SitesBLAST
Comparing BWI76_RS07040 FitnessBrowser__Koxy:BWI76_RS07040 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)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
83% identity, 100% coverage: 1:349/349 of query aligns to 1:349/349 of P77555
- S43 (= S43) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H44) 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 (= R48) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y52) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H116) mutation to A: Loss of dehydrogenase activity.
- S140 (= S140) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (= D141) 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 (= M251) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (= R259) 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)
83% identity, 97% coverage: 1:338/349 of query aligns to 1:338/338 of 4fjuA
- binding glyoxylic acid: R48 (= R48), H116 (= H116), S140 (= S140), D141 (= D141)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (= I41), H44 (= H44), H116 (= H116), G118 (= G118), I120 (= I120), S140 (= S140), F147 (= F147), T156 (= T156), P158 (= P158), F173 (= F173), D174 (= D174), M175 (= M175), A176 (= A176), P223 (= P223), K224 (= K224), Y303 (= Y303), G306 (= G306), D308 (≠ N308), Q309 (≠ L309)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
36% identity, 91% coverage: 16:331/349 of query aligns to 16:329/340 of 1vbiA
- active site: H44 (= H44)
- binding nicotinamide-adenine-dinucleotide: H44 (= H44), H115 (= H116), G117 (= G118), A119 (≠ I120), T155 (= T156), P157 (= P158), A171 (≠ F173), D172 (= D174), L173 (≠ M175), A174 (= A176), F301 (≠ Y303), P303 (= P305), L306 (≠ N308), E307 (≠ L309)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
36% identity, 95% coverage: 1:331/349 of query aligns to 1:328/344 of 2x06A
- active site: H44 (= H44)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ I41), H44 (= H44), H116 (= H116), F117 (≠ S117), G118 (= G118), I119 (≠ A119), A120 (≠ I120), T156 (= T156), P158 (= P158), D173 (= D174), M174 (= M175), A175 (= A176), L301 (≠ Y303), I306 (= I311), E307 (≠ N312)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
30% identity, 95% coverage: 1:331/349 of query aligns to 12:336/348 of 1v9nA
- active site: H55 (= H44)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H44), H127 (= H116), G129 (= G118), I130 (≠ A119), A131 (≠ I120), T167 (= T156), P169 (= P158), L183 (≠ F173), D184 (= D174), M185 (= M175), A186 (= A176), P191 (≠ A181), W308 (≠ Y303), H310 (≠ P305), G311 (= G306), K313 (≠ N308), G314 (≠ L309)
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)
31% identity, 94% coverage: 3:331/349 of query aligns to 4:328/332 of 2cwhA
- active site: H45 (= H44)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H44), A119 (≠ G118), A120 (= A119), L121 (≠ I120), H148 (≠ F147), T157 (= T156), P159 (= P158), F174 (= F173), D175 (= D174), L176 (≠ M175), A177 (= A176), H227 (≠ P223), K228 (= K224), R300 (≠ Y303), G303 (= G306), R305 (≠ N308), R306 (≠ L309)
- binding pyrrole-2-carboxylate: H45 (= H44), R49 (= R48), M142 (≠ D141), T157 (= T156), H183 (≠ W182), G184 (= G183)
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
31% identity, 94% coverage: 3:331/349 of query aligns to 7:331/337 of 2cwfB
- active site: H48 (= H44)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H44), H120 (= H116), A122 (≠ G118), A123 (= A119), L124 (≠ I120), T160 (= T156), P162 (= P158), F177 (= F173), D178 (= D174), L179 (≠ M175), A180 (= A176), H230 (≠ P223), K231 (= K224), R303 (≠ Y303), G306 (= G306), R308 (≠ N308), R309 (≠ L309)
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)
31% identity, 94% coverage: 3:331/349 of query aligns to 13:337/343 of Q4U331
- HFAAL 126:130 (≠ HSGAI 116:120) binding in other chain
- DLA 184:186 (≠ DMA 174:176) binding in other chain
- HK 236:237 (≠ PK 223:224) binding
- 309:315 (vs. 303:309, 29% identical) binding in other chain
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
28% identity, 88% coverage: 3:308/349 of query aligns to 5:325/361 of 3i0pA
- active site: H46 (= H44)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ I41), H46 (= H44), H119 (= H116), I122 (≠ A119), A123 (≠ I120), T159 (= T156), P161 (= P158), F176 (= F173), D177 (= D174), G178 (≠ M175), A179 (= A176), P184 (≠ A181), R187 (≠ K184), Y320 (= Y303), A322 (≠ P305), G323 (= G306), K325 (≠ N308)
Sites not aligning to the query:
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
29% identity, 83% coverage: 20:308/349 of query aligns to 21:312/350 of 1z2iA
- active site: H45 (= H44)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ I41), H45 (= H44), H117 (= H116), F118 (≠ S117), G119 (= G118), P120 (≠ A119), A121 (≠ I120), T157 (= T156), P159 (= P158), D175 (= D174), M176 (= M175), A177 (= A176), P182 (≠ A181), F227 (vs. gap), K228 (= K224), M307 (≠ Y303), R312 (≠ N308)
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, 89% coverage: 6:314/349 of query aligns to 10:320/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
29% identity, 89% coverage: 6:314/349 of query aligns to 8:318/359 of 2g8yA
- active site: H46 (= H44)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ I41), H46 (= H44), G120 (= G118), I122 (= I120), T160 (= T156), P162 (= P158), L176 (≠ T172), L177 (≠ F173), D178 (= D174), Y179 (≠ M175), A180 (= A176), H232 (≠ P223), Y235 (= Y226), N268 (≠ G262), G311 (= G306), E314 (≠ D310)
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)
23% identity, 94% coverage: 1:328/349 of query aligns to 1:326/335 of 1s20G
- active site: H44 (= H44)
- binding nicotinamide-adenine-dinucleotide: H44 (= H44), H116 (= H116), W147 (≠ F147), T156 (= T156), P158 (= P158), D172 (= D174), M173 (= M175), S174 (≠ A176), W224 (≠ P223), K225 (= K224), R301 (≠ Y303), G304 (= G306), E306 (≠ N308)
Query Sequence
>BWI76_RS07040 FitnessBrowser__Koxy:BWI76_RS07040
MKVSRETLHQLIANKLNIAGLTHNHADIIADVLVYADARGIHSHGAVRVEYYAERIAKGG
TNRQPNFTFEKTGPCSGILHADNAAGQVAAKMGMEHAIEIARENGVAVVGIRRMGHSGAI
SYFVQQAARAGFIGLSLCQSDPMVVPFGGAEIYYGTNPLAFAAPGEGDDIITFDMATTVQ
AWGKILDARSRHETIPDSWAVDKNGAPTSDPFAVHALLPAAGPKGYGLMMMIDVLSGILL
NLPFGRQVSSMYDNLSQGRELGQLHIVINPAFFSSSALFRQHISDTMRELNAIAPAPGFN
QVYYPGQNLDINEKNSAVDGIEIVDEIYDYLVSDALYNRSYETHSPFAQ
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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