SitesBLAST
Comparing RR42_RS02230 FitnessBrowser__Cup4G11:RR42_RS02230 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)
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
37% identity, 93% coverage: 21:332/334 of query aligns to 21:332/332 of 2cwhA
- active site: H45 (= H45)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H45), A119 (≠ G119), A120 (= A120), L121 (≠ V121), H148 (≠ W148), T157 (= T157), P159 (= P159), F174 (≠ I174), D175 (= D175), L176 (= L176), A177 (≠ S177), H227 (≠ V226), K228 (= K227), R300 (= R300), G303 (= G303), R305 (= R305), R306 (= R306)
- binding pyrrole-2-carboxylate: H45 (= H45), R49 (= R49), M142 (≠ P142), T157 (= T157), H183 (≠ R183), G184 (= G184)
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)
37% identity, 93% coverage: 21:332/334 of query aligns to 30:341/343 of Q4U331
- HFAAL 126:130 (≠ HAGAV 117:121) binding in other chain
- DLA 184:186 (≠ DLS 175:177) binding in other chain
- HK 236:237 (≠ VK 226:227) binding
- 309:315 (vs. 300:306, 86% identical) binding in other chain
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
37% identity, 93% coverage: 21:332/334 of query aligns to 24:335/337 of 2cwfB
- active site: H48 (= H45)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H45), H120 (= H117), A122 (≠ G119), A123 (= A120), L124 (≠ V121), T160 (= T157), P162 (= P159), F177 (≠ I174), D178 (= D175), L179 (= L176), A180 (≠ S177), H230 (≠ V226), K231 (= K227), R303 (= R300), G306 (= G303), R308 (= R305), R309 (= R306)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
32% identity, 99% coverage: 4:333/334 of query aligns to 3:333/344 of 2x06A
- active site: H44 (= H45)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ L42), H44 (= H45), H116 (= H117), F117 (≠ A118), G118 (= G119), I119 (≠ A120), A120 (≠ V121), T156 (= T157), P158 (= P159), D173 (= D175), M174 (≠ L176), A175 (≠ S177), L301 (vs. gap), I306 (= I307), E307 (≠ D308)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
35% identity, 99% coverage: 4:333/334 of query aligns to 3:334/340 of 1vbiA
- active site: H44 (= H45)
- binding nicotinamide-adenine-dinucleotide: H44 (= H45), H115 (= H117), G117 (= G119), A119 (≠ V121), T155 (= T157), P157 (= P159), A171 (≠ I174), D172 (= D175), L173 (= L176), A174 (≠ S177), F301 (≠ R300), P303 (= P302), L306 (≠ R305), E307 (≠ R306)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
29% identity, 96% coverage: 7:328/334 of query aligns to 6:331/349 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 (= R49) 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 (= S141) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ P142) 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 (≠ F254) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ P262) 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)
29% identity, 96% coverage: 7:328/334 of query aligns to 6:331/338 of 4fjuA
- binding glyoxylic acid: R48 (= R49), H116 (= H117), S140 (= S141), D141 (≠ P142)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ L42), H44 (= H45), H116 (= H117), G118 (= G119), I120 (≠ V121), S140 (= S141), F147 (≠ W148), T156 (= T157), P158 (= P159), F173 (≠ I174), D174 (= D175), M175 (≠ L176), A176 (≠ S177), P223 (≠ V226), K224 (= K227), Y303 (vs. gap), G306 (vs. gap), D308 (= D308), Q309 (≠ A309)
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
27% identity, 98% coverage: 7:332/334 of query aligns to 8:352/361 of 3i0pA
- active site: H46 (= H45)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ L42), H46 (= H45), H119 (= H117), I122 (≠ A120), A123 (≠ V121), T159 (= T157), P161 (= P159), F176 (≠ I174), D177 (= D175), G178 (≠ L176), A179 (≠ S177), P184 (≠ A182), R187 (≠ K185), Y320 (vs. gap), A322 (vs. gap), G323 (vs. gap), K325 (vs. gap), E326 (vs. gap)
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, 72% coverage: 4:244/334 of query aligns to 7:252/361 of P30178
Sites not aligning to the query:
- 270 binding
- 313:316 binding
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
32% identity, 72% coverage: 4:244/334 of query aligns to 5:250/359 of 2g8yA
- active site: H46 (= H45)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ L42), H46 (= H45), G120 (= G119), I122 (≠ V121), T160 (= T157), P162 (= P159), L176 (≠ V173), L177 (≠ I174), D178 (= D175), Y179 (≠ L176), A180 (≠ S177), H232 (≠ V226), Y235 (≠ A229)
Sites not aligning to the query:
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
28% identity, 98% coverage: 7:333/334 of query aligns to 17:341/348 of 1v9nA
- active site: H55 (= H45)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H45), H127 (= H117), G129 (= G119), I130 (≠ A120), A131 (≠ V121), T167 (= T157), P169 (= P159), L183 (≠ I174), D184 (= D175), M185 (≠ L176), A186 (≠ S177), P191 (≠ A182), W308 (≠ D308), H310 (= H310), G311 (≠ A311), K313 (≠ A313), G314 (vs. gap)
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: 9:333/334 of query aligns to 5:334/335 of 1s20G
- active site: H44 (= H45)
- binding nicotinamide-adenine-dinucleotide: H44 (= H45), H116 (= H117), W147 (= W148), T156 (= T157), P158 (= P159), D172 (= D175), M173 (≠ L176), S174 (= S177), W224 (≠ V226), K225 (= K227), R301 (= R300), G304 (= G303), E306 (≠ R305)
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
28% identity, 99% coverage: 5:333/334 of query aligns to 5:340/350 of 1z2iA
- active site: H45 (= H45)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ L42), H45 (= H45), H117 (= H117), F118 (≠ A118), G119 (= G119), P120 (≠ A120), A121 (≠ V121), T157 (= T157), P159 (= P159), D175 (= D175), M176 (≠ L176), A177 (≠ S177), P182 (≠ A182), F227 (≠ V226), K228 (= K227), M307 (≠ R300), R312 (= R305), E313 (≠ R306)
Query Sequence
>RR42_RS02230 FitnessBrowser__Cup4G11:RR42_RS02230
MTAFRAEELEQLAANALRSAGASAAQAGPTAHALVQADLAGLPSHGVSRVPMYVAHLRHQ
RVNGDAQPTVARQTPGTTLIDAQGGFAFPACAQAVSAAIASARECGIGAGVVTNSHHAGA
VALHLDPVAQAGMIGIAMGNSPAAMPAWGGRTPLFGTNPIAAVFPRRDAAPLVIDLSLSE
VARGKIMVAAKQGKPIPLGWALDADGKPTTDAQAALRGSMLPAGGVKGAMLALLVETLIV
SLAGAHFGAEADSFFEDAGNQPRIGQLFLAFNPGGFAGDAAYHARLEALIAAMLSDSGTR
LPGTRRIDAHAKAREHGIEIPEALEKELRKLAQA
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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