SitesBLAST
Comparing 3609158 FitnessBrowser__Dino:3609158 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)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
37% identity, 97% coverage: 8:346/351 of query aligns to 5:338/340 of 1vbiA
- active site: H44 (= H47)
- binding nicotinamide-adenine-dinucleotide: H44 (= H47), H115 (= H119), G117 (= G121), A119 (≠ L123), T155 (= T160), P157 (= P162), A171 (≠ F177), D172 (= D178), L173 (≠ M179), A174 (= A180), F301 (≠ R309), P303 (= P311), L306 (≠ G314), E307 (≠ K315)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
33% identity, 96% coverage: 9:346/351 of query aligns to 6:337/344 of 2x06A
- active site: H44 (= H47)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ Y44), H44 (= H47), H116 (= H119), F117 (≠ A120), G118 (= G121), I119 (≠ P122), A120 (≠ L123), T156 (= T160), P158 (= P162), D173 (= D178), M174 (= M179), A175 (= A180), L301 (≠ R309), I306 (≠ G314), E307 (≠ K315)
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
34% identity, 88% coverage: 6:315/351 of query aligns to 3:309/338 of 4fjuA
- binding glyoxylic acid: R48 (= R51), H116 (= H119), S140 (= S144), D141 (≠ A145)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ Y44), H44 (= H47), H116 (= H119), G118 (= G121), I120 (≠ L123), S140 (= S144), F147 (≠ Y151), T156 (= T160), P158 (= P162), F173 (= F177), D174 (= D178), M175 (= M179), A176 (= A180), P223 (= P229), K224 (= K230), Y303 (≠ R309), G306 (= G312), D308 (≠ G314), Q309 (≠ K315)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
34% identity, 88% coverage: 6:315/351 of query aligns to 3:309/349 of P77555
- S43 (≠ T46) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H47) 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 (= R51) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y55) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H119) mutation to A: Loss of dehydrogenase activity.
- S140 (= S144) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ A145) 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 (≠ F257) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ T265) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
34% identity, 96% coverage: 11:347/351 of query aligns to 19:346/348 of 1v9nA
- active site: H55 (= H47)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H47), H127 (= H119), G129 (= G121), I130 (≠ P122), A131 (≠ L123), T167 (= T160), P169 (= P162), L183 (≠ F177), D184 (= D178), M185 (= M179), A186 (= A180), P191 (≠ A185), W308 (≠ R309), H310 (≠ P311), G311 (= G312), K313 (≠ G314), G314 (≠ K315)
Sites not aligning to the query:
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
27% identity, 97% coverage: 5:346/351 of query aligns to 4:357/361 of 3i0pA
- active site: H46 (= H47)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ Y44), H46 (= H47), H119 (= H119), I122 (≠ P122), A123 (≠ L123), T159 (= T160), P161 (= P162), F176 (= F177), D177 (= D178), G178 (≠ M179), A179 (= A180), P184 (≠ A185), R187 (≠ K188), Y320 (≠ R309), A322 (≠ P311), G323 (= G312), K325 (≠ G314), E326 (≠ K315)
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, 98% coverage: 2:345/351 of query aligns to 9:342/343 of Q4U331
- HFAAL 126:130 (≠ HAGPL 119:123) binding in other chain
- DLA 184:186 (≠ DMA 178:180) binding in other chain
- HK 236:237 (≠ PK 229:230) binding
- 309:315 (vs. 309:315, 71% identical) binding in other chain
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
34% identity, 98% coverage: 2:345/351 of query aligns to 3:336/337 of 2cwfB
- active site: H48 (= H47)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H47), H120 (= H119), A122 (≠ G121), A123 (≠ P122), L124 (= L123), T160 (= T160), P162 (= P162), F177 (= F177), D178 (= D178), L179 (≠ M179), A180 (= A180), H230 (≠ P229), K231 (= K230), R303 (= R309), G306 (= G312), R308 (≠ G314), R309 (≠ K315)
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
34% identity, 96% coverage: 5:342/351 of query aligns to 3:330/332 of 2cwhA
- active site: H45 (= H47)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H47), A119 (≠ G121), A120 (≠ P122), L121 (= L123), H148 (≠ Y151), T157 (= T160), P159 (= P162), F174 (= F177), D175 (= D178), L176 (≠ M179), A177 (= A180), H227 (≠ P229), K228 (= K230), R300 (= R309), G303 (= G312), R305 (≠ G314), R306 (≠ K315)
- binding pyrrole-2-carboxylate: H45 (= H47), R49 (= R51), M142 (≠ A145), T157 (= T160), H183 (≠ M186), G184 (= G187)
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
32% identity, 97% coverage: 9:348/351 of query aligns to 7:346/350 of 1z2iA
- active site: H45 (= H47)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ Y44), H45 (= H47), H117 (= H119), F118 (≠ A120), G119 (= G121), P120 (= P122), A121 (≠ L123), T157 (= T160), P159 (= P162), D175 (= D178), M176 (= M179), A177 (= A180), P182 (≠ A185), F227 (= F232), K228 (vs. gap), M307 (≠ R309), R312 (≠ G314), E313 (≠ K315)
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, 92% coverage: 8:330/351 of query aligns to 9:331/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
28% identity, 92% coverage: 8:330/351 of query aligns to 7:329/359 of 2g8yA
- active site: H46 (= H47)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ Y44), H46 (= H47), G120 (= G121), I122 (≠ L123), T160 (= T160), P162 (= P162), L176 (≠ V176), L177 (≠ F177), D178 (= D178), Y179 (≠ M179), A180 (= A180), H232 (≠ P229), Y235 (≠ F232), N268 (≠ T267), G311 (= G312), E314 (≠ K315)
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)
25% identity, 96% coverage: 6:342/351 of query aligns to 3:334/335 of 1s20G
- active site: H44 (= H47)
- binding nicotinamide-adenine-dinucleotide: H44 (= H47), H116 (= H119), W147 (≠ Y151), T156 (= T160), P158 (= P162), D172 (= D178), M173 (= M179), S174 (≠ A180), W224 (≠ P229), K225 (= K230), R301 (= R309), G304 (= G312), E306 (≠ G314)
Query Sequence
>3609158 FitnessBrowser__Dino:3609158
MPDDTISAEALQDFVARALSARGVPTQDANKVAGLMVEADIYGYGTHGVFRLRQYLARLE
GGGCNPAPNISVLQQTVATALIDGDNGFGHLAMAAARDLAMEKARQAGIGWVGVRRGNHA
GPLALYVRPQAEAGLLGMAAAVGSANHVPPYGGTDLLLGTNPIAFSAPAEGPDPFVFDMA
TTVAAMGKIKTLLQQGADMPEGWMVGRDGKPLTDPARKSEGFLLPIGGPKGFGLSVAIGL
MAGVLNGAAFGSDVVDFTSDTTSPTNTGQFVMALDPAAFGLGDGFAETARRVFGEMRASP
PLPGHHPVRLPGDGKTQAAETRRRQGLTLNPALRKDLDALAEKYGVEPVSS
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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