SitesBLAST
Comparing WP_086509097.1 NCBI__GCF_002151265.1:WP_086509097.1 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)
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
52% identity, 96% coverage: 12:352/357 of query aligns to 7:346/350 of 1z2iA
- active site: H45 (= H50)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ T47), H45 (= H50), H117 (= H122), F118 (= F123), G119 (= G124), P120 (≠ A125), A121 (= A126), T157 (= T162), P159 (= P164), D175 (= D180), M176 (= M181), A177 (= A182), P182 (= P187), F227 (= F233), K228 (= K234), M307 (≠ L313), R312 (= R318), E313 (= E319)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
38% identity, 93% coverage: 20:351/357 of query aligns to 14:339/340 of 1vbiA
- active site: H44 (= H50)
- binding nicotinamide-adenine-dinucleotide: H44 (= H50), H115 (= H122), G117 (= G124), A119 (= A126), T155 (= T162), P157 (= P164), A171 (≠ L179), D172 (= D180), L173 (≠ M181), A174 (= A182), F301 (≠ L313), P303 (= P315), L306 (≠ R318), E307 (= E319)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
32% identity, 91% coverage: 8:333/357 of query aligns to 2:323/349 of P77555
- S43 (= S49) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H50) 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 (≠ L54) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y58) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H122) mutation to A: Loss of dehydrogenase activity.
- S140 (= S146) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (= D147) 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 (= M261) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (= R270) 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)
32% identity, 91% coverage: 8:333/357 of query aligns to 2:323/338 of 4fjuA
- binding glyoxylic acid: R48 (≠ L54), H116 (= H122), S140 (= S146), D141 (= D147)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ T47), H44 (= H50), H116 (= H122), G118 (= G124), I120 (≠ A126), S140 (= S146), F147 (≠ H153), T156 (= T162), P158 (= P164), F173 (≠ L179), D174 (= D180), M175 (= M181), A176 (= A182), P223 (≠ S229), K224 (= K234), Y303 (≠ L313), G306 (= G316), D308 (≠ R318), Q309 (≠ E319)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
31% identity, 98% coverage: 3:353/357 of query aligns to 8:348/348 of 1v9nA
- active site: H55 (= H50)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H50), H127 (= H122), G129 (= G124), I130 (≠ A125), A131 (= A126), T167 (= T162), P169 (= P164), L183 (= L179), D184 (= D180), M185 (= M181), A186 (= A182), P191 (= P187), W308 (≠ L313), H310 (≠ P315), G311 (= G316), K313 (≠ R318), G314 (≠ E319)
Sites not aligning to the query:
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
29% identity, 94% coverage: 12:348/357 of query aligns to 6:335/344 of 2x06A
- active site: H44 (= H50)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ T47), H44 (= H50), H116 (= H122), F117 (= F123), G118 (= G124), I119 (≠ A125), A120 (= A126), T156 (= T162), P158 (= P164), D173 (= D180), M174 (= M181), A175 (= A182), L301 (= L313), I306 (≠ R318), E307 (= E319)
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
30% identity, 96% coverage: 8:351/357 of query aligns to 4:358/361 of 3i0pA
- active site: H46 (= H50)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ T47), H46 (= H50), H119 (= H122), I122 (≠ A125), A123 (= A126), T159 (= T162), P161 (= P164), F176 (≠ L179), D177 (= D180), G178 (≠ M181), A179 (= A182), P184 (= P187), R187 (= R190), Y320 (≠ L313), A322 (≠ P315), G323 (= G316), K325 (≠ R318), E326 (= E319)
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, 97% coverage: 7:351/357 of query aligns to 5:348/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
29% identity, 97% coverage: 7:351/357 of query aligns to 3:346/359 of 2g8yA
- active site: H46 (= H50)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ T47), H46 (= H50), G120 (= G124), I122 (≠ A126), T160 (= T162), P162 (= P164), L176 (= L178), L177 (= L179), D178 (= D180), Y179 (≠ M181), A180 (= A182), H232 (vs. gap), Y235 (≠ A236), N268 (≠ P269), G311 (= G316), E314 (= E319)
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, 95% coverage: 8:346/357 of query aligns to 2:334/335 of 1s20G
- active site: H44 (= H50)
- binding nicotinamide-adenine-dinucleotide: H44 (= H50), H116 (= H122), W147 (≠ H153), T156 (= T162), P158 (= P164), D172 (= D180), M173 (= M181), S174 (≠ A182), W224 (≠ F233), K225 (= K234), R301 (≠ L313), G304 (= G316), E306 (≠ R318)
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
33% identity, 85% coverage: 41:345/357 of query aligns to 36:332/332 of 2cwhA
- active site: H45 (= H50)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H50), A119 (≠ G124), A120 (= A125), L121 (≠ A126), H148 (= H153), T157 (= T162), P159 (= P164), F174 (≠ L179), D175 (= D180), L176 (≠ M181), A177 (= A182), H227 (≠ S229), K228 (= K234), R300 (≠ V312), G303 (= G316), R305 (= R318), R306 (≠ E319)
- binding pyrrole-2-carboxylate: H45 (= H50), R49 (≠ L54), M142 (≠ D147), T157 (= T162), H183 (≠ W188), G184 (≠ N189)
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
33% identity, 85% coverage: 41:345/357 of query aligns to 39:335/337 of 2cwfB
- active site: H48 (= H50)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H50), H120 (= H122), A122 (≠ G124), A123 (= A125), L124 (≠ A126), T160 (= T162), P162 (= P164), F177 (≠ L179), D178 (= D180), L179 (≠ M181), A180 (= A182), H230 (≠ S229), K231 (= K234), R303 (≠ V312), G306 (= G316), R308 (= R318), R309 (≠ E319)
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)
33% identity, 85% coverage: 41:345/357 of query aligns to 45:341/343 of Q4U331
- HFAAL 126:130 (≠ HFGAA 122:126) binding in other chain
- DLA 184:186 (≠ DMA 180:182) binding in other chain
- H----K 236:237 (≠ SDFGFK 229:234) binding
- 309:315 (vs. 312:319, 50% identical) binding in other chain
Query Sequence
>WP_086509097.1 NCBI__GCF_002151265.1:WP_086509097.1
MGDATDYRVAREELERFMLAALARAGADEASAGAATRALVTASRMGTDSHGLRLLPHYVQ
ALQGGRLKGAPEMRFERRLPATGYLDADHGLGHLAAYTAMAHAAEMAEQVGMGAVAVGNA
SHFGAAGCYALAAAERGLIGLVTCNSDPFVLLHQGSRPFHGTNPIAFAAPVAGESPYLLD
MATSAIPWNRVQQYGAIGRELPDQVAADAEGRVTRTPGEVAALLPLGGSDFGFKGAGLGG
MVEVLSSMLAGMQHGYRLLPMGGPDMATPRGVAHFVMALKPDAFAPGDPFPACLRRYLDD
LRAQPGRNGCEVLVPGEREWGCQAQRDARGIPLDSANQAAYAELAERLDVPPLRPLS
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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