SitesBLAST
Comparing AZOBR_RS04630 FitnessBrowser__azobra:AZOBR_RS04630 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)
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
66% identity, 94% coverage: 14:354/361 of query aligns to 7:347/350 of 1z2iA
- active site: H45 (= H52)
- binding nicotinamide-adenine-dinucleotide: V42 (= V49), H45 (= H52), H117 (= H124), F118 (= F125), G119 (= G126), P120 (= P127), A121 (= A128), T157 (= T164), P159 (= P166), D175 (= D182), M176 (= M183), A177 (= A184), P182 (= P189), F227 (= F234), K228 (= K235), M307 (= M314), R312 (= R319), E313 (= E320)
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
30% identity, 96% coverage: 8:354/361 of query aligns to 2:360/361 of 3i0pA
- active site: H46 (= H52)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ V49), H46 (= H52), H119 (= H124), I122 (≠ P127), A123 (= A128), T159 (= T164), P161 (= P166), F176 (= F181), D177 (= D182), G178 (≠ M183), A179 (= A184), P184 (= P189), R187 (= R192), Y320 (≠ M314), A322 (≠ P316), G323 (= G317), K325 (≠ R319), E326 (= E320)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
37% identity, 95% coverage: 10:352/361 of query aligns to 2:339/340 of 1vbiA
- active site: H44 (= H52)
- binding nicotinamide-adenine-dinucleotide: H44 (= H52), H115 (= H124), G117 (= G126), A119 (= A128), T155 (= T164), P157 (= P166), A171 (≠ F181), D172 (= D182), L173 (≠ M183), A174 (= A184), F301 (≠ M314), P303 (= P316), L306 (≠ R319), E307 (= E320)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
33% identity, 95% coverage: 10:351/361 of query aligns to 13:345/348 of 1v9nA
- active site: H55 (= H52)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H52), H127 (= H124), G129 (= G126), I130 (≠ P127), A131 (= A128), T167 (= T164), P169 (= P166), L183 (≠ F181), D184 (= D182), M185 (= M183), A186 (= A184), P191 (= P189), W308 (≠ M314), H310 (≠ P316), G311 (= G317), K313 (≠ R319), G314 (≠ E320)
Sites not aligning to the query:
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
30% identity, 91% coverage: 23:351/361 of query aligns to 15:337/344 of 2x06A
- active site: H44 (= H52)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ V49), H44 (= H52), H116 (= H124), F117 (= F125), G118 (= G126), I119 (≠ P127), A120 (= A128), T156 (= T164), P158 (= P166), D173 (= D182), M174 (= M183), A175 (= A184), L301 (≠ M314), I306 (≠ R319), E307 (= E320)
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)
31% identity, 95% coverage: 10:352/361 of query aligns to 6:348/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
31% identity, 95% coverage: 10:352/361 of query aligns to 4:346/359 of 2g8yA
- active site: H46 (= H52)
- binding nicotinamide-adenine-dinucleotide: H43 (≠ V49), H46 (= H52), G120 (= G126), I122 (≠ A128), T160 (= T164), P162 (= P166), L176 (= L180), L177 (≠ F181), D178 (= D182), Y179 (≠ M183), A180 (= A184), H232 (vs. gap), Y235 (≠ A237), N268 (≠ R271), G311 (= G317), E314 (= E320)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
30% identity, 89% coverage: 14:334/361 of query aligns to 6:323/349 of P77555
- S43 (= S51) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H52) 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 (≠ L56) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y60) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H124) mutation to A: Loss of dehydrogenase activity.
- S140 (= S148) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (= D149) 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 (= M262) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (= R271) 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)
30% identity, 89% coverage: 14:334/361 of query aligns to 6:323/338 of 4fjuA
- binding glyoxylic acid: R48 (≠ L56), H116 (= H124), S140 (= S148), D141 (= D149)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ V49), H44 (= H52), H116 (= H124), G118 (= G126), I120 (≠ A128), S140 (= S148), F147 (≠ H155), T156 (= T164), P158 (= P166), F173 (= F181), D174 (= D182), M175 (= M183), A176 (= A184), P223 (≠ E231), K224 (= K235), Y303 (≠ M314), G306 (= G317), D308 (≠ R319), Q309 (≠ E320)
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
30% identity, 94% coverage: 6:346/361 of query aligns to 2:335/337 of 2cwfB
- active site: H48 (= H52)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H52), H120 (= H124), A122 (≠ G126), A123 (≠ P127), L124 (≠ A128), T160 (= T164), P162 (= P166), F177 (= F181), D178 (= D182), L179 (≠ M183), A180 (= A184), H230 (≠ E231), K231 (= K235), R303 (= R306), G306 (= G317), R308 (= R319), R309 (≠ E320)
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)
30% identity, 94% coverage: 6:346/361 of query aligns to 8:341/343 of Q4U331
- HFAAL 126:130 (≠ HFGPA 124:128) binding in other chain
- DLA 184:186 (≠ DMA 182:184) binding in other chain
- H---K 236:237 (≠ EFGFK 231:235) binding
- 309:315 (vs. 306:320, 33% identical) binding in other chain
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)
28% identity, 88% coverage: 23:338/361 of query aligns to 15:325/335 of 1s20G
- active site: H44 (= H52)
- binding nicotinamide-adenine-dinucleotide: H44 (= H52), H116 (= H124), W147 (≠ H155), T156 (= T164), P158 (= P166), D172 (= D182), M173 (= M183), S174 (≠ A184), W224 (≠ F234), K225 (= K235), R301 (≠ M314), G304 (= G317), E306 (= E320)
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
30% identity, 92% coverage: 16:346/361 of query aligns to 9:332/332 of 2cwhA
- active site: H45 (= H52)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H52), A119 (≠ G126), A120 (≠ P127), L121 (≠ A128), H148 (= H155), T157 (= T164), P159 (= P166), F174 (= F181), D175 (= D182), L176 (≠ M183), A177 (= A184), H227 (≠ E231), K228 (= K235), R300 (= R306), G303 (= G317), R305 (= R319), R306 (≠ E320)
- binding pyrrole-2-carboxylate: H45 (= H52), R49 (≠ L56), M142 (≠ D149), T157 (= T164), H183 (≠ Y190), G184 (≠ N191)
Query Sequence
>AZOBR_RS04630 FitnessBrowser__azobra:AZOBR_RS04630
VTGPAQPTARYGADALDSFCRAVFLAAGADEATADAATRAMMHGSRLGVDSHGVRLLGHY
VATMTQGRVNPRPAPRILSEFGAVATLDADNAHGALGAYRAQEKAVELAGRFGIGAVAIR
NNSHFGPAGAFALAAAEAGCIGMAFCNSDSFMRLHDGAERFHGTNPIAIAVPVKDGDPWL
FDMATSAIPYNRVQLYRSLGIPLPEATASDPEGRDTTDPERAEMLAPLGGEFGFKGAGLA
GFVEILSAVLTGMKLSFEILPMPGPDLSTPRGMGAFVMAIRPEAFLPQENFQDNMARYLA
ALRGSRAVPGRTVMAPGDREWAEAERRRSLGIPIDQTTVDSFNQLAQAYGVPAPAPAASP
S
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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