SitesBLAST
Comparing AZOBR_RS16020 FitnessBrowser__azobra:AZOBR_RS16020 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)
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)
39% identity, 95% coverage: 2:339/356 of query aligns to 4:338/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
39% identity, 95% coverage: 2:339/356 of query aligns to 2:336/359 of 2g8yA
- active site: H46 (= H46)
- binding nicotinamide-adenine-dinucleotide: H43 (= H43), H46 (= H46), G120 (= G120), I122 (≠ V122), T160 (= T160), P162 (= P162), L176 (= L177), L177 (= L178), D178 (= D179), Y179 (≠ F180), A180 (= A181), H232 (= H233), Y235 (= Y236), N268 (= N267), G311 (= G314), E314 (= E317)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
35% identity, 96% coverage: 13:354/356 of query aligns to 11:343/344 of 2x06A
- active site: H44 (= H46)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ H43), H44 (= H46), H116 (= H118), F117 (≠ I119), G118 (= G120), I119 (≠ R121), A120 (≠ V122), T156 (= T160), P158 (= P162), D173 (= D179), M174 (≠ F180), A175 (= A181), L301 (= L311), I306 (≠ P316), E307 (= E317)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
33% identity, 97% coverage: 5:348/356 of query aligns to 3:338/340 of 1vbiA
- active site: H44 (= H46)
- binding nicotinamide-adenine-dinucleotide: H44 (= H46), H115 (= H118), G117 (= G120), A119 (≠ V122), T155 (= T160), P157 (= P162), A171 (≠ L178), D172 (= D179), L173 (≠ F180), A174 (= A181), F301 (≠ L311), P303 (= P313), L306 (≠ P316), E307 (= E317)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
37% identity, 69% coverage: 7:252/356 of query aligns to 16:250/348 of 1v9nA
- active site: H55 (= H46)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H46), H127 (= H118), G129 (= G120), I130 (≠ R121), A131 (≠ V122), T167 (= T160), P169 (= P162), L183 (= L178), D184 (= D179), M185 (≠ F180), A186 (= A181), P191 (≠ A186)
Sites not aligning to the query:
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
36% identity, 69% coverage: 9:252/356 of query aligns to 11:249/337 of 2cwfB
- active site: H48 (= H46)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H46), H120 (= H118), A122 (≠ G120), A123 (≠ R121), L124 (≠ V122), T160 (= T160), P162 (= P162), F177 (≠ L178), D178 (= D179), L179 (≠ F180), A180 (= A181), H230 (= H233), K231 (= K234)
Sites not aligning to the query:
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
36% identity, 69% coverage: 9:252/356 of query aligns to 8:246/332 of 2cwhA
- active site: H45 (= H46)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H46), A119 (≠ G120), A120 (≠ R121), L121 (≠ V122), H148 (= H151), T157 (= T160), P159 (= P162), F174 (≠ L178), D175 (= D179), L176 (≠ F180), A177 (= A181), H227 (= H233), K228 (= K234)
- binding pyrrole-2-carboxylate: H45 (= H46), R49 (≠ Q50), M142 (≠ R145), T157 (= T160), H183 (≠ A187), G184 (≠ N188)
Sites not aligning to the query:
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)
36% identity, 69% coverage: 9:252/356 of query aligns to 17:255/343 of Q4U331
Sites not aligning to the query:
- 309:315 binding in other chain
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
28% identity, 93% coverage: 8:339/356 of query aligns to 6:331/338 of 4fjuA
- binding glyoxylic acid: R48 (≠ Q50), H116 (= H118), S140 (= S144), D141 (≠ R145)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ H43), H44 (= H46), H116 (= H118), G118 (= G120), I120 (≠ V122), S140 (= S144), F147 (≠ H151), T156 (= T160), P158 (= P162), F173 (≠ L178), D174 (= D179), M175 (≠ F180), A176 (= A181), P223 (≠ H233), K224 (= K234), Y303 (≠ L311), G306 (= G314), D308 (≠ P316), Q309 (≠ E317)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
28% identity, 93% coverage: 8:339/356 of query aligns to 6:331/349 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 (≠ Q50) 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 (= S144) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ R145) 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 (≠ L256) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (= R264) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
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)
30% identity, 69% coverage: 8:252/356 of query aligns to 6:243/335 of 1s20G
Sites not aligning to the query:
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
25% identity, 97% coverage: 6:351/356 of query aligns to 6:360/361 of 3i0pA
- active site: H46 (= H46)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ H43), H46 (= H46), H119 (= H118), I122 (≠ R121), A123 (≠ V122), T159 (= T160), P161 (= P162), F176 (≠ L178), D177 (= D179), G178 (≠ F180), A179 (= A181), P184 (≠ A186), R187 (≠ K189), Y320 (≠ L311), A322 (≠ P313), G323 (= G314), K325 (≠ P316), E326 (= E317)
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
32% identity, 69% coverage: 8:251/356 of query aligns to 7:245/350 of 1z2iA
- active site: H45 (= H46)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ H43), H45 (= H46), H117 (= H118), F118 (≠ I119), G119 (= G120), P120 (≠ R121), A121 (≠ V122), T157 (= T160), P159 (= P162), D175 (= D179), M176 (≠ F180), A177 (= A181), P182 (≠ A186), F227 (≠ H233), K228 (= K234)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS16020 FitnessBrowser__azobra:AZOBR_RS16020
MGGPYAADHLVALLDAILQRSGSSPEEAAIVAANLVDSDATGHASHGVCQIAVYAKSLEL
GHLQPNRHARVVRDEAPFLVVDGEVGYGQVIAREATDLAIARAKAGGACVLALRNAHHIG
RVGAYGEQCIAAGLIGVFFVNVVSRPLAAPHGGGRPRLGTNPICIAVPATPGHPPFLLDF
ATSAVAANKCRVAAASGKEVADGLLIDERGAPTRDPGVMFRDPTGAILPFGGHKGYGLAL
ACEILAGALAGGLPALPENLRPGRVVNNVLAFLIDPARVSDAGSGGWQALTDAVLDHIQD
TPPVPGGDGVLVPGGPERRSRVLAAERGITLDPDTVRALHGIGGALGLDVPAFLGA
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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