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Comparing WP_083492033.1 NCBI__GCF_001431535.1:WP_083492033.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
37% identity, 97% coverage: 6:238/240 of query aligns to 2:264/269 of 5tejB
- active site: H155 (= H150), K159 (= K154)
- binding 2,5 Furan Dicarboxylic Acid: T100 (= T96), H156 (= H151), K159 (= K154), S164 (= S159), G165 (= G160), T166 (= T161)
- binding nicotinamide-adenine-dinucleotide: G8 (= G12), G11 (= G15), R12 (= R16), M13 (= M17), E34 (vs. gap), R35 (vs. gap), F75 (= F71), T76 (≠ S72), S80 (≠ G76), G98 (= G94), T100 (= T96), P123 (≠ S119), N124 (= N120), Y125 (≠ F121), F239 (= F213)
5tejA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
37% identity, 97% coverage: 6:238/240 of query aligns to 2:264/269 of 5tejA
- active site: H155 (= H150), K159 (= K154)
- binding nicotinamide-adenine-dinucleotide: G8 (= G12), G11 (= G15), R12 (= R16), M13 (= M17), E34 (vs. gap), R35 (vs. gap), F75 (= F71), T76 (≠ S72), S80 (≠ G76), G98 (= G94), T100 (= T96), P123 (≠ S119)
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
37% identity, 97% coverage: 6:238/240 of query aligns to 2:264/266 of 5temA
- active site: H155 (= H150), K159 (= K154)
- binding nicotinamide-adenine-dinucleotide: G8 (= G12), G11 (= G15), R12 (= R16), M13 (= M17), E34 (vs. gap), R35 (vs. gap), F75 (= F71), T76 (≠ S72), S80 (≠ G76), G98 (= G94), T100 (= T96), P123 (≠ S119), N124 (= N120), Y125 (≠ F121), F239 (= F213)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T96), P123 (≠ S119), H156 (= H151), K159 (= K154), S164 (= S159), G165 (= G160), T166 (= T161)
Q9X1K8 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
39% identity, 96% coverage: 10:240/240 of query aligns to 5:214/216 of Q9X1K8
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
38% identity, 100% coverage: 1:239/240 of query aligns to 1:269/273 of P04036
- G12 (= G12) binding
- GRM 15:17 (= GRM 15:17) binding
- RM 16:17 (= RM 16:17) binding
- E38 (≠ Q45) binding
- R39 (= R46) binding
- TR 80:81 (≠ SL 72:73) binding
- GTT 102:104 (= GTT 94:96) binding ; binding
- AANF 126:129 (≠ ASNF 118:121) binding
- F129 (= F121) binding
- H159 (= H150) mutation H->A,Q: 135 to 200-fold reduction in catalytic activity.
- K163 (= K154) binding ; mutation K->A,C,Q: 625 to 830-fold reduction in catalytic activity.
