SitesBLAST
Comparing 8501262 FitnessBrowser__Miya:8501262 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)
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
40% identity, 91% coverage: 10:334/356 of query aligns to 12:323/337 of 2cwfB
- active site: H48 (= H46)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H46), H120 (= H118), A122 (≠ G120), A123 (≠ V121), L124 (≠ A122), T160 (= T158), P162 (= P160), F177 (≠ M190), D178 (= D191), L179 (= L192), A180 (≠ S193), H230 (≠ A242), K231 (= K243), R303 (= R314), G306 (= G317), R308 (= R319), 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)
40% identity, 91% coverage: 10:334/356 of query aligns to 18:329/343 of Q4U331
- HFAAL 126:130 (≠ HCGVA 118:122) binding in other chain
- DLA 184:186 (≠ DLS 191:193) binding in other chain
- HK 236:237 (≠ AK 242:243) binding
- 309:315 (vs. 314:320, 86% 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)
40% identity, 91% coverage: 10:334/356 of query aligns to 9:320/332 of 2cwhA
- active site: H45 (= H46)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H46), A119 (≠ G120), A120 (≠ V121), L121 (≠ A122), H148 (≠ W149), T157 (= T158), P159 (= P160), F174 (≠ M190), D175 (= D191), L176 (= L192), A177 (≠ S193), H227 (≠ A242), K228 (= K243), R300 (= R314), G303 (= G317), R305 (= R319), R306 (= R320)
- binding pyrrole-2-carboxylate: H45 (= H46), R49 (= R50), M142 (≠ P143), T157 (= T158), H183 (≠ R199), G184 (= G200)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
37% identity, 93% coverage: 6:335/356 of query aligns to 4:322/340 of 1vbiA
- active site: H44 (= H46)
- binding nicotinamide-adenine-dinucleotide: H44 (= H46), H115 (= H118), G117 (= G120), A119 (= A122), T155 (= T158), P157 (= P160), A171 (≠ M190), D172 (= D191), L173 (= L192), A174 (≠ S193), F301 (≠ R314), P303 (= P316), L306 (≠ R319), E307 (≠ R320)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
30% identity, 96% coverage: 3:342/356 of query aligns to 1:328/344 of 2x06A
- active site: H44 (= H46)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ I43), H44 (= H46), H116 (= H118), F117 (≠ C119), G118 (= G120), I119 (≠ V121), A120 (= A122), T156 (= T158), P158 (= P160), D173 (= D191), M174 (≠ L192), A175 (≠ S193), L301 (≠ R314), I306 (≠ R319), E307 (≠ R320)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
29% identity, 95% coverage: 8:346/356 of query aligns to 6:335/349 of P77555
- S43 (= S45) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H46) 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 (= R50) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y54) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H118) mutation to A: Loss of dehydrogenase activity.
- S140 (≠ T142) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ P143) 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 (≠ F270) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ P278) 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, 95% coverage: 8:346/356 of query aligns to 6:335/338 of 4fjuA
- binding glyoxylic acid: R48 (= R50), H116 (= H118), S140 (≠ T142), D141 (≠ P143)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (= I43), H44 (= H46), H116 (= H118), G118 (= G120), I120 (≠ A122), S140 (≠ T142), F147 (≠ W149), T156 (= T158), P158 (= P160), F173 (≠ M190), D174 (= D191), M175 (≠ L192), A176 (≠ S193), P223 (≠ A242), K224 (= K243), Y303 (vs. gap), G306 (= G317), D308 (≠ R319), Q309 (≠ R320)
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)
28% identity, 91% coverage: 10:332/356 of query aligns to 12:328/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
28% identity, 91% coverage: 10:332/356 of query aligns to 10:326/359 of 2g8yA
- active site: H46 (= H46)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ I43), H46 (= H46), G120 (= G120), I122 (≠ A122), T160 (= T158), P162 (= P160), L176 (≠ V189), L177 (≠ M190), D178 (= D191), Y179 (≠ L192), A180 (≠ S193), H232 (≠ A242), Y235 (≠ A245), N268 (≠ Q282), G311 (= G317), E314 (≠ R320)
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
32% identity, 82% coverage: 2:292/356 of query aligns to 1:278/350 of 1z2iA
- active site: H45 (= H46)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ I43), H45 (= H46), H117 (= H118), F118 (≠ C119), G119 (= G120), P120 (≠ V121), A121 (= A122), T157 (= T158), P159 (= P160), D175 (= D191), M176 (≠ L192), A177 (≠ S193), P182 (≠ A198), F227 (vs. gap), K228 (= K243)
Sites not aligning to the query:
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
29% identity, 71% coverage: 7:260/356 of query aligns to 16:249/348 of 1v9nA
- active site: H55 (= H46)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H46), H127 (= H118), G129 (= G120), I130 (≠ V121), A131 (= A122), T167 (= T158), P169 (= P160), L183 (≠ M190), D184 (= D191), M185 (≠ L192), A186 (≠ S193), P191 (≠ A198)
Sites not aligning to the query:
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
26% identity, 72% coverage: 8:262/356 of query aligns to 8:261/361 of 3i0pA
- active site: H46 (= H46)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ I43), H46 (= H46), H119 (= H118), I122 (≠ V121), A123 (= A122), T159 (= T158), P161 (= P160), F176 (≠ M190), D177 (= D191), G178 (≠ L192), A179 (≠ S193), P184 (≠ A198), R187 (≠ K201)
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)
26% identity, 70% coverage: 11:259/356 of query aligns to 10:241/335 of 1s20G
Sites not aligning to the query:
Query Sequence
>8501262 FitnessBrowser__Miya:8501262
MSVILRPDDLAALCRTVLERAGVLPAAASSVAGALVAAECMGIPSHGVARLPQYADQVAA
GKVRGDAVPRVETPLPATVRVDAGCGFAYPALEAGLDVAVPLALRMGCAALGVTNSHHCG
VAGLHVERAARQGLVALLFANTPAAMAPWGGNRASLGTNPLAFACPAPPEDAPEPTAAAG
AGPEHDPLVMDLSLSTVARGKIVAAAREGQPIPAGWAVDAHGSPTTDARAALGGMLLPFG
GAKGAALALMVELLAASLTGSNHAYEASSFLDAAGGPPRTGQCMLLIAPQAFGADFSGRA
AALLGHVLDQPCTRLPGARRFERQRRAHREGVAIPWSLHQDMLRRAEGVHADNPRP
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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