SitesBLAST
Comparing BPHYT_RS28460 FitnessBrowser__BFirm:BPHYT_RS28460 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)
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
34% identity, 90% coverage: 32:359/363 of query aligns to 33:359/361 of 3i0pA
- active site: H46 (= H45)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ I42), H46 (= H45), H119 (= H117), I122 (≠ A120), A123 (= A121), T159 (= T158), P161 (= P160), F176 (≠ L175), D177 (= D176), G178 (≠ M177), A179 (≠ S178), P184 (≠ A183), R187 (≠ K186), Y320 (≠ L320), A322 (≠ P322), G323 (= G323), K325 (≠ P325), E326 (= E326)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
36% identity, 94% coverage: 16:357/363 of query aligns to 26:345/348 of 1v9nA
- active site: H55 (= H45)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H45), H127 (= H117), G129 (= G119), I130 (≠ A120), A131 (= A121), T167 (= T158), P169 (= P160), L183 (= L175), D184 (= D176), M185 (= M177), A186 (≠ S178), P191 (≠ A183), W308 (≠ L320), H310 (≠ P322), G311 (= G323), K313 (≠ P325), G314 (≠ E326)
Sites not aligning to the query:
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
35% identity, 94% coverage: 16:356/363 of query aligns to 15:336/344 of 2x06A
- active site: H44 (= H45)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ I42), H44 (= H45), H116 (= H117), F117 (= F118), G118 (= G119), I119 (≠ A120), A120 (= A121), T156 (= T158), P158 (= P160), D173 (= D176), M174 (= M177), A175 (≠ S178), L301 (= L320), I306 (≠ P325), E307 (= E326)
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)
32% identity, 98% coverage: 3:358/363 of query aligns to 6:348/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
32% identity, 98% coverage: 3:358/363 of query aligns to 4:346/359 of 2g8yA
- active site: H46 (= H45)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ I42), H46 (= H45), G120 (= G119), I122 (≠ A121), T160 (= T158), P162 (= P160), L176 (≠ I174), L177 (= L175), D178 (= D176), Y179 (≠ M177), A180 (≠ S178), H232 (= H241), Y235 (= Y244), N268 (≠ H280), G311 (= G323), E314 (= E326)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
33% identity, 95% coverage: 14:359/363 of query aligns to 13:340/340 of 1vbiA
- active site: H44 (= H45)
- binding nicotinamide-adenine-dinucleotide: H44 (= H45), H115 (= H117), G117 (= G119), A119 (= A121), T155 (= T158), P157 (= P160), A171 (vs. gap), D172 (= D176), L173 (≠ M177), A174 (≠ S178), F301 (≠ L320), P303 (= P322), L306 (≠ P325), E307 (= E326)
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
28% identity, 95% coverage: 3:348/363 of query aligns to 2:331/338 of 4fjuA
- binding glyoxylic acid: R48 (≠ M49), H116 (= H117), S140 (≠ T141), D141 (≠ R142)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (= I42), H44 (= H45), H116 (= H117), G118 (= G119), I120 (≠ A121), S140 (≠ T141), F147 (≠ T149), T156 (= T158), P158 (= P160), F173 (≠ L175), D174 (= D176), M175 (= M177), A176 (≠ S178), P223 (≠ H241), K224 (= K242), Y303 (≠ L320), G306 (= G323), D308 (≠ P325), Q309 (≠ E326)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
28% identity, 95% coverage: 3:348/363 of query aligns to 2:331/349 of P77555
- S43 (= S44) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H45) 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 (≠ M49) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y53) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H117) mutation to A: Loss of dehydrogenase activity.
- S140 (≠ T141) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ R142) 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 (≠ K271) 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.
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
33% identity, 86% coverage: 41:353/363 of query aligns to 41:340/350 of 1z2iA
- active site: H45 (= H45)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ I42), H45 (= H45), H117 (= H117), F118 (= F118), G119 (= G119), P120 (≠ A120), A121 (= A121), T157 (= T158), P159 (= P160), D175 (= D176), M176 (= M177), A177 (≠ S178), P182 (≠ A183), F227 (≠ H241), K228 (= K242), M307 (≠ L320), R312 (≠ P325), E313 (= E326)
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
27% identity, 93% coverage: 16:352/363 of query aligns to 16:332/332 of 2cwhA
- active site: H45 (= H45)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H45), A119 (≠ G119), A120 (= A120), L121 (≠ A121), H148 (≠ T149), T157 (= T158), P159 (= P160), F174 (≠ L175), D175 (= D176), L176 (≠ M177), A177 (≠ S178), H227 (= H241), K228 (= K242), R300 (≠ Q311), G303 (= G323), R305 (≠ P325), R306 (≠ E326)
- binding pyrrole-2-carboxylate: H45 (= H45), R49 (≠ M49), M142 (≠ L143), T157 (= T158), H183 (≠ S184), G184 (≠ N185)
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
27% identity, 93% coverage: 16:352/363 of query aligns to 19:335/337 of 2cwfB
- active site: H48 (= H45)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H45), H120 (= H117), A122 (≠ G119), A123 (= A120), L124 (≠ A121), T160 (= T158), P162 (= P160), F177 (≠ L175), D178 (= D176), L179 (≠ M177), A180 (≠ S178), H230 (= H241), K231 (= K242), R303 (≠ Q311), G306 (= G323), R308 (≠ P325), R309 (≠ E326)
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)
27% identity, 93% coverage: 16:352/363 of query aligns to 25:341/343 of Q4U331
- HFAAL 126:130 (≠ HFGAA 117:121) binding in other chain
- DLA 184:186 (≠ DMS 176:178) binding in other chain
- HK 236:237 (= HK 241:242) binding
- 309:315 (vs. 311:326, 19% identical) binding in other chain
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, 92% coverage: 16:349/363 of query aligns to 15:330/335 of 1s20G
- active site: H44 (= H45)
- binding nicotinamide-adenine-dinucleotide: H44 (= H45), H116 (= H117), W147 (≠ F150), T156 (= T158), P158 (= P160), D172 (= D176), M173 (= M177), S174 (= S178), W224 (≠ H241), K225 (= K242), R301 (≠ L320), G304 (= G323), E306 (≠ P325)
Query Sequence
>BPHYT_RS28460 FitnessBrowser__BFirm:BPHYT_RS28460
MPRVGAAIARQQIEVILEAWGMSPGQVAASADILIDSDLKGIDSHGISMLMFYDQLYRAG
QIDMKASARIVRETATTALIDGNAAMGHPTSRMAMELAIEKALACDMGAVSVFNSQHFGA
AGYYAEMAAERGLIALVSCSTRLATVVPTFGAEPMLGTNPFAFATPAGRHPPVILDMSTS
VVASNKVKVYALQGKPLPPGWALDANGNPLTDSAEAYRLLFERLGGGLAPLGGDGKTLGG
HKGYGLGLFAQILGSTLGGGSFSPVRNRTQKSDEPDNIGHFFLAMNPAAFRPIEEYHADL
DAVIDALRESQPADPAQPVLIPGDPERLTRAARSAEGIPMPDSLREKIREVAKAAGAPFL
LAV
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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