- R240 (= R210) binding
- F243 (= F213) binding
1vm6B Crystal structure of dihydrodipicolinate reductase (tm1520) from thermotoga maritima at 2.27 a resolution
38% identity, 95% coverage: 10:238/240 of query aligns to 10:217/218 of 1vm6B
- active site: H132 (= H150), K136 (= K154)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S14 (= S14), G15 (= G15), R16 (= R16), M17 (= M17), D37 (vs. gap), V38 (= V48), F53 (= F71), S54 (= S72), S55 (≠ L73), E57 (= E75), A58 (≠ G76), G76 (= G94), T78 (= T96), Y101 (≠ S119), N102 (= N120), F103 (= F121), F192 (= F213)
1drvA Escherichia coli dhpr/acnadh complex (see paper)
38% identity, 98% coverage: 6:239/240 of query aligns to 3:266/270 of 1drvA
- active site: H156 (= H150), K160 (= K154)
- binding 3-acetylpyridine adenine dinucleotide: G9 (= G12), G12 (= G15), R13 (= R16), M14 (= M17), E35 (≠ Q45), F76 (= F71), T77 (≠ S72), R78 (≠ L73), G81 (= G76), G99 (= G94), A124 (≠ S119), F126 (= F121), R237 (= R210)
1druA Escherichia coli dhpr/nadh complex (see paper)
38% identity, 98% coverage: 6:239/240 of query aligns to 3:266/270 of 1druA
- active site: H156 (= H150), K160 (= K154)
- binding nicotinamide-adenine-dinucleotide: G9 (= G12), G12 (= G15), R13 (= R16), M14 (= M17), E35 (≠ Q45), R36 (= R46), F76 (= F71), T77 (≠ S72), R78 (≠ L73), G81 (= G76), G99 (= G94), T100 (= T95), T101 (= T96), A124 (≠ S119), N125 (= N120), F126 (= F121), F240 (= F213)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
38% identity, 98% coverage: 6:239/240 of query aligns to 3:266/270 of 1arzA
1arzB Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
38% identity, 98% coverage: 6:239/240 of query aligns to 2:265/269 of 1arzB
- active site: H155 (= H150), K159 (= K154)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G12), G10 (≠ S14), G11 (= G15), R12 (= R16), M13 (= M17), E34 (≠ Q45), F75 (= F71), T76 (≠ S72), R77 (≠ L73), G80 (= G76), H84 (≠ I80), G98 (= G94), T100 (= T96), A123 (≠ S119), N124 (= N120), F125 (= F121), F239 (= F213)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T96), H156 (= H151), K159 (= K154), S164 (= S159), G165 (= G160), T166 (= T161), F239 (= F213)
1drwA Escherichia coli dhpr/nhdh complex (see paper)
38% identity, 98% coverage: 6:239/240 of query aligns to 5:268/272 of 1drwA
- active site: H158 (= H150), K162 (= K154)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (= G12), G14 (= G15), R15 (= R16), M16 (= M17), E37 (≠ Q45), R38 (= R46), F78 (= F71), T79 (≠ S72), R80 (≠ L73), G101 (= G94), T102 (= T95), T103 (= T96), A126 (≠ S119), N127 (= N120), F128 (= F121), F242 (= F213)
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
38% identity, 98% coverage: 6:239/240 of query aligns to 5:268/272 of 1dihA
- active site: H158 (= H150), K162 (= K154)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G12), G14 (= G15), R15 (= R16), M16 (= M17), R38 (= R46), F78 (= F71), T79 (≠ S72), R80 (≠ L73), G83 (= G76), G101 (= G94), T103 (= T96), N127 (= N120), F128 (= F121), R239 (= R210), F242 (= F213)
4ywjA Crystal structure of 4-hydroxy-tetrahydrodipicolinate reductase (htpa reductase) from pseudomonas aeruginosa
37% identity, 97% coverage: 7:238/240 of query aligns to 3:265/268 of 4ywjA
- active site: H156 (= H150), K160 (= K154)
- binding nicotinamide-adenine-dinucleotide: G11 (= G15), R12 (= R16), M13 (= M17), D35 (≠ E27), R36 (≠ H28), F76 (= F71), T77 (≠ S72), V81 (≠ G76), G99 (= G94), T101 (= T96), A124 (≠ S119), N125 (= N120), F126 (= F121), R237 (= R210), F240 (= F213)
