SitesBLAST
Comparing AO356_26080 AO356_26080 lactate dehydrogenase 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: 1:342/343 of query aligns to 1:342/343 of Q4U331
- HFAAL 126:130 (= HFAAL 126:130) binding in other chain
- DLA 184:186 (= DLA 184:186) binding in other chain
- HK 236:237 (= HK 236:237) binding
- 309:315 (vs. 309:315, 100% identical) binding in other chain
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
76% identity, 97% coverage: 12:342/343 of query aligns to 6:336/337 of 2cwfB
- active site: H48 (= H54)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H54), H120 (= H126), A122 (= A128), A123 (= A129), L124 (= L130), T160 (= T166), P162 (= P168), F177 (= F183), D178 (= D184), L179 (= L185), A180 (= A186), H230 (= H236), K231 (= K237), R303 (= R309), G306 (= G312), R308 (= R314), R309 (= R315)
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
76% identity, 96% coverage: 12:341/343 of query aligns to 3:332/332 of 2cwhA
- active site: H45 (= H54)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H54), A119 (= A128), A120 (= A129), L121 (= L130), H148 (= H157), T157 (= T166), P159 (= P168), F174 (= F183), D175 (= D184), L176 (= L185), A177 (= A186), H227 (= H236), K228 (= K237), R300 (= R309), G303 (= G312), R305 (= R314), R306 (= R315)
- binding pyrrole-2-carboxylate: H45 (= H54), R49 (= R58), M142 (= M151), T157 (= T166), H183 (= H192), G184 (= G193)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
36% identity, 95% coverage: 16:340/343 of query aligns to 6:332/340 of 1vbiA
- active site: H44 (= H54)
- binding nicotinamide-adenine-dinucleotide: H44 (= H54), H115 (= H126), G117 (≠ A128), A119 (≠ L130), T155 (= T166), P157 (= P168), A171 (≠ F183), D172 (= D184), L173 (= L185), A174 (= A186), F301 (≠ R309), P303 (= P311), L306 (≠ R314), E307 (≠ R315)
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)
34% identity, 92% coverage: 15:330/343 of query aligns to 7:331/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
34% identity, 92% coverage: 15:330/343 of query aligns to 5:329/359 of 2g8yA
- active site: H46 (= H54)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ A51), H46 (= H54), G120 (≠ A128), I122 (≠ L130), T160 (= T166), P162 (= P168), L176 (≠ V182), L177 (≠ F183), D178 (= D184), Y179 (≠ L185), A180 (= A186), H232 (= H236), Y235 (≠ S239), N268 (≠ T274), G311 (= G312), E314 (≠ R315)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
29% identity, 94% coverage: 20:341/343 of query aligns to 10:332/344 of 2x06A
- active site: H44 (= H54)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ A51), H44 (= H54), H116 (= H126), F117 (= F127), G118 (≠ A128), I119 (≠ A129), A120 (≠ L130), T156 (= T166), P158 (= P168), D173 (= D184), M174 (≠ L185), A175 (= A186), L301 (= L310), I306 (≠ R314), E307 (≠ R315)
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
34% identity, 95% coverage: 15:341/343 of query aligns to 6:339/350 of 1z2iA
- active site: H45 (= H54)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ A51), H45 (= H54), H117 (= H126), F118 (= F127), G119 (≠ A128), P120 (≠ A129), A121 (≠ L130), T157 (= T166), P159 (= P168), D175 (= D184), M176 (≠ L185), A177 (= A186), P182 (≠ A191), F227 (vs. gap), K228 (= K237), M307 (vs. gap), R312 (= R314), E313 (≠ R315)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
31% identity, 92% coverage: 13:329/343 of query aligns to 3:323/349 of P77555
- S43 (= S53) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H54) 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 (= R58) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y62) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H126) mutation to A: Loss of dehydrogenase activity.
- S140 (= S150) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ M151) 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 (≠ E260) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ A269) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
30% identity, 95% coverage: 13:337/343 of query aligns to 3:331/338 of 4fjuA
- binding glyoxylic acid: R48 (= R58), H116 (= H126), S140 (= S150), D141 (≠ M151)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ A51), H44 (= H54), H116 (= H126), G118 (≠ A128), I120 (≠ L130), S140 (= S150), F147 (≠ H157), T156 (= T166), P158 (= P168), F173 (= F183), D174 (= D184), M175 (≠ L185), A176 (= A186), P223 (≠ H236), K224 (= K237), Y303 (vs. gap), G306 (= G312), D308 (≠ R314), Q309 (≠ R315)
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
26% identity, 96% coverage: 12:341/343 of query aligns to 4:352/361 of 3i0pA
- active site: H46 (= H54)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ A51), H46 (= H54), H119 (= H126), I122 (≠ A129), A123 (≠ L130), T159 (= T166), P161 (= P168), F176 (= F183), D177 (= D184), G178 (≠ L185), A179 (= A186), P184 (≠ A191), R187 (≠ D194), Y320 (vs. gap), A322 (vs. gap), G323 (= G312), K325 (≠ R314), E326 (≠ R315)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
28% identity, 95% coverage: 16:341/343 of query aligns to 17:340/348 of 1v9nA
- active site: H55 (= H54)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H54), H127 (= H126), G129 (≠ A128), I130 (≠ A129), A131 (≠ L130), T167 (= T166), P169 (= P168), L183 (≠ F183), D184 (= D184), M185 (≠ L185), A186 (= A186), P191 (≠ A191), W308 (vs. gap), H310 (= H316), G311 (≠ R317), K313 (≠ R319), G314 (≠ S320)
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, 96% coverage: 13:340/343 of query aligns to 3:332/335 of 1s20G
- active site: H44 (= H54)
- binding nicotinamide-adenine-dinucleotide: H44 (= H54), H116 (= H126), W147 (≠ H157), T156 (= T166), P158 (= P168), D172 (= D184), M173 (≠ L185), S174 (≠ A186), W224 (≠ H236), K225 (= K237), R301 (= R309), G304 (= G312), E306 (≠ R314)
Query Sequence
>AO356_26080 AO356_26080 lactate dehydrogenase
MSAPSDHAASCTLSFDALVSLLEKIFLRHGTSTEVARCLAENCAGAERDGAHSHGVFRLP
GYVSTLNSGWVNGKAVPVVEDVASGFVAVDAGNGFAQPALAAARPLLVEKARSAGIAVLA
IRNSHHFAALWPDVEPFAYEGLVALSVVNSMTCVVPHGADRPLFGTNPIAFAAPRADGEP
IVFDLATSAIAHGDVQIAARKGELLPPGMGVDSLGQPTRDPKAILEGGALLPFGGHKGSA
LSMMVELLAAALTGGNFSFEFDWSNHPGAKTPWTGQLLIVIDPSKTAGQDFAERSRELVR
QMHGVGLRRLPGDRRHRERSKANEQGISLDEQTLAQLRELAGI
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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