SitesBLAST
Comparing WP_011803151.1 NCBI__GCF_000015505.1:WP_011803151.1 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 20 (the maximum) hits to proteins with known functional sites (download)
4ywjA Crystal structure of 4-hydroxy-tetrahydrodipicolinate reductase (htpa reductase) from pseudomonas aeruginosa
58% identity, 98% coverage: 7:271/271 of query aligns to 2:268/268 of 4ywjA
- active site: H156 (= H159), K160 (= K163)
- binding nicotinamide-adenine-dinucleotide: G11 (= G16), R12 (= R17), M13 (= M18), D35 (= D39), R36 (= R40), F76 (= F79), T77 (= T80), V81 (≠ G84), G99 (= G102), T101 (= T104), A124 (≠ P127), N125 (= N128), F126 (≠ M129), R237 (= R240), F240 (≠ Y243)
1drvA Escherichia coli dhpr/acnadh complex (see paper)
60% identity, 97% coverage: 8:271/271 of query aligns to 4:268/270 of 1drvA
- active site: H156 (= H159), K160 (= K163)
- binding 3-acetylpyridine adenine dinucleotide: G9 (= G13), G12 (= G16), R13 (= R17), M14 (= M18), E35 (≠ D39), F76 (= F79), T77 (= T80), R78 (= R81), G81 (= G84), G99 (= G102), A124 (≠ P127), F126 (≠ M129), R237 (= R240)
1druA Escherichia coli dhpr/nadh complex (see paper)
60% identity, 97% coverage: 8:271/271 of query aligns to 4:268/270 of 1druA
- active site: H156 (= H159), K160 (= K163)
- binding nicotinamide-adenine-dinucleotide: G9 (= G13), G12 (= G16), R13 (= R17), M14 (= M18), E35 (≠ D39), R36 (= R40), F76 (= F79), T77 (= T80), R78 (= R81), G81 (= G84), G99 (= G102), T100 (= T103), T101 (= T104), A124 (≠ P127), N125 (= N128), F126 (≠ M129), F240 (≠ Y243)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
60% identity, 97% coverage: 8:271/271 of query aligns to 4:268/270 of 1arzA
1arzB Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
60% identity, 97% coverage: 8:271/271 of query aligns to 3:267/269 of 1arzB
- active site: H155 (= H159), K159 (= K163)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G13), G10 (≠ S15), G11 (= G16), R12 (= R17), M13 (= M18), E34 (≠ D39), F75 (= F79), T76 (= T80), R77 (= R81), G80 (= G84), H84 (= H88), G98 (= G102), T100 (= T104), A123 (≠ P127), N124 (= N128), F125 (≠ M129), F239 (≠ Y243)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T104), H156 (= H160), K159 (= K163), S164 (= S168), G165 (= G169), T166 (= T170), F239 (≠ Y243)
1drwA Escherichia coli dhpr/nhdh complex (see paper)
60% identity, 97% coverage: 8:271/271 of query aligns to 6:270/272 of 1drwA
- active site: H158 (= H159), K162 (= K163)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (= G13), G14 (= G16), R15 (= R17), M16 (= M18), E37 (≠ D39), R38 (= R40), F78 (= F79), T79 (= T80), R80 (= R81), G101 (= G102), T102 (= T103), T103 (= T104), A126 (≠ P127), N127 (= N128), F128 (≠ M129), F242 (≠ Y243)
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
60% identity, 97% coverage: 8:271/271 of query aligns to 6:270/272 of 1dihA
- active site: H158 (= H159), K162 (= K163)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G13), G14 (= G16), R15 (= R17), M16 (= M18), R38 (= R40), F78 (= F79), T79 (= T80), R80 (= R81), G83 (= G84), G101 (= G102), T103 (= T104), N127 (= N128), F128 (≠ M129), R239 (= R240), F242 (≠ Y243)
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
60% identity, 97% coverage: 8:271/271 of query aligns to 7:271/273 of P04036
- G12 (= G13) binding NADP(+)
- GRM 15:17 (= GRM 16:18) binding NAD(+)
- RM 16:17 (= RM 17:18) binding NADP(+)
- E38 (≠ D39) binding NAD(+)
- R39 (= R40) binding NADP(+)
- TR 80:81 (= TR 80:81) binding NAD(+)
- GTT 102:104 (= GTT 102:104) binding NAD(+); binding NADP(+)
- AANF 126:129 (≠ APNM 126:129) binding NAD(+)
- F129 (≠ M129) binding NADP(+)
- H159 (= H159) mutation H->A,Q: 135 to 200-fold reduction in catalytic activity.
