, 99% coverage: 3:332/332 of query aligns to 13:342/343 of Q4U331
- HFAAL 126:130 (= HFAAL 116:120) binding in other chain
- DLA 184:186 (≠ DMA 174:176) binding in other chain
- HK 236:237 (= HK 226:227) binding
- 309:315 (vs. 299:305, 71% identical) binding in other chain
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
72% identity, 99% coverage: 3:330/332 of query aligns to 4:331/332 of 2cwhA
- active site: H45 (= H44)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H44), A119 (= A118), A120 (= A119), L121 (= L120), H148 (= H147), T157 (= T156), P159 (= P158), F174 (= F173), D175 (= D174), L176 (≠ M175), A177 (= A176), H227 (= H226), K228 (= K227), R300 (= R299), G303 (= G302), R305 (= R304), R306 (= R305)
- binding pyrrole-2-carboxylate: H45 (= H44), R49 (= R48), M142 (= M141), T157 (= T156), H183 (= H182), G184 (= G183)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
29% identity, 97% coverage: 9:330/332 of query aligns to 9:331/344 of 2x06A
- active site: H44 (= H44)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ A41), H44 (= H44), H116 (= H116), F117 (= F117), G118 (≠ A118), I119 (≠ A119), A120 (≠ L120), T156 (= T156), P158 (= P158), D173 (= D174), M174 (= M175), A175 (= A176), L301 (≠ R299), I306 (≠ R304), E307 (≠ R305)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
34% identity, 100% coverage: 1:332/332 of query aligns to 1:337/340 of 1vbiA
- active site: H44 (= H44)
- binding nicotinamide-adenine-dinucleotide: H44 (= H44), H115 (= H116), G117 (≠ A118), A119 (≠ L120), T155 (= T156), P157 (= P158), A171 (≠ F173), D172 (= D174), L173 (≠ M175), A174 (= A176), F301 (≠ R299), P303 (= P301), L306 (≠ R304), E307 (≠ R305)
P30178 Hydroxycarboxylate dehydrogenase B; 2-oxoglutarate reductase; Hydroxyphenylpyruvate reductase; Phenylpyruvate reductase; EC 1.1.1.-; EC 1.1.1.237 from Escherichia coli (strain K12)
30% identity, 95% coverage: 2:317/332 of query aligns to 6:328/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
31% identity, 93% coverage: 8:317/332 of query aligns to 10:326/359 of 2g8yA
- active site: H46 (= H44)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ A41), H46 (= H44), G120 (≠ A118), I122 (≠ L120), T160 (= T156), P162 (= P158), L176 (≠ V172), L177 (≠ F173), D178 (= D174), Y179 (≠ M175), A180 (= A176), H232 (= H226), Y235 (≠ S229), N268 (≠ T264), G311 (= G302), E314 (≠ R305)
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
35% identity, 80% coverage: 7:273/332 of query aligns to 8:275/350 of 1z2iA
- active site: H45 (= H44)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ A41), H45 (= H44), H117 (= H116), F118 (= F117), G119 (≠ A118), P120 (≠ A119), A121 (≠ L120), T157 (= T156), P159 (= P158), D175 (= D174), M176 (= M175), A177 (= A176), P182 (≠ A181), F227 (vs. gap), K228 (= K227)
Sites not aligning to the query:
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
28% identity, 99% coverage: 1:330/332 of query aligns to 12:339/348 of 1v9nA
- active site: H55 (= H44)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H44), H127 (= H116), G129 (≠ A118), I130 (≠ A119), A131 (≠ L120), T167 (= T156), P169 (= P158), L183 (≠ F173), D184 (= D174), M185 (= M175), A186 (= A176), P191 (≠ A181), W308 (vs. gap), H310 (≠ P301), G311 (= G302), K313 (≠ R304), G314 (≠ R305)
Sites not aligning to the query:
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
30% identity, 97% coverage: 1:321/332 of query aligns to 1:325/338 of 4fjuA
- binding glyoxylic acid: R48 (= R48), H116 (= H116), S140 (= S140), D141 (≠ M141)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ A41), H44 (= H44), H116 (= H116), G118 (≠ A118), I120 (≠ L120), S140 (= S140), F147 (≠ H147), T156 (= T156), P158 (= P158), F173 (= F173), D174 (= D174), M175 (= M175), A176 (= A176), P223 (≠ H226), K224 (= K227), Y303 (vs. gap), G306 (= G302), D308 (≠ R304), Q309 (≠ R305)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
30% identity, 97% coverage: 1:321/332 of query aligns to 1:325/349 of P77555
- S43 (= S43) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H44) mutation to A: 16-fold decrease of the affinity for (S)-ureidoglycolate, but same affinity for NAD compared to the wild-type. Strong decrease of the catalytic efficiency.
- R48 (= R48) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y52) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H116) mutation to A: Loss of dehydrogenase activity.
- S140 (= S140) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ M141) mutation to A: 5-fold decrease of the affinity for (S)-ureidoglycolate, but same affinity for NAD compared to the wild-type. Strong decrease of the catalytic efficiency.; mutation to E: 14-fold decrease of the affinity for (S)-ureidoglycolate, but same affinity for NAD compared to the wild-type. Strong decrease of the catalytic efficiency.; mutation to N: 6-fold decrease of the affinity for (S)-ureidoglycolate, but same affinity for NAD compared to the wild-type. Strong decrease of the catalytic efficiency.
- M251 (≠ E250) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ A259) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
1s20G A novel NAD binding protein revealed by the crystal structure of e. Coli 2,3-diketogulonate reductase (yiak) northeast structural genomics consortium target er82 (see paper)
28% identity, 74% coverage: 1:245/332 of query aligns to 1:243/335 of 1s20G
Sites not aligning to the query:
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
26% identity, 74% coverage: 2:247/332 of query aligns to 4:262/361 of 3i0pA
- active site: H46 (= H44)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ A41), H46 (= H44), H119 (= H116), I122 (≠ A119), A123 (≠ L120), T159 (= T156), P161 (= P158), F176 (= F173), D177 (= D174), G178 (≠ M175), A179 (= A176), P184 (≠ A181), R187 (≠ D184)
Sites not aligning to the query:
Query Sequence
>PP_3591 FitnessBrowser__Putida:PP_3591
MRVPFTELQSLLQAIFQRHGCSEAVARVLAHNCASAQRDGAHSHGVFRMPGYVSTLASGW
VDGQATPQVSDVAAGYVRVDAAGGFAQPALAAARELLVAKARSAGIAVLAIHNSHHFAAL
WPDVEPFAEEGLVALSVVNSMTCVVPHGARKPLFGTNPIAFAAPCAEHDPIVFDMATSAM
AHGDVQIAARAGQQLPEGMGVDADGQPTTDPKAILEGGALLPFGGHKGSALSMMVELLAA
ALTGGHFSWEFDWSGHPGAKTPWTGQLIIVIDPGKAEGQRFAQRSRELVEHMQAVGLTRM
PGERRYREREVAEEEGVAVTEQELKGLKELLG
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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