SitesBLAST
Comparing SM_b20261 FitnessBrowser__Smeli:SM_b20261 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)
41% identity, 97% coverage: 4:336/345 of query aligns to 10:340/343 of Q4U331
- HFAAL 126:130 (≠ HFSAL 121:125) binding in other chain
- DLA 184:186 (≠ DFA 179:181) binding in other chain
- HK 236:237 (= HK 230:231) binding
- 309:315 (vs. 305:311, 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)
41% identity, 97% coverage: 4:336/345 of query aligns to 1:331/332 of 2cwhA
- active site: H45 (= H48)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H48), A119 (≠ S123), A120 (= A124), L121 (= L125), H148 (≠ T152), T157 (= T161), P159 (= P163), F174 (= F178), D175 (= D179), L176 (≠ F180), A177 (= A181), H227 (= H230), K228 (= K231), R300 (= R305), G303 (≠ S308), R305 (= R310), R306 (= R311)
- binding pyrrole-2-carboxylate: H45 (= H48), R49 (= R52), M142 (≠ Y146), T157 (= T161), H183 (≠ R187), G184 (= G188)
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
41% identity, 97% coverage: 4:336/345 of query aligns to 4:334/337 of 2cwfB
- active site: H48 (= H48)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H48), H120 (= H121), A122 (≠ S123), A123 (= A124), L124 (= L125), T160 (= T161), P162 (= P163), F177 (= F178), D178 (= D179), L179 (≠ F180), A180 (= A181), H230 (= H230), K231 (= K231), R303 (= R305), G306 (≠ S308), R308 (= R310), R309 (= R311)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
34% identity, 67% coverage: 17:248/345 of query aligns to 13:239/340 of 1vbiA
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)
29% identity, 92% coverage: 12:327/345 of query aligns to 12:332/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
29% identity, 92% coverage: 12:327/345 of query aligns to 10:330/359 of 2g8yA
- active site: H46 (= H48)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ C45), H46 (= H48), G120 (≠ S123), I122 (≠ L125), T160 (= T161), P162 (= P163), L176 (≠ V177), L177 (≠ F178), D178 (= D179), Y179 (≠ F180), A180 (= A181), H232 (= H230), Y235 (≠ S233), N268 (≠ H268), G311 (≠ S308), E314 (≠ R311)
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
27% identity, 71% coverage: 3:246/345 of query aligns to 1:257/361 of 3i0pA
- active site: H46 (= H48)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ C45), H46 (= H48), H119 (= H121), I122 (≠ A124), A123 (≠ L125), T159 (= T161), P161 (= P163), F176 (= F178), D177 (= D179), G178 (≠ F180), A179 (= A181), P184 (≠ A186), R187 (≠ E189)
Sites not aligning to the query:
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
29% identity, 80% coverage: 7:282/345 of query aligns to 3:275/338 of 4fjuA
- binding glyoxylic acid: R48 (= R52), H116 (= H121), S140 (= S145), D141 (≠ Y146)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ C45), H44 (= H48), H116 (= H121), G118 (≠ S123), I120 (≠ L125), S140 (= S145), F147 (≠ T152), T156 (= T161), P158 (= P163), F173 (= F178), D174 (= D179), M175 (≠ F180), A176 (= A181), P223 (≠ H230), K224 (= K231)
Sites not aligning to the query:
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
29% identity, 80% coverage: 7:282/345 of query aligns to 3:275/349 of P77555
- S43 (= S47) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H48) 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 (= R52) mutation to A: Loss of dehydrogenase activity.
- Y52 (≠ A56) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H121) mutation to A: Loss of dehydrogenase activity.
- S140 (= S145) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ Y146) 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 (≠ Y258) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ P266) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
32% identity, 66% coverage: 19:245/345 of query aligns to 15:239/344 of 2x06A
- active site: H44 (= H48)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ C45), H44 (= H48), H116 (= H121), F117 (= F122), G118 (≠ S123), I119 (≠ A124), A120 (≠ L125), T156 (= T161), P158 (= P163), D173 (= D179), M174 (≠ F180), A175 (= A181)
Sites not aligning to the query:
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
28% identity, 90% coverage: 12:322/345 of query aligns to 9:324/350 of 1z2iA
- active site: H45 (= H48)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ C45), H45 (= H48), H117 (= H121), F118 (= F122), G119 (≠ S123), P120 (≠ A124), A121 (≠ L125), T157 (= T161), P159 (= P163), D175 (= D179), M176 (≠ F180), A177 (= A181), P182 (≠ A186), F227 (vs. gap), K228 (= K231), M307 (vs. gap), R312 (= R310), E313 (≠ R311)
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, 94% coverage: 14:337/345 of query aligns to 6:333/335 of 1s20G
- active site: H44 (= H48)
- binding nicotinamide-adenine-dinucleotide: H44 (= H48), H116 (= H121), W147 (≠ T152), T156 (= T161), P158 (= P163), D172 (= D179), M173 (≠ F180), S174 (≠ A181), W224 (≠ H230), K225 (= K231), R301 (= R305), G304 (≠ S308), E306 (≠ R310)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
28% identity, 66% coverage: 29:255/345 of query aligns to 36:256/348 of 1v9nA
- active site: H55 (= H48)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H48), H127 (= H121), G129 (≠ S123), I130 (≠ A124), A131 (≠ L125), T167 (= T161), P169 (= P163), L183 (≠ F178), D184 (= D179), M185 (≠ F180), A186 (= A181), P191 (≠ A186)
Sites not aligning to the query:
Query Sequence
>SM_b20261 FitnessBrowser__Smeli:SM_b20261
MSETTTLTTTALQERVEAIFRKGGLNVVQAGALARVIVAGERDACKSHGIYRIEGALRTV
KAGKVKPDAEPEIVAQEASAIVKVNAGGGFANPAFELGLPVLAERARKHGIAALAINDCT
HFSALWPEAEALTGEGLAGLVMCPSYATVAPTGGNKPLLGTNPFAFGWPRAGKPPYVFDF
ATSVAARGEIELHRRAGKPLPEGWAIDAQGNPTTDPEAALAGAMLPFGGHKGSAIGTMIE
LLAGIMIGDLTSPEVLDYLGTTTLAPFHGELIVAFSPQAFAAGRPGDPFARAELLFEAIV
GQGARLPSQRRFAARAKSEAEGITLSAAEIEQLDRLLALGLDAVA
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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