SitesBLAST
Comparing RR42_RS03780 FitnessBrowser__Cup4G11:RR42_RS03780 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)
34% identity, 98% coverage: 2:344/349 of query aligns to 6:347/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
34% identity, 98% coverage: 2:344/349 of query aligns to 4:345/359 of 2g8yA
- active site: H46 (= H44)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ Y41), H46 (= H44), G120 (= G118), I122 (≠ M120), T160 (= T159), P162 (= P161), L176 (≠ V176), L177 (≠ V177), D178 (= D178), Y179 (≠ I179), A180 (= A180), H232 (= H232), Y235 (= Y235), N268 (= N266), G311 (= G311), E314 (= E314)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
31% identity, 99% coverage: 1:346/349 of query aligns to 1:339/344 of 2x06A
- active site: H44 (= H44)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ Y41), H44 (= H44), H116 (= H116), F117 (≠ L117), G118 (= G118), I119 (≠ R119), A120 (≠ M120), T156 (= T159), P158 (= P161), D173 (= D178), M174 (≠ I179), A175 (= A180), L301 (≠ Q308), I306 (≠ F313), E307 (= E314)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
38% identity, 91% coverage: 1:318/349 of query aligns to 1:311/340 of 1vbiA
- active site: H44 (= H44)
- binding nicotinamide-adenine-dinucleotide: H44 (= H44), H115 (= H116), G117 (= G118), A119 (≠ M120), T155 (= T159), P157 (= P161), A171 (≠ V177), D172 (= D178), L173 (≠ I179), A174 (= A180), F301 (≠ Q308), P303 (= P310), L306 (≠ F313), E307 (= E314)
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: 11:339/349 of query aligns to 21:341/343 of Q4U331
- HFAAL 126:130 (≠ HLGRM 116:120) binding in other chain
- DLA 184:186 (≠ DIA 178:180) binding in other chain
- HK 236:237 (= HK 232:233) binding
- 309:315 (vs. 308:314, 29% identical) binding in other chain
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: 11:339/349 of query aligns to 12:332/332 of 2cwhA
- active site: H45 (= H44)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H44), A119 (≠ G118), A120 (≠ R119), L121 (≠ M120), H148 (≠ Y150), T157 (= T159), P159 (= P161), F174 (≠ V177), D175 (= D178), L176 (≠ I179), A177 (= A180), H227 (= H232), K228 (= K233), R300 (≠ Q308), G303 (= G311), R305 (≠ F313), R306 (≠ E314)
- binding pyrrole-2-carboxylate: H45 (= H44), R49 (≠ I48), M142 (≠ I141), T157 (= T159), H183 (≠ I186), G184 (≠ N187)
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
31% identity, 94% coverage: 11:339/349 of query aligns to 15:335/337 of 2cwfB
- active site: H48 (= H44)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H44), H120 (= H116), A122 (≠ G118), A123 (≠ R119), L124 (≠ M120), T160 (= T159), P162 (= P161), F177 (≠ V177), D178 (= D178), L179 (≠ I179), A180 (= A180), H230 (= H232), K231 (= K233), R303 (≠ Q308), G306 (= G311), R308 (≠ F313), R309 (≠ E314)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
30% identity, 95% coverage: 15:344/349 of query aligns to 26:345/348 of 1v9nA
- active site: H55 (= H44)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H44), H127 (= H116), G129 (= G118), I130 (≠ R119), A131 (≠ M120), T167 (= T159), P169 (= P161), L183 (≠ V177), D184 (= D178), M185 (≠ I179), A186 (= A180), P191 (≠ A185), W308 (≠ Q308), H310 (≠ P310), G311 (= G311), K313 (≠ A316), G314 (≠ N317)
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, 97% coverage: 1:338/349 of query aligns to 1:332/335 of 1s20G
- active site: H44 (= H44)
- binding nicotinamide-adenine-dinucleotide: H44 (= H44), H116 (= H116), W147 (≠ Y150), T156 (= T159), P158 (= P161), D172 (= D178), M173 (≠ I179), S174 (≠ A180), W224 (≠ H232), K225 (= K233), R301 (≠ Q308), G304 (= G311), E306 (= E312)
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
30% identity, 96% coverage: 1:335/349 of query aligns to 1:331/338 of 4fjuA
- binding glyoxylic acid: R48 (≠ I48), H116 (= H116), S140 (≠ R143), D141 (≠ S144)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ Y41), H44 (= H44), H116 (= H116), G118 (= G118), I120 (≠ M120), S140 (≠ R143), F147 (≠ Y150), T156 (= T159), P158 (= P161), F173 (≠ V177), D174 (= D178), M175 (≠ I179), A176 (= A180), P223 (≠ H232), K224 (= K233), Y303 (≠ Q308), G306 (= G311), D308 (≠ F313), Q309 (≠ E314)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
30% identity, 96% coverage: 1:335/349 of query aligns to 1:331/349 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 (≠ I48) 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 (≠ R143) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ S144) 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 (≠ E257) 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.
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
26% identity, 89% coverage: 3:314/349 of query aligns to 5:326/361 of 3i0pA
- active site: H46 (= H44)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ Y41), H46 (= H44), H119 (= H116), I122 (≠ R119), A123 (≠ M120), T159 (= T159), P161 (= P161), F176 (≠ V177), D177 (= D178), G178 (≠ I179), A179 (= A180), P184 (≠ A185), R187 (≠ K188), Y320 (≠ Q308), A322 (≠ P310), G323 (= G311), K325 (≠ F313), E326 (= E314)
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
26% identity, 98% coverage: 5:347/349 of query aligns to 6:347/350 of 1z2iA
- active site: H45 (= H44)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ Y41), H45 (= H44), H117 (= H116), F118 (≠ L117), G119 (= G118), P120 (≠ R119), A121 (≠ M120), T157 (= T159), P159 (= P161), D175 (= D178), M176 (≠ I179), A177 (= A180), P182 (≠ A185), F227 (vs. gap), K228 (= K233), M307 (≠ Q308), R312 (≠ F313), E313 (= E314)
Query Sequence
>RR42_RS03780 FitnessBrowser__Cup4G11:RR42_RS03780
MKITLQSATRLARDLLAAQGVPTDIANDVAEHLVEADRCGYTSHGLSILPNYQRSLATGN
VNPAGRAECVLDRDSLLVFDGNGGFGQHVGKCVIETAIERVRQHGHCIVTLRRSHHLGRM
GHYGEMVAKERFVLLSFTNVINRSPVVAPYGGRTARLTTNPLCFAGPMPNGRPPLVVDIA
TSAIAINKARVLAEKGEPAPENSIIDGDGNPTTDAGAMFSEHPGALLPFGGHKGYALGVV
AELLAGVLSGGGTIQPENPRGGVATNNMFAVLMNPELDLGLSWQGAEVEAFVNYLHDTPP
APGFDNVQYPGEFEAANRALTTTHLEVNPAIWRNLETLAKELGVALPAG
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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