SitesBLAST
Comparing AZOBR_RS31690 FitnessBrowser__azobra:AZOBR_RS31690 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)
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)
62% identity, 99% coverage: 1:325/327 of query aligns to 18:342/343 of Q4U331
- HFAAL 126:130 (≠ HFSAL 109:113) binding in other chain
- DLA 184:186 (≠ DQA 167:169) binding in other chain
- HK 236:237 (= HK 219:220) binding
- 309:315 (vs. 292:298, 71% identical) binding in other chain
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
62% identity, 99% coverage: 1:325/327 of query aligns to 12:336/337 of 2cwfB
- active site: H48 (= H37)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H37), H120 (= H109), A122 (≠ S111), A123 (= A112), L124 (= L113), T160 (= T149), P162 (= P151), F177 (= F166), D178 (= D167), L179 (≠ Q168), A180 (= A169), H230 (= H219), K231 (= K220), R303 (= R292), G306 (= G295), R308 (= R297), R309 (= R298)
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
62% identity, 99% coverage: 1:324/327 of query aligns to 9:332/332 of 2cwhA
- active site: H45 (= H37)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H37), A119 (≠ S111), A120 (= A112), L121 (= L113), H148 (≠ S140), T157 (= T149), P159 (= P151), F174 (= F166), D175 (= D167), L176 (≠ Q168), A177 (= A169), H227 (= H219), K228 (= K220), R300 (= R292), G303 (= G295), R305 (= R297), R306 (= R298)
- binding pyrrole-2-carboxylate: H45 (= H37), R49 (= R41), M142 (≠ F134), T157 (= T149), H183 (≠ N175), G184 (= G176)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
35% identity, 99% coverage: 1:323/327 of query aligns to 8:332/340 of 1vbiA
- active site: H44 (= H37)
- binding nicotinamide-adenine-dinucleotide: H44 (= H37), H115 (= H109), G117 (≠ S111), A119 (≠ L113), T155 (= T149), P157 (= P151), A171 (≠ F166), D172 (= D167), L173 (≠ Q168), A174 (= A169), F301 (vs. gap), P303 (= P294), L306 (≠ R297), E307 (≠ R298)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
32% identity, 99% coverage: 4:326/327 of query aligns to 11:334/344 of 2x06A
- active site: H44 (= H37)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ S34), H44 (= H37), H116 (= H109), F117 (= F110), G118 (≠ S111), I119 (≠ A112), A120 (≠ L113), T156 (= T149), P158 (= P151), D173 (= D167), M174 (≠ Q168), A175 (= A169), L301 (≠ R292), I306 (≠ R297), E307 (≠ R298)
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, 95% coverage: 1:312/327 of query aligns to 12:330/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
32% identity, 95% coverage: 1:312/327 of query aligns to 10:328/359 of 2g8yA
- active site: H46 (= H37)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ S34), H46 (= H37), G120 (≠ S111), I122 (≠ L113), T160 (= T149), P162 (= P151), L176 (≠ V165), L177 (≠ F166), D178 (= D167), Y179 (≠ Q168), A180 (= A169), H232 (= H219), Y235 (≠ G222), N268 (≠ P255), G311 (= G295), E314 (≠ R298)
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
35% identity, 82% coverage: 1:267/327 of query aligns to 8:271/338 of 4fjuA
- binding glyoxylic acid: R48 (= R41), H116 (= H109), S140 (= S133), D141 (≠ F134)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ S34), H44 (= H37), H116 (= H109), G118 (≠ S111), I120 (≠ L113), S140 (= S133), F147 (≠ S140), T156 (= T149), P158 (= P151), F173 (= F166), D174 (= D167), M175 (≠ Q168), A176 (= A169), P223 (≠ H219), K224 (= K220)
Sites not aligning to the query:
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
35% identity, 82% coverage: 1:267/327 of query aligns to 8:271/349 of P77555
- S43 (= S36) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H37) 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 (= R41) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y45) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H109) mutation to A: Loss of dehydrogenase activity.
- S140 (= S133) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (≠ F134) 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 (≠ S247) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ P255) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
28% identity, 99% coverage: 1:324/327 of query aligns to 19:340/348 of 1v9nA
- active site: H55 (= H37)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H37), H127 (= H109), G129 (≠ S111), I130 (≠ A112), A131 (≠ L113), T167 (= T149), P169 (= P151), L183 (≠ F166), D184 (= D167), M185 (≠ Q168), A186 (= A169), P191 (≠ A174), W308 (≠ R292), H310 (≠ P294), G311 (= G295), K313 (≠ R297), G314 (≠ R298)
Sites not aligning to the query:
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
30% identity, 98% coverage: 5:324/327 of query aligns to 9:339/350 of 1z2iA
- active site: H45 (= H37)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ S34), H45 (= H37), H117 (= H109), F118 (= F110), G119 (≠ S111), P120 (≠ A112), A121 (≠ L113), T157 (= T149), P159 (= P151), D175 (= D167), M176 (≠ Q168), A177 (= A169), P182 (≠ A174), F227 (vs. gap), K228 (= K220), M307 (≠ R292), R312 (= R297), E313 (≠ R298)
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, 99% coverage: 1:323/327 of query aligns to 8:332/335 of 1s20G
- active site: H44 (= H37)
- binding nicotinamide-adenine-dinucleotide: H44 (= H37), H116 (= H109), W147 (≠ S140), T156 (= T149), P158 (= P151), D172 (= D167), M173 (≠ Q168), S174 (≠ A169), W224 (≠ H219), K225 (= K220), R301 (= R292), G304 (= G295), E306 (≠ R297)
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
24% identity, 98% coverage: 4:324/327 of query aligns to 13:352/361 of 3i0pA
- active site: H46 (= H37)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ S34), H46 (= H37), H119 (= H109), I122 (≠ A112), A123 (≠ L113), T159 (= T149), P161 (= P151), F176 (= F166), D177 (= D167), G178 (≠ Q168), A179 (= A169), P184 (≠ A174), R187 (≠ D177), Y320 (vs. gap), A322 (≠ P294), G323 (= G295), K325 (≠ R297), E326 (≠ R298)
Query Sequence
>AZOBR_RS31690 FitnessBrowser__azobra:AZOBR_RS31690
LVALLERIFLRHGTSERVAAILAENCASCERDGSTSHGVFRIPGYVGSLKSGWVDGRAEP
TVEEAGPAFLRVDAANGFTQPAFLAARDRFLEMVRDNGVAVMAIRNSHHFSALWPDVEPF
AREGLVALSFVNSFACVVPSGGKAAVYGTNPMAFATPVAGGDPMVFDQAASSMANGDVRI
AAREGHAIPAGSGVDRDGKPTTDPKAVLDGGALLPFGGHKGGSIAFMIEVLAAALTGGKY
SREVDWSAHPGAETPCTGQLFIVIDPERGGTGAFADRVAGLIGDVKEAGQDRMPGERRYA
RRARTLRDGIPLTPARLAELRALAGDA
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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