SitesBLAST
Comparing Pf1N1B4_5979 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5979 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)
44% identity, 97% coverage: 8:333/335 of query aligns to 8:331/332 of 2cwhA
- active site: H45 (= H45)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H45), A119 (≠ S119), A120 (= A120), L121 (= L121), H148 (≠ A148), T157 (= T157), P159 (= P159), F174 (= F174), D175 (= D175), L176 (≠ F176), A177 (= A177), H227 (= H227), K228 (= K228), R300 (= R302), G303 (≠ S305), R305 (= R307), R306 (= R308)
- binding pyrrole-2-carboxylate: H45 (= H45), R49 (= R49), M142 (≠ H142), 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)
44% identity, 97% coverage: 8:333/335 of query aligns to 17:340/343 of Q4U331
- HFAAL 126:130 (≠ HFSAL 117:121) binding in other chain
- DLA 184:186 (≠ DFA 175:177) binding in other chain
- HK 236:237 (= HK 227:228) binding
- 309:315 (vs. 302:308, 71% identical) binding in other chain
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
44% identity, 97% coverage: 8:333/335 of query aligns to 11:334/337 of 2cwfB
- active site: H48 (= H45)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H45), H120 (= H117), A122 (≠ S119), A123 (= A120), L124 (= L121), T160 (= T157), P162 (= P159), F177 (= F174), D178 (= D175), L179 (≠ F176), A180 (= A177), H230 (= H227), K231 (= K228), R303 (= R302), G306 (≠ S305), R308 (= R307), R309 (= R308)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
33% identity, 96% coverage: 13:333/335 of query aligns to 12:332/340 of 1vbiA
- active site: H44 (= H45)
- binding nicotinamide-adenine-dinucleotide: H44 (= H45), H115 (= H117), G117 (≠ S119), A119 (≠ L121), T155 (= T157), P157 (= P159), A171 (≠ F174), D172 (= D175), L173 (≠ F176), A174 (= A177), F301 (≠ R302), P303 (= P304), L306 (≠ R307), E307 (≠ R308)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
27% identity, 97% coverage: 10:333/335 of query aligns to 9:331/344 of 2x06A
- active site: H44 (= H45)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ C42), H44 (= H45), H116 (= H117), F117 (= F118), G118 (≠ S119), I119 (≠ A120), A120 (≠ L121), T156 (= T157), P158 (= P159), D173 (= D175), M174 (≠ F176), A175 (= A177), L301 (≠ R302), I306 (≠ R307), E307 (≠ R308)
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)
33% identity, 71% coverage: 14:251/335 of query aligns to 17:258/361 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.
33% identity, 71% coverage: 14:251/335 of query aligns to 15:256/359 of 2g8yA
- active site: H46 (= H45)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ C42), H46 (= H45), G120 (≠ S119), I122 (≠ L121), T160 (= T157), P162 (= P159), L176 (≠ V173), L177 (≠ F174), D178 (= D175), Y179 (≠ F176), A180 (= A177), H232 (= H227), Y235 (≠ S230)
Sites not aligning to the query:
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
27% identity, 96% coverage: 10:330/335 of query aligns to 9:331/349 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 (≠ C53) 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 (≠ H142) 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 (≠ A254) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ S259) 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, 96% coverage: 10:330/335 of query aligns to 9:331/338 of 4fjuA
- binding glyoxylic acid: R48 (= R49), H116 (= H117), S140 (= S141), D141 (≠ H142)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ C42), H44 (= H45), H116 (= H117), G118 (≠ S119), I120 (≠ L121), S140 (= S141), F147 (≠ A148), T156 (= T157), P158 (= P159), F173 (= F174), D174 (= D175), M175 (≠ F176), A176 (= A177), P223 (≠ H227), K224 (= K228), Y303 (≠ R302), G306 (≠ S305), D308 (≠ R307), Q309 (≠ R308)
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
26% identity, 70% coverage: 10:243/335 of query aligns to 11:257/361 of 3i0pA
- active site: H46 (= H45)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ C42), H46 (= H45), H119 (= H117), I122 (≠ A120), A123 (≠ L121), T159 (= T157), P161 (= P159), F176 (= F174), D177 (= D175), G178 (≠ F176), A179 (= A177), P184 (≠ A182), R187 (≠ D185)
Sites not aligning to the query:
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
27% identity, 95% coverage: 6:322/335 of query aligns to 6:327/350 of 1z2iA
- active site: H45 (= H45)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ C42), H45 (= H45), H117 (= H117), F118 (= F118), G119 (≠ S119), P120 (≠ A120), A121 (≠ L121), T157 (= T157), P159 (= P159), D175 (= D175), M176 (≠ F176), A177 (= A177), P182 (≠ A182), F227 (≠ H227), K228 (= K228), M307 (≠ R302), R312 (= R307), E313 (≠ R308)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
28% identity, 65% coverage: 27:245/335 of query aligns to 37:249/348 of 1v9nA
- active site: H55 (= H45)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H45), H127 (= H117), G129 (≠ S119), I130 (≠ A120), A131 (≠ L121), T167 (= T157), P169 (= P159), L183 (≠ F174), D184 (= D175), M185 (≠ F176), A186 (= A177), P191 (≠ A182)
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)
24% identity, 99% coverage: 2:334/335 of query aligns to 1:333/335 of 1s20G
- active site: H44 (= H45)
- binding nicotinamide-adenine-dinucleotide: H44 (= H45), H116 (= H117), W147 (≠ A148), T156 (= T157), P158 (= P159), D172 (= D175), M173 (≠ F176), S174 (≠ A177), W224 (≠ H227), K225 (= K228), R301 (= R302), G304 (≠ S305), E306 (≠ R307)
Query Sequence
>Pf1N1B4_5979 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5979
MIRLTLIQARELAESILLHNGFNLAHAQAVAATVIAGERDGCASHGLYRILGCVNSLRAG
KVSADAEPQVIDQAPSIVRVDAGGGFSQLAFQAGLGLLAEKTRANGIAALAINRCVHFSA
LWVEIEQLTAVGLVALACNPSHAWVAPAGGRVPVFGTNPIAFGWPRAGQDPFVFDFATSA
IARGDIELHRRAGKAIPEGWGVDAEGRPSTDANVVLDSGAMLTFGGHKGSALAAMVELIA
GPLIGDLTSAESLAYDAGSKSSPYHGELIIALDPRRFLGAATEEHLARAEVLFQGIEGQG
ARLPSQRRYAARARSVVEGVQIPEALYNDLKALLA
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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