- K163 (= K163) binding NAD(+); mutation K->A,C,Q: 625 to 830-fold reduction in catalytic activity.
- R240 (= R240) binding NADP(+)
- F243 (≠ Y243) binding NAD(+)
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
51% identity, 97% coverage: 8:271/271 of query aligns to 3:267/269 of 5tejB
- active site: H155 (= H159), K159 (= K163)
- binding 2,5 Furan Dicarboxylic Acid: T100 (= T104), H156 (= H160), K159 (= K163), S164 (= S168), G165 (= G169), T166 (= T170)
- binding nicotinamide-adenine-dinucleotide: G8 (= G13), G11 (= G16), R12 (= R17), M13 (= M18), E34 (≠ D39), R35 (= R40), F75 (= F79), T76 (= T80), S80 (≠ G84), G98 (= G102), T100 (= T104), P123 (= P127), N124 (= N128), Y125 (≠ M129), F239 (≠ Y243)
5tejA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
51% identity, 97% coverage: 8:271/271 of query aligns to 3:267/269 of 5tejA
- active site: H155 (= H159), K159 (= K163)
- binding nicotinamide-adenine-dinucleotide: G8 (= G13), G11 (= G16), R12 (= R17), M13 (= M18), E34 (≠ D39), R35 (= R40), F75 (= F79), T76 (= T80), S80 (≠ G84), G98 (= G102), T100 (= T104), P123 (= P127)
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
51% identity, 97% coverage: 8:270/271 of query aligns to 3:266/266 of 5temA
- active site: H155 (= H159), K159 (= K163)
- binding nicotinamide-adenine-dinucleotide: G8 (= G13), G11 (= G16), R12 (= R17), M13 (= M18), E34 (≠ D39), R35 (= R40), F75 (= F79), T76 (= T80), S80 (≠ G84), G98 (= G102), T100 (= T104), P123 (= P127), N124 (= N128), Y125 (≠ M129), F239 (≠ Y243)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T104), P123 (= P127), H156 (= H160), K159 (= K163), S164 (= S168), G165 (= G169), T166 (= T170)
3ijpB Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
42% identity, 97% coverage: 8:271/271 of query aligns to 3:267/267 of 3ijpB
3ijpA Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
42% identity, 97% coverage: 8:270/271 of query aligns to 3:266/266 of 3ijpA
- active site: H155 (= H159), K159 (= K163)
- binding sodium ion: I21 (≠ V26), Q22 (≠ N27), R24 (≠ S29), V27 (≠ C32)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G13), N10 (≠ S15), G11 (= G16), R12 (= R17), M13 (= M18), R35 (= R40), F75 (= F79), S76 (≠ T80), Q77 (≠ R81), A80 (≠ G84), G98 (= G102), T100 (= T104), G123 (≠ P127), N124 (= N128), M125 (= M129), F239 (≠ Y243)
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)
31% identity, 80% coverage: 51:268/271 of query aligns to 18:212/216 of Q9X1K8
Sites not aligning to the query:
1vm6B Crystal structure of dihydrodipicolinate reductase (tm1520) from thermotoga maritima at 2.27 a resolution
31% identity, 80% coverage: 51:268/271 of query aligns to 23:217/218 of 1vm6B
- active site: H132 (= H159), K136 (= K163)
