SitesBLAST
Comparing 3608646 FitnessBrowser__Dino:3608646 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)
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)
38% identity, 97% coverage: 6:335/339 of query aligns to 10:341/343 of Q4U331
- HFAAL 126:130 (≠ HCGAL 122:126) binding in other chain
- DLA 184:186 (≠ DLS 180:182) binding in other chain
- HK 236:237 (≠ AK 231:232) binding
- 309:315 (vs. 303:309, 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)
38% identity, 97% coverage: 6:335/339 of query aligns to 1:332/332 of 2cwhA
- active site: H45 (= H50)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H50), A119 (≠ G124), A120 (= A125), L121 (= L126), H148 (≠ W153), T157 (= T162), P159 (= P164), F174 (≠ I179), D175 (= D180), L176 (= L181), A177 (≠ S182), H227 (≠ A231), K228 (= K232), R300 (= R303), G303 (= G306), R305 (= R308), R306 (= R309)
- binding pyrrole-2-carboxylate: H45 (= H50), R49 (= R54), M142 (≠ P147), T157 (= T162), H183 (≠ R188), G184 (= G189)
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
38% identity, 97% coverage: 6:335/339 of query aligns to 4:335/337 of 2cwfB
- active site: H48 (= H50)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H50), H120 (= H122), A122 (≠ G124), A123 (= A125), L124 (= L126), T160 (= T162), P162 (= P164), F177 (≠ I179), D178 (= D180), L179 (= L181), A180 (≠ S182), H230 (≠ A231), K231 (= K232), R303 (= R303), G306 (= G306), R308 (= R308), R309 (= R309)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
36% identity, 88% coverage: 26:324/339 of query aligns to 20:322/340 of 1vbiA
- active site: H44 (= H50)
- binding nicotinamide-adenine-dinucleotide: H44 (= H50), H115 (= H122), G117 (= G124), A119 (≠ L126), T155 (= T162), P157 (= P164), A171 (≠ I179), D172 (= D180), L173 (= L181), A174 (≠ S182), F301 (≠ R303), P303 (= P305), L306 (≠ R308), E307 (≠ R309)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
31% identity, 85% coverage: 13:300/339 of query aligns to 7:293/344 of 2x06A
- active site: H44 (= H50)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ Q47), H44 (= H50), H116 (= H122), F117 (≠ C123), G118 (= G124), I119 (≠ A125), A120 (≠ L126), T156 (= T162), P158 (= P164), D173 (= D180), M174 (≠ L181), A175 (≠ S182)
Sites not aligning to the query:
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
28% identity, 84% coverage: 15:299/339 of query aligns to 9:293/338 of 4fjuA
- binding glyoxylic acid: R48 (= R54), H116 (= H122), S140 (≠ A146), D141 (≠ P147)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ Q47), H44 (= H50), H116 (= H122), G118 (= G124), I120 (≠ L126), S140 (≠ A146), F147 (≠ W153), T156 (= T162), P158 (= P164), F173 (≠ I179), D174 (= D180), M175 (≠ L181), A176 (≠ S182), P223 (≠ A231), K224 (= K232)
Sites not aligning to the query:
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
28% identity, 84% coverage: 15:299/339 of query aligns to 9:293/349 of P77555
- S43 (≠ G49) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H50) 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 (= R54) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y58) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H122) mutation to A: Loss of dehydrogenase activity.
- S140 (≠ A146) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ P147) 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 (≠ F259) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ P267) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
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, 67% coverage: 22:249/339 of query aligns to 20:252/361 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.
33% identity, 67% coverage: 22:249/339 of query aligns to 18:250/359 of 2g8yA
- active site: H46 (= H50)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ Q47), H46 (= H50), G120 (= G124), I122 (≠ L126), T160 (= T162), P162 (= P164), L176 (≠ V178), L177 (≠ I179), D178 (= D180), Y179 (≠ L181), A180 (≠ S182), H232 (≠ A231), Y235 (≠ T234)
Sites not aligning to the query:
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
26% identity, 99% coverage: 2:335/339 of query aligns to 6:340/348 of 1v9nA
- active site: H55 (= H50)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H50), H127 (= H122), G129 (= G124), I130 (≠ A125), A131 (≠ L126), T167 (= T162), P169 (= P164), L183 (≠ I179), D184 (= D180), M185 (≠ L181), A186 (≠ S182), P191 (≠ A187), W308 (≠ R303), H310 (≠ P305), G311 (= G306), K313 (≠ R308), G314 (≠ R309)
Sites not aligning to the query:
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
26% identity, 73% coverage: 5:252/339 of query aligns to 1:262/361 of 3i0pA
- active site: H46 (= H50)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ Q47), H46 (= H50), H119 (= H122), I122 (≠ A125), A123 (≠ L126), T159 (= T162), P161 (= P164), F176 (≠ I179), D177 (= D180), G178 (≠ L181), A179 (≠ S182), P184 (≠ A187), R187 (≠ K190)
Sites not aligning to the query:
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
30% identity, 79% coverage: 22:288/339 of query aligns to 17:281/350 of 1z2iA
- active site: H45 (= H50)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ Q47), H45 (= H50), H117 (= H122), F118 (≠ C123), G119 (= G124), P120 (≠ A125), A121 (≠ L126), T157 (= T162), P159 (= P164), D175 (= D180), M176 (≠ L181), A177 (≠ S182), P182 (≠ A187), F227 (vs. gap), K228 (= K232)
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)
23% identity, 90% coverage: 20:323/339 of query aligns to 14:321/335 of 1s20G
- active site: H44 (= H50)
- binding nicotinamide-adenine-dinucleotide: H44 (= H50), H116 (= H122), W147 (= W153), T156 (= T162), P158 (= P164), D172 (= D180), M173 (≠ L181), S174 (= S182), W224 (≠ A231), K225 (= K232), R301 (= R303), G304 (= G306), E306 (≠ R308)
Query Sequence
>3608646 FitnessBrowser__Dino:3608646
MYMSETETLSLPDARDLLFRAFTANGVPEGAARSTADALVAAEAEGQVGHGFSRLEDYVA
QARSGKIVAGAEVTITRPAPTTLLVDAGHGFAYPALERAIDEGIAVARELGTAAIAVTRS
HHCGALSIHVERAAKAGLVAMMVVNAPAAIAPWGGKTPLFGTNPIAFATPRAGSAPLVID
LSLSKVARGKVMNAKKAGKPIPEGWALDAAGNPTTDAEAALGGTMVPIGEAKGTALALMV
EILSAVMTGAALSTEAGSFFSADGPPPGVGQFLTLWRPPEGAEAFTARLAPLLAQIETME
GARLPGTRRLAALNAAQAHGIAVPRAYLDGARRLAATHP
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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