SitesBLAST
Comparing SMa0265 FitnessBrowser__Smeli:SMa0265 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)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
36% identity, 99% coverage: 1:331/334 of query aligns to 1:331/344 of 2x06A
- active site: H44 (= H44)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ L41), H44 (= H44), H116 (= H116), F117 (≠ M117), G118 (= G118), I119 (≠ M119), A120 (≠ L120), T156 (= T156), P158 (= P158), D173 (= D173), M174 (≠ L174), A175 (= A175), L301 (≠ A300), I306 (≠ A306), E307 (≠ R307)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
36% identity, 99% coverage: 1:331/334 of query aligns to 1:332/340 of 1vbiA
- active site: H44 (= H44)
- binding nicotinamide-adenine-dinucleotide: H44 (= H44), H115 (= H116), G117 (= G118), A119 (≠ L120), T155 (= T156), P157 (= P158), A171 (≠ L172), D172 (= D173), L173 (= L174), A174 (= A175), F301 (≠ A300), P303 (= P302), L306 (≠ G305), E307 (≠ A306)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
31% identity, 99% coverage: 1:331/334 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 (= G118), I130 (≠ M119), A131 (≠ L120), T167 (= T156), P169 (= P158), L183 (= L172), D184 (= D173), M185 (≠ L174), A186 (= A175), P191 (≠ S180), W308 (≠ A300), H310 (≠ P302), G311 (= G303), K313 (≠ G305), G314 (≠ A306)
Sites not aligning to the query:
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
31% identity, 99% coverage: 1:330/334 of query aligns to 1:333/338 of 4fjuA
- binding glyoxylic acid: R48 (= R48), H116 (= H116), S140 (= S140), D141 (≠ E141)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ L41), H44 (= H44), H116 (= H116), G118 (= G118), I120 (≠ L120), S140 (= S140), F147 (= F147), T156 (= T156), P158 (= P158), F173 (≠ L172), D174 (= D173), M175 (≠ L174), A176 (= A175), P223 (≠ A224), K224 (= K225), Y303 (≠ A300), G306 (= G303), D308 (≠ G305), Q309 (≠ A306)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
31% identity, 99% coverage: 1:330/334 of query aligns to 1:333/349 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 (≠ L52) 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 (≠ E141) 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 (≠ T252) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (vs. gap) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
34% identity, 94% coverage: 19:331/334 of query aligns to 23:334/337 of 2cwfB
- active site: H48 (= H44)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H44), H120 (= H116), A122 (≠ G118), A123 (≠ M119), L124 (= L120), T160 (= T156), P162 (= P158), F177 (≠ L172), D178 (= D173), L179 (= L174), A180 (= A175), H230 (≠ A224), K231 (= K225), R303 (≠ A300), G306 (= G303), R308 (≠ G305), R309 (≠ A306)
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
34% identity, 94% coverage: 19:331/334 of query aligns to 20:331/332 of 2cwhA
- active site: H45 (= H44)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H44), A119 (≠ G118), A120 (≠ M119), L121 (= L120), H148 (≠ F147), T157 (= T156), P159 (= P158), F174 (≠ L172), D175 (= D173), L176 (= L174), A177 (= A175), H227 (≠ A224), K228 (= K225), R300 (≠ A300), G303 (= G303), R305 (≠ G305), R306 (≠ A306)
- binding pyrrole-2-carboxylate: H45 (= H44), R49 (= R48), M142 (≠ E141), T157 (= T156), H183 (≠ M181), G184 (= G182)
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)
34% identity, 94% coverage: 19:331/334 of query aligns to 29:340/343 of Q4U331
- HFAAL 126:130 (≠ HMGML 116:120) binding in other chain
- DLA 184:186 (= DLA 173:175) binding in other chain
- HK 236:237 (≠ AK 224:225) binding
- 309:315 (vs. 300:306, 43% identical) binding in other chain
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
27% identity, 78% coverage: 8:269/334 of query aligns to 10:286/361 of 3i0pA
- active site: H46 (= H44)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ L41), H46 (= H44), H119 (= H116), I122 (≠ M119), A123 (≠ L120), T159 (= T156), P161 (= P158), F176 (≠ L172), D177 (= D173), G178 (≠ L174), A179 (= A175), P184 (≠ S180), R187 (≠ K183)
Sites not aligning to the query:
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)
28% identity, 96% coverage: 2:320/334 of query aligns to 6:330/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
28% identity, 96% coverage: 2:320/334 of query aligns to 4:328/359 of 2g8yA
- active site: H46 (= H44)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ L41), H46 (= H44), G120 (= G118), I122 (≠ L120), T160 (= T156), P162 (= P158), L176 (≠ V171), L177 (= L172), D178 (= D173), Y179 (≠ L174), A180 (= A175), H232 (≠ A224), Y235 (= Y227), N268 (≠ D254), G311 (= G303), E314 (≠ A306)
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)
24% identity, 99% coverage: 1:331/334 of query aligns to 1:332/335 of 1s20G
- active site: H44 (= H44)
- binding nicotinamide-adenine-dinucleotide: H44 (= H44), H116 (= H116), W147 (≠ F147), T156 (= T156), P158 (= P158), D172 (= D173), M173 (≠ L174), S174 (≠ A175), W224 (≠ A224), K225 (= K225), R301 (≠ A300), G304 (= G303), E306 (≠ G305)
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
29% identity, 89% coverage: 7:304/334 of query aligns to 8:311/350 of 1z2iA
- active site: H45 (= H44)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ L41), H45 (= H44), H117 (= H116), F118 (≠ M117), G119 (= G118), P120 (≠ M119), A121 (≠ L120), T157 (= T156), P159 (= P158), D175 (= D173), M176 (≠ L174), A177 (= A175), P182 (≠ S180), F227 (vs. gap), K228 (= K225), M307 (≠ A300)
Sites not aligning to the query:
Query Sequence
>SMa0265 FitnessBrowser__Smeli:SMa0265
MRLPPARLRNLSVALLEKRGVPADSARLQANLLLEAELRGLPSHGLQRLPLLLSRLDKGL
ANPTTRGNGTWRRASFLSVDGERGLGPVVMMDAMRVTRRILKETGLAIAAIRNANHMGML
AYYAEAAARDGLIGIVMSTSEALVHPFGGTQALIGTNPVAIGIPAAGHPFVLDLATSIVS
MGKINNHAMRGLAIPPGWAVDRDGRATTDPHAAQAGAIAPFGDAKGYGLGLAIELLVAAL
AGSNLAPDVNGTLDDIHPANKGDLLILIDPSAGAGSIPALAAYLDRLRLSRPLDPTQPVA
IPGDGARARRAAAAKTGIELPQPLFDHLTALEAA
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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