- binding nicotinamide-adenine-dinucleotide: D37 (= D65), V38 (≠ L66), F53 (= F79), S54 (≠ T80), S55 (≠ R81), E57 (= E83), A58 (≠ G84), G76 (= G102), T78 (= T104), Y101 (≠ P127), N102 (= N128), F103 (≠ M129), F192 (≠ Y243)
Sites not aligning to the query:
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
31% identity, 90% coverage: 8:252/271 of query aligns to 2:226/245 of 1p9lA
- active site: H132 (= H159), K136 (= K163)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (= G13), G10 (= G16), K11 (≠ R17), V12 (≠ M18), D33 (= D39), A34 (≠ R40), F52 (= F79), T53 (= T80), V57 (≠ G84), G75 (= G102), T77 (= T104), P103 (= P127), N104 (= N128), F105 (≠ M129), F217 (≠ Y243)
- binding pyridine-2,6-dicarboxylic acid: H133 (= H160), K136 (= K163), S141 (= S168), G142 (= G169), T143 (= T170), A192 (≠ G218)
1c3vA Dihydrodipicolinate reductase from mycobacterium tuberculosis complexed with NADPH and pdc (see paper)
31% identity, 90% coverage: 8:252/271 of query aligns to 2:226/245 of 1c3vA
- active site: H132 (= H159), K136 (= K163)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K9 (≠ S15), G10 (= G16), K11 (≠ R17), V12 (≠ M18), D33 (= D39), A34 (≠ R40), F52 (= F79), T53 (= T80), V57 (≠ G84), G75 (= G102), T77 (= T104), P103 (= P127), N104 (= N128), F217 (≠ Y243)
- binding pyridine-2,6-dicarboxylic acid: T77 (= T104), N104 (= N128), K136 (= K163), S141 (= S168), G142 (= G169), T143 (= T170), A192 (≠ G218)
5ugvA Dapb from mycobacterium tuberculosis (see paper)
31% identity, 90% coverage: 8:252/271 of query aligns to 3:227/245 of 5ugvA
5tjzA Structure of 4-hydroxytetrahydrodipicolinate reductase from mycobacterium tuberculosis with NADPH and 2,6 pyridine dicarboxylic acid (see paper)
31% identity, 90% coverage: 8:252/271 of query aligns to 3:227/245 of 5tjzA
- active site: H133 (= H159), K137 (= K163)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G13), G11 (= G16), K12 (≠ R17), V13 (≠ M18), D34 (= D39), A35 (≠ R40), F53 (= F79), T54 (= T80), G76 (= G102), T77 (= T103), T78 (= T104), P104 (= P127), N105 (= N128), F106 (≠ M129), F218 (≠ Y243)
- binding pyridine-2,6-dicarboxylic acid: T78 (= T104), P104 (= P127), H134 (= H160), K137 (= K163), S142 (= S168), G143 (= G169), T144 (= T170), A193 (≠ G218)
1yl5A Crystal structure of mycobacterium tuberculosis dihydrodipicolinate reductase (rv2773c) (crystal form a) (see paper)
31% identity, 90% coverage: 8:252/271 of query aligns to 4:228/247 of 1yl5A
Query Sequence
>WP_011803151.1 NCBI__GCF_000015505.1:WP_011803151.1
MAQDRPHRIAVAGASGRMGHMLIDAVNASTDCLLTGALDRPASAAIGTDASAFAGRASGV
LIHSDLREGLKNSRVLIDFTRPEGTLAHLAVCRELGIKLVIGTTGFSDAQKAEIAAAAKD
IAIVMAPNMSVGVNVTLKLLEMAARALSTGYDIEIIEAHHRHKVDAPSGTALKMGEVIAG
ALGRDLKDCAVYAREGVTGERDPSSIGFATIRGGDIVGDHTVLFLGDGERIEISHKSSSR
ATYAQGSLRAARFLDSQASGLFDMFDVLNLK
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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