3ijpB Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
33% identity, 98% coverage: 5:238/240 of query aligns to 1:264/267 of 3ijpB
3ijpA Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
33% identity, 98% coverage: 5:238/240 of query aligns to 1:264/266 of 3ijpA
- active site: H155 (= H150), K159 (= K154)
- binding sodium ion: I21 (≠ A25), Q22 (≠ A26), R24 (≠ H28), V27 (≠ T31)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), N10 (≠ S14), G11 (= G15), R12 (= R16), M13 (= M17), R35 (≠ Y38), F75 (= F71), S76 (= S72), Q77 (≠ L73), A80 (≠ G76), G98 (= G94), T100 (= T96), G123 (≠ S119), N124 (= N120), M125 (≠ F121), F239 (= F213)
5wolA Crystal structure of dihydrodipicolinate reductase dapb from coxiella burnetii
26% identity, 97% coverage: 6:238/240 of query aligns to 2:230/230 of 5wolA
- active site: H133 (= H150), K137 (= K154)
- binding pyridine-2-carboxylic acid: P104 (≠ S119), T144 (= T161), K147 (≠ T164)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N7 (≠ H11), G11 (= G15), K12 (≠ R16), M13 (= M17), G34 (= G40), R35 (= R41), F54 (= F71), T55 (≠ S72), T56 (≠ L73), S59 (≠ G76), G77 (= G94), T78 (= T95), T79 (= T96), P104 (≠ S119), N105 (= N120), F106 (= F121)
5z2fA NADPH/pda bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
26% identity, 97% coverage: 6:238/240 of query aligns to 3:265/265 of 5z2fA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R11 (≠ S14), G12 (= G15), K13 (≠ R16), M14 (= M17), D35 (vs. gap), H36 (vs. gap), K37 (vs. gap), L76 (≠ F71), T77 (≠ S72), G99 (= G94), T100 (= T95), T101 (= T96), P126 (≠ S119), N127 (= N120), F128 (= F121)
- binding pyridine-2,6-dicarboxylic acid: P126 (≠ S119), H155 (= H150), H156 (= H151), K159 (= K154), S164 (= S159), G165 (= G160), T166 (= T161), A215 (≠ G188)
5z2eA Dipicolinate bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
26% identity, 97% coverage: 6:238/240 of query aligns to 3:265/265 of 5z2eA
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
27% identity, 94% coverage: 6:230/240 of query aligns to 1:233/245 of 1p9lA
- active site: H132 (= H150), K136 (= K154)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (= G12), G10 (= G15), K11 (≠ R16), V12 (≠ M17), D33 (≠ T39), A34 (≠ G40), F52 (= F71), T53 (≠ S72), V57 (≠ G76), G75 (= G94), T77 (= T96), P103 (≠ S119), N104 (= N120), F105 (= F121), F217 (= F213)
- binding pyridine-2,6-dicarboxylic acid: H133 (= H151), K136 (= K154), S141 (= S159), G142 (= G160), T143 (= T161), A192 (vs. gap)
1c3vA Dihydrodipicolinate reductase from mycobacterium tuberculosis complexed with NADPH and pdc (see paper)
27% identity, 94% coverage: 6:230/240 of query aligns to 1:233/245 of 1c3vA
- active site: H132 (= H150), K136 (= K154)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K9 (≠ S14), G10 (= G15), K11 (≠ R16), V12 (≠ M17), D33 (≠ T39), A34 (≠ G40), F52 (= F71), T53 (≠ S72), V57 (≠ G76), G75 (= G94), T77 (= T96), P103 (≠ S119), N104 (= N120), F217 (= F213)
- binding pyridine-2,6-dicarboxylic acid: T77 (= T96), N104 (= N120), K136 (= K154), S141 (= S159), G142 (= G160), T143 (= T161), A192 (vs. gap)
Query Sequence
>WP_083492033.1 NCBI__GCF_001431535.1:WP_083492033.1
MNQTPLRLLIHGASGRMGQALLRLAAEHTDTLNVVGAYTGRAPAQRVVDGIPHFAAKELH
GAPPFDVAIDFSLPEGFDAILALCVERGAGLVSGTTGISQAQREALDAAAKAIPLVWASN
FSLGVAVLDELVERAAQALAGWDCDIVESHHTRKLDAPSGTALTLGAAAGRGGATPQYAS
LRAGDIVGEHLVQFTGLGERIELVHRATNRDIFARGALFAARQLGQRAPGSYRVRDLLNG
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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