SitesBLAST
Comparing SMa1459 FitnessBrowser__Smeli:SMa1459 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
39% identity, 90% coverage: 3:303/334 of query aligns to 9:312/343 of Q4U331
Sites not aligning to the query:
- 309:315 binding in other chain
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
39% identity, 90% coverage: 3:303/334 of query aligns to 3:306/337 of 2cwfB
- active site: H48 (≠ C47)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (≠ C47), H120 (≠ N118), A122 (≠ L120), A123 (= A121), L124 (= L122), T160 (= T158), P162 (= P160), F177 (≠ V176), D178 (= D177), L179 (≠ Q178), A180 (≠ S179), H230 (≠ R228), K231 (= K229), R303 (= R300), G306 (= G303)
Sites not aligning to the query:
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
39% identity, 89% coverage: 6:303/334 of query aligns to 4:303/332 of 2cwhA
- active site: H45 (≠ C47)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (≠ C47), A119 (≠ L120), A120 (= A121), L121 (= L122), H148 (≠ P149), T157 (= T158), P159 (= P160), F174 (≠ V176), D175 (= D177), L176 (≠ Q178), A177 (≠ S179), H227 (≠ R228), K228 (= K229), R300 (= R300), G303 (= G303)
- binding pyrrole-2-carboxylate: H45 (≠ C47), R49 (≠ Y51), M142 (≠ P143), T157 (= T158), H183 (≠ K185), G184 (≠ T186)
Sites not aligning to the query:
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
36% identity, 80% coverage: 23:290/334 of query aligns to 20:284/340 of 1vbiA
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)
27% identity, 95% coverage: 4:320/334 of query aligns to 1:328/335 of 1s20G
- active site: H44 (≠ C47)
- binding nicotinamide-adenine-dinucleotide: H44 (≠ C47), H116 (≠ N118), W147 (≠ P149), T156 (= T158), P158 (= P160), D172 (= D177), M173 (≠ Q178), S174 (= S179), W224 (≠ R228), K225 (= K229), R301 (= R300), G304 (= G303), E306 (vs. gap)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
26% identity, 93% coverage: 9:320/334 of query aligns to 6:327/344 of 2x06A
- active site: H44 (≠ C47)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ N44), H44 (≠ C47), H116 (≠ N118), F117 (≠ C119), G118 (≠ L120), I119 (≠ A121), A120 (≠ L122), T156 (= T158), P158 (= P160), D173 (= D177), M174 (≠ Q178), A175 (≠ S179), L301 (≠ R300), I306 (vs. gap), E307 (vs. gap)
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
27% identity, 92% coverage: 4:311/334 of query aligns to 1:311/338 of 4fjuA
- binding glyoxylic acid: R48 (≠ Y51), H116 (≠ N118), S140 (≠ A142), D141 (≠ P143)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ N44), H44 (≠ C47), H116 (≠ N118), G118 (≠ L120), I120 (≠ L122), S140 (≠ A142), F147 (≠ P149), T156 (= T158), P158 (= P160), F173 (≠ V176), D174 (= D177), M175 (≠ Q178), A176 (≠ S179), P223 (≠ R228), K224 (= K229), Y303 (≠ G303), G306 (= G306), D308 (≠ K308), Q309 (= Q309)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
27% identity, 92% coverage: 4:311/334 of query aligns to 1:311/349 of P77555
- S43 (≠ V46) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (≠ C47) 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 (≠ Y51) mutation to A: Loss of dehydrogenase activity.
- Y52 (≠ F55) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (≠ N118) mutation to A: Loss of dehydrogenase activity.
- S140 (≠ A142) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ P143) 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 (≠ F256) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ P264) 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
30% identity, 85% coverage: 9:291/334 of query aligns to 7:292/350 of 1z2iA
- active site: H45 (≠ C47)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ N44), H45 (≠ C47), H117 (≠ N118), F118 (≠ C119), G119 (≠ L120), P120 (≠ A121), A121 (≠ L122), T157 (= T158), P159 (= P160), D175 (= D177), M176 (≠ Q178), A177 (≠ S179), P182 (≠ T184), F227 (vs. gap), K228 (= K229)
Sites not aligning to the query:
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
26% identity, 89% coverage: 7:304/334 of query aligns to 6:316/361 of 3i0pA
- active site: H46 (≠ C47)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ N44), H46 (≠ C47), H119 (≠ N118), I122 (≠ A121), A123 (≠ L122), T159 (= T158), P161 (= P160), F176 (≠ V175), D177 (≠ V176), G178 (≠ D177), A179 (vs. gap), P184 (≠ A182), R187 (≠ K185)
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, 91% coverage: 16:319/334 of query aligns to 7:336/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
31% identity, 69% coverage: 16:246/334 of query aligns to 5:250/359 of 2g8yA
- active site: H46 (≠ C47)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ N44), H46 (≠ C47), G120 (≠ L120), I122 (≠ L122), T160 (= T158), P162 (= P160), L176 (≠ V175), L177 (≠ V176), D178 (= D177), Y179 (≠ Q178), A180 (≠ S179), H232 (≠ R228), Y235 (≠ A231)
Sites not aligning to the query:
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
25% identity, 84% coverage: 13:291/334 of query aligns to 21:292/348 of 1v9nA
- active site: H55 (≠ C47)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (≠ C47), H127 (≠ N118), G129 (≠ L120), I130 (≠ A121), A131 (≠ L122), T167 (= T158), P169 (= P160), L183 (≠ V176), D184 (= D177), M185 (≠ Q178), A186 (≠ S179), P191 (= P199)
Sites not aligning to the query:
Query Sequence
>SMa1459 FitnessBrowser__Smeli:SMa1459
MTPVETSWEEIEAVCLEALTLHGAAAETARAVAGAITRAEADGNRVCGLYYLPIFCRHLA
IGKVDGEAVPEVTTRGVTVTVDARSGFAHPAIAAGTPALIDLARQAGLAAMAVRNSYNCL
ALGHHVRPLADAGLIGICVSNAPASVAPPGATRALFGTNPLAFAVPSKEGAPTIVVDQSM
SAVTKTEMILRRDRGEAIPIGWAQDGNGQPTTDAATGLEGSLLPAGGRKGANIALLVEVL
AAALTGSALSTEASAFGNEEGGPPHVGQFLIAIDPDHFAAGHFSEAMDNLVASHDAAGVR
LPGHFGRKQPVCVDADLWKKAVLLSKSKNRQKPG
Or try a new SitesBLAST search
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