SitesBLAST
Comparing RR42_RS29130 FitnessBrowser__Cup4G11:RR42_RS29130 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
48% identity, 95% coverage: 2:347/364 of query aligns to 3:345/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
48% identity, 95% coverage: 2:347/364 of query aligns to 1:343/359 of 2g8yA
- active site: H46 (= H47)
- binding nicotinamide-adenine-dinucleotide: H43 (= H44), H46 (= H47), G120 (= G121), I122 (≠ V123), T160 (= T161), P162 (= P163), L176 (≠ V177), L177 (≠ M178), D178 (= D179), Y179 (≠ F180), A180 (= A181), H232 (= H236), Y235 (= Y239), N268 (= N271), G311 (= G316), E314 (= E319)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
32% identity, 91% coverage: 12:342/364 of query aligns to 9:330/344 of 2x06A
- active site: H44 (= H47)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ H44), H44 (= H47), H116 (= H119), F117 (≠ L120), G118 (= G121), I119 (≠ R122), A120 (≠ V123), T156 (= T161), P158 (= P163), D173 (= D179), M174 (≠ F180), A175 (= A181), L301 (= L313), I306 (≠ P318), E307 (= E319)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
34% identity, 92% coverage: 11:346/364 of query aligns to 8:335/340 of 1vbiA
- active site: H44 (= H47)
- binding nicotinamide-adenine-dinucleotide: H44 (= H47), H115 (= H119), G117 (= G121), A119 (≠ V123), T155 (= T161), P157 (= P163), A171 (≠ M178), D172 (= D179), L173 (≠ F180), A174 (= A181), F301 (≠ L313), P303 (= P315), L306 (≠ P318), E307 (= E319)
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
33% identity, 88% coverage: 6:327/364 of query aligns to 7:316/337 of 2cwfB
- active site: H48 (= H47)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H47), H120 (= H119), A122 (≠ G121), A123 (≠ R122), L124 (≠ V123), T160 (= T161), P162 (= P163), F177 (≠ M178), D178 (= D179), L179 (≠ F180), A180 (= A181), H230 (= H236), K231 (= K237), R303 (≠ L313), G306 (= G316), R308 (≠ E319), R309 (= R320)
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, 88% coverage: 6:327/364 of query aligns to 13:322/343 of Q4U331
- HFAAL 126:130 (≠ HLGRV 119:123) binding in other chain
- DLA 184:186 (≠ DFA 179:181) binding in other chain
- HK 236:237 (= HK 236:237) binding
- 309:315 (vs. 313:320, 50% 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)
33% identity, 88% coverage: 6:327/364 of query aligns to 4:313/332 of 2cwhA
- active site: H45 (= H47)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H47), A119 (≠ G121), A120 (≠ R122), L121 (≠ V123), H148 (= H152), T157 (= T161), P159 (= P163), F174 (≠ M178), D175 (= D179), L176 (≠ F180), A177 (= A181), H227 (= H236), K228 (= K237), R300 (≠ L313), G303 (= G316), R305 (≠ E319), R306 (= R320)
- binding pyrrole-2-carboxylate: H45 (= H47), R49 (≠ M51), M142 (≠ L144), T157 (= T161), H183 (≠ L187), G184 (= G188)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
29% identity, 94% coverage: 5:347/364 of query aligns to 13:343/348 of 1v9nA
- active site: H55 (= H47)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H47), H127 (= H119), G129 (= G121), I130 (≠ R122), A131 (≠ V123), T167 (= T161), P169 (= P163), L183 (≠ M178), D184 (= D179), M185 (≠ F180), A186 (= A181), P191 (≠ A186), W308 (≠ L313), H310 (≠ P315), G311 (= G316), K313 (≠ P318), G314 (≠ E319)
Sites not aligning to the query:
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
30% identity, 89% coverage: 5:327/364 of query aligns to 2:317/338 of 4fjuA
- binding glyoxylic acid: R48 (≠ M51), H116 (= H119), S140 (= S145), D141 (≠ K146)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ H44), H44 (= H47), H116 (= H119), G118 (= G121), I120 (≠ V123), S140 (= S145), F147 (≠ H152), T156 (= T161), P158 (= P163), F173 (≠ M178), D174 (= D179), M175 (≠ F180), A176 (= A181), P223 (≠ H236), K224 (= K237), Y303 (≠ L313), G306 (= G316), D308 (≠ P318), Q309 (≠ E319)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
30% identity, 89% coverage: 5:327/364 of query aligns to 2:317/349 of P77555
- S43 (= S46) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H47) 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 (≠ M51) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y55) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H119) mutation to A: Loss of dehydrogenase activity.
- S140 (= S145) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ K146) 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 (≠ T264) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ W270) 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: 6:329/364 of query aligns to 5:336/361 of 3i0pA
- active site: H46 (= H47)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ H44), H46 (= H47), H119 (= H119), I122 (≠ R122), A123 (≠ V123), T159 (= T161), P161 (= P163), F176 (≠ M178), D177 (= D179), G178 (≠ F180), A179 (= A181), P184 (≠ A186), R187 (≠ K189), Y320 (≠ L313), A322 (≠ P315), G323 (= G316), K325 (≠ P318), E326 (= E319)
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
28% identity, 93% coverage: 11:350/364 of query aligns to 9:345/350 of 1z2iA
- active site: H45 (= H47)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ H44), H45 (= H47), H117 (= H119), F118 (≠ L120), G119 (= G121), P120 (≠ R122), A121 (≠ V123), T157 (= T161), P159 (= P163), D175 (= D179), M176 (≠ F180), A177 (= A181), P182 (≠ A186), F227 (≠ H236), K228 (= K237), M307 (≠ L313), R312 (≠ P318), E313 (= 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)
25% identity, 81% coverage: 23:316/364 of query aligns to 20:304/335 of 1s20G
- active site: H44 (= H47)
- binding nicotinamide-adenine-dinucleotide: H44 (= H47), H116 (= H119), W147 (≠ H152), T156 (= T161), P158 (= P163), D172 (= D179), M173 (≠ F180), S174 (≠ A181), W224 (≠ H236), K225 (= K237), R301 (≠ L313), G304 (= G316)
Sites not aligning to the query:
Query Sequence
>RR42_RS29130 FitnessBrowser__Cup4G11:RR42_RS29130
MSEHRIPTPALHQWVVDLWRAAGSDAREARLTADHLVGANLSGHDSHGVGMIPKYVMSWQ
GEQLQLNQRVSVVHEAGGILSLDGNRGMGQAVTEEAMGLAIERAREHGVCVLGLRASHHL
GRVGHWAEQATAAGMISIHFVNVLSKPIVAPHGGYEARYGTNPFTIGVPVAGGEPLVMDF
ATSAIALGKVRVANNKGVAVPPGCLLDTEGHPTDDPAVMFPPAGEAQGALRPFGEHKGYV
LAVMCELLGAAVTGGHTIRPETLTHEHAVWNNMLAIVFDPERLGSSTTFGHEVQAFVDWL
RSSHLQPGTDAILLPGEPERAWRRARAEFMPVDSGTLAQLDDAAARVQAARGKSPGPLSR
LAVD
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