SitesBLAST
Comparing PfGW456L13_2974 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2974 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)
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)
75% identity, 100% coverage: 1:345/346 of query aligns to 1:342/343 of Q4U331
- HFAAL 126:130 (= HFAAL 129:133) binding in other chain
- DLA 184:186 (= DLA 187:189) binding in other chain
- HK 236:237 (= HK 239:240) binding
- 309:315 (vs. 312:318, 100% identical) binding in other chain
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
77% identity, 95% coverage: 16:345/346 of query aligns to 7:336/337 of 2cwfB
- active site: H48 (= H57)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H57), H120 (= H129), A122 (= A131), A123 (= A132), L124 (= L133), T160 (= T169), P162 (= P171), F177 (= F186), D178 (= D187), L179 (= L188), A180 (= A189), H230 (= H239), K231 (= K240), R303 (= R312), G306 (= G315), R308 (= R317), R309 (= R318)
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
77% identity, 95% coverage: 16:344/346 of query aligns to 4:332/332 of 2cwhA
- active site: H45 (= H57)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H57), A119 (= A131), A120 (= A132), L121 (= L133), H148 (= H160), T157 (= T169), P159 (= P171), F174 (= F186), D175 (= D187), L176 (= L188), A177 (= A189), H227 (= H239), K228 (= K240), R300 (= R312), G303 (= G315), R305 (= R317), R306 (= R318)
- binding pyrrole-2-carboxylate: H45 (= H57), R49 (= R61), M142 (= M154), T157 (= T169), H183 (= H195), G184 (= G196)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
35% identity, 93% coverage: 21:343/346 of query aligns to 8:332/340 of 1vbiA
- active site: H44 (= H57)
- binding nicotinamide-adenine-dinucleotide: H44 (= H57), H115 (= H129), G117 (≠ A131), A119 (≠ L133), T155 (= T169), P157 (= P171), A171 (≠ F186), D172 (= D187), L173 (= L188), A174 (= A189), F301 (≠ R312), P303 (= P314), L306 (≠ R317), E307 (≠ R318)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
29% identity, 95% coverage: 16:344/346 of query aligns to 3:332/344 of 2x06A
- active site: H44 (= H57)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ A54), H44 (= H57), H116 (= H129), F117 (= F130), G118 (≠ A131), I119 (≠ A132), A120 (≠ L133), T156 (= T169), P158 (= P171), D173 (= D187), M174 (≠ L188), A175 (= A189), L301 (= L313), I306 (≠ R317), E307 (≠ R318)
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)
33% identity, 91% coverage: 19:334/346 of query aligns to 10:332/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
32% identity, 91% coverage: 19:334/346 of query aligns to 8:330/359 of 2g8yA
- active site: H46 (= H57)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ A54), H46 (= H57), G120 (≠ A131), I122 (≠ L133), T160 (= T169), P162 (= P171), L176 (≠ V185), L177 (≠ F186), D178 (= D187), Y179 (≠ L188), A180 (= A189), H232 (= H239), Y235 (≠ S242), N268 (≠ T277), G311 (= G315), E314 (≠ R318)
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
31% identity, 92% coverage: 16:332/346 of query aligns to 3:323/338 of 4fjuA
- binding glyoxylic acid: R48 (= R61), H116 (= H129), S140 (= S153), D141 (≠ M154)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ A54), H44 (= H57), H116 (= H129), G118 (≠ A131), I120 (≠ L133), S140 (= S153), F147 (≠ H160), T156 (= T169), P158 (= P171), F173 (= F186), D174 (= D187), M175 (≠ L188), A176 (= A189), P223 (≠ H239), K224 (= K240), Y303 (vs. gap), G306 (= G315), D308 (≠ R317), Q309 (≠ R318)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
31% identity, 92% coverage: 16:332/346 of query aligns to 3:323/349 of P77555
- S43 (= S56) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H57) 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 (= R61) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y65) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H129) mutation to A: Loss of dehydrogenase activity.
- S140 (= S153) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ M154) 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 (≠ K267) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ P275) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
32% identity, 95% coverage: 18:344/346 of query aligns to 6:339/350 of 1z2iA
- active site: H45 (= H57)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ A54), H45 (= H57), H117 (= H129), F118 (= F130), G119 (≠ A131), P120 (≠ A132), A121 (≠ L133), T157 (= T169), P159 (= P171), D175 (= D187), M176 (≠ L188), A177 (= A189), P182 (≠ A194), F227 (vs. gap), K228 (= K240), M307 (vs. gap), R312 (= R317), E313 (≠ R318)
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
25% identity, 96% coverage: 14:346/346 of query aligns to 3:354/361 of 3i0pA
- active site: H46 (= H57)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ A54), H46 (= H57), H119 (= H129), I122 (≠ A132), A123 (≠ L133), T159 (= T169), P161 (= P171), F176 (= F186), D177 (= D187), G178 (≠ L188), A179 (= A189), P184 (≠ A194), R187 (≠ D197), Y320 (vs. gap), A322 (vs. gap), G323 (= G315), K325 (≠ R317), E326 (≠ R318)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
28% identity, 87% coverage: 6:305/346 of query aligns to 8:295/348 of 1v9nA
- active site: H55 (= H57)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H57), H127 (= H129), G129 (≠ A131), I130 (≠ A132), A131 (≠ L133), T167 (= T169), P169 (= P171), L183 (≠ F186), D184 (= D187), M185 (≠ L188), A186 (= A189), P191 (≠ A194)
Sites not aligning to the query:
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)
26% identity, 95% coverage: 15:343/346 of query aligns to 2:332/335 of 1s20G
- active site: H44 (= H57)
- binding nicotinamide-adenine-dinucleotide: H44 (= H57), H116 (= H129), W147 (≠ H160), T156 (= T169), P158 (= P171), D172 (= D187), M173 (≠ L188), S174 (≠ A189), W224 (≠ H239), K225 (= K240), R301 (= R312), G304 (= G315), E306 (≠ R317)
Query Sequence
>PfGW456L13_2974 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2974
MSAPHDHASTAVPSHLSLEALSALLEKIFLRHGTSVEVARVLAQNCACAERDGAHSHGVF
RIPGYVSTLQSGWVNGQAVPLVEDVASGFVRVDANNGFAQPALAAARELLVQKARSAGIA
VLAIRNSHHFAALWPDVEPFAEEGLVALSVVNSMTCVVPHGADRPLFGTNPIAFAAPRAE
GGPIVFDLATSAIAHGDVQIAAREGERLPEGMGVDSLGQPTTDPKAILEGGALLPFGGHK
GSALSMMVELLAAALTGGNFSFEFDWKNHPGAKTPWTGQLLIVIDPDKAAGQSFAERSQE
LVRQMHGVGLKRLPGDRRHHQRARSLANGIELDARTLANLRELAGL
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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