SitesBLAST
Comparing BWI76_RS16775 FitnessBrowser__Koxy:BWI76_RS16775 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)
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)
72% identity, 100% coverage: 1:360/360 of query aligns to 1:360/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
72% identity, 99% coverage: 3:360/360 of query aligns to 1:358/359 of 2g8yA
- active site: H46 (= H48)
- binding nicotinamide-adenine-dinucleotide: H43 (= H45), H46 (= H48), G120 (= G122), I122 (= I124), T160 (= T162), P162 (= P164), L176 (= L178), L177 (= L179), D178 (= D180), Y179 (= Y181), A180 (= A182), H232 (= H234), Y235 (= Y237), N268 (= N270), G311 (= G313), E314 (= E316)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
33% identity, 93% coverage: 13:347/360 of query aligns to 9:337/344 of 2x06A
- active site: H44 (= H48)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ H45), H44 (= H48), H116 (= H120), F117 (≠ I121), G118 (= G122), I119 (≠ R123), A120 (≠ I124), T156 (= T162), P158 (= P164), D173 (= D180), M174 (≠ Y181), A175 (= A182), L301 (= L310), I306 (≠ W315), E307 (= E316)
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
34% identity, 69% coverage: 12:258/360 of query aligns to 9:251/332 of 2cwhA
- active site: H45 (= H48)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H48), A119 (≠ G122), A120 (≠ R123), L121 (≠ I124), H148 (≠ F153), T157 (= T162), P159 (= P164), F174 (≠ L179), D175 (= D180), L176 (≠ Y181), A177 (= A182), H227 (= H234), K228 (= K235)
- binding pyrrole-2-carboxylate: H45 (= H48), R49 (≠ M52), M142 (≠ V145), T157 (= T162), H183 (≠ F188), G184 (= G189)
Sites not aligning to the query:
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
34% identity, 69% coverage: 12:258/360 of query aligns to 12:254/337 of 2cwfB
- active site: H48 (= H48)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H48), H120 (= H120), A122 (≠ G122), A123 (≠ R123), L124 (≠ I124), T160 (= T162), P162 (= P164), F177 (≠ L179), D178 (= D180), L179 (≠ Y181), A180 (= A182), H230 (= H234), K231 (= K235)
Sites not aligning to the query:
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, 69% coverage: 12:258/360 of query aligns to 18:260/343 of Q4U331
Sites not aligning to the query:
- 309:315 binding in other chain
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
31% identity, 94% coverage: 11:347/360 of query aligns to 8:344/350 of 1z2iA
- active site: H45 (= H48)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ H45), H45 (= H48), H117 (= H120), F118 (≠ I121), G119 (= G122), P120 (≠ R123), A121 (≠ I124), T157 (= T162), P159 (= P164), D175 (= D180), M176 (≠ Y181), A177 (= A182), P182 (≠ A187), F227 (= F231), K228 (= K235), M307 (≠ L310), R312 (vs. gap), E313 (= E314)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
31% identity, 95% coverage: 6:348/360 of query aligns to 2:339/340 of 1vbiA
- active site: H44 (= H48)
- binding nicotinamide-adenine-dinucleotide: H44 (= H48), H115 (= H120), G117 (= G122), A119 (≠ I124), T155 (= T162), P157 (= P164), A171 (≠ L179), D172 (= D180), L173 (≠ Y181), A174 (= A182), F301 (≠ L310), P303 (= P312), L306 (≠ W315), E307 (= E316)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
30% identity, 95% coverage: 6:347/360 of query aligns to 13:345/348 of 1v9nA
- active site: H55 (= H48)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H48), H127 (= H120), G129 (= G122), I130 (≠ R123), A131 (≠ I124), T167 (= T162), P169 (= P164), L183 (= L179), D184 (= D180), M185 (≠ Y181), A186 (= A182), P191 (≠ A187), W308 (≠ L310), H310 (≠ P312), G311 (= G313), K313 (≠ W315), G314 (≠ E316)
Sites not aligning to the query:
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
27% identity, 92% coverage: 12:342/360 of query aligns to 8:335/349 of P77555
- S43 (= S47) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H48) 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 (≠ M52) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y56) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H120) mutation to A: Loss of dehydrogenase activity.
- S140 (≠ G146) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ N147) 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 (≠ L261) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ F269) 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)
27% identity, 92% coverage: 12:342/360 of query aligns to 8:335/338 of 4fjuA
- binding glyoxylic acid: R48 (≠ M52), H116 (= H120), S140 (≠ G146), D141 (≠ N147)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ H45), H44 (= H48), H116 (= H120), G118 (= G122), I120 (= I124), S140 (≠ G146), F147 (= F153), T156 (= T162), P158 (= P164), F173 (≠ L179), D174 (= D180), M175 (≠ Y181), A176 (= A182), P223 (≠ H234), K224 (= K235), Y303 (≠ L310), G306 (= G313), D308 (≠ W315), Q309 (≠ E316)
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
30% identity, 67% coverage: 12:251/360 of query aligns to 10:258/361 of 3i0pA
- active site: H46 (= H48)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ H45), H46 (= H48), H119 (= H120), I122 (≠ R123), A123 (≠ I124), T159 (= T162), P161 (= P164), F176 (≠ L179), D177 (= D180), G178 (≠ Y181), A179 (= A182), P184 (≠ A187), R187 (≠ K190)
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)
25% identity, 91% coverage: 15:343/360 of query aligns to 12:334/335 of 1s20G
- active site: H44 (= H48)
- binding nicotinamide-adenine-dinucleotide: H44 (= H48), H116 (= H120), W147 (≠ F153), T156 (= T162), P158 (= P164), D172 (= D180), M173 (≠ Y181), S174 (≠ A182), W224 (≠ H234), K225 (= K235), R301 (≠ L310), G304 (= G313), E306 (≠ W315)
Query Sequence
>BWI76_RS16775 FitnessBrowser__Koxy:BWI76_RS16775
MQTGHRFQATDLHQFVKTLFTHMGSSPTEASLIADHLIAANLAGHDSHGVGMIPSYVRSH
AQGYLQLNRHASVMKDAGAVVTLDGNGGFGQVVAHEAMQIGIEKAKQHGLAAVALRNAHH
IGRIGYWAEQCAAAGMISIHFVNVVGNVMVAPFRGKDSRFGTNPLCVVFPRVGHPPLLLD
YATSAIAFGKTRVAWHKGVPVPAGSLIDARGVPTTDPAVMQTSPLGALLTFAEHKGYALA
TLCEAIGGAVSGGKTSHQETLQGSVDAIFNCMTTIILSPEAFDAPDMQRETEAFIDWCKQ
SPHEPDAPILAPGEWEEANRRQRLAQGIPLDAGSWQAICAAAEEVGVPADTLAQLRQKLA
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