SitesBLAST
Comparing WP_008807487.1 NCBI__GCF_000025465.1:WP_008807487.1 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)
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
92% identity, 100% coverage: 1:273/273 of query aligns to 1:273/273 of P04036
- G12 (= G12) binding NADP(+)
- GRM 15:17 (= GRM 15:17) binding NAD(+)
- RM 16:17 (= RM 16:17) binding NADP(+)
- E38 (= E38) binding NAD(+)
- R39 (= R39) binding NADP(+)
- TR 80:81 (= TR 80:81) binding NAD(+)
- GTT 102:104 (= GTT 102:104) binding NAD(+); binding NADP(+)
- AANF 126:129 (= AANF 126:129) binding NAD(+)
- F129 (= F129) 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 (= F243) binding NAD(+)
1drwA Escherichia coli dhpr/nhdh complex (see paper)
92% identity, 100% coverage: 2:273/273 of query aligns to 1:272/272 of 1drwA
- active site: H158 (= H159), K162 (= K163)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (= G12), G14 (= G15), R15 (= R16), M16 (= M17), E37 (= E38), R38 (= R39), F78 (= F79), T79 (= T80), R80 (= R81), G101 (= G102), T102 (= T103), T103 (= T104), A126 (= A127), N127 (= N128), F128 (= F129), F242 (= F243)
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
92% identity, 100% coverage: 2:273/273 of query aligns to 1:272/272 of 1dihA
- active site: H158 (= H159), K162 (= K163)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G12), G14 (= G15), R15 (= R16), M16 (= M17), R38 (= R39), F78 (= F79), T79 (= T80), R80 (= R81), G83 (= G84), G101 (= G102), T103 (= T104), N127 (= N128), F128 (= F129), R239 (= R240), F242 (= F243)
1drvA Escherichia coli dhpr/acnadh complex (see paper)
91% identity, 99% coverage: 4:273/273 of query aligns to 1:270/270 of 1drvA
- active site: H156 (= H159), K160 (= K163)
- binding 3-acetylpyridine adenine dinucleotide: G9 (= G12), G12 (= G15), R13 (= R16), M14 (= M17), E35 (= E38), F76 (= F79), T77 (= T80), R78 (= R81), G81 (= G84), G99 (= G102), A124 (= A127), F126 (= F129), R237 (= R240)
1druA Escherichia coli dhpr/nadh complex (see paper)
91% identity, 99% coverage: 4:273/273 of query aligns to 1:270/270 of 1druA
- active site: H156 (= H159), K160 (= K163)
- binding nicotinamide-adenine-dinucleotide: G9 (= G12), G12 (= G15), R13 (= R16), M14 (= M17), E35 (= E38), R36 (= R39), F76 (= F79), T77 (= T80), R78 (= R81), G81 (= G84), G99 (= G102), T100 (= T103), T101 (= T104), A124 (= A127), N125 (= N128), F126 (= F129), F240 (= F243)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
91% identity, 99% coverage: 4:273/273 of query aligns to 1:270/270 of 1arzA
1arzB Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
91% identity, 99% coverage: 5:273/273 of query aligns to 1:269/269 of 1arzB
- active site: H155 (= H159), K159 (= K163)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G12), G10 (= G14), G11 (= G15), R12 (= R16), M13 (= M17), E34 (= E38), F75 (= F79), T76 (= T80), R77 (= R81), G80 (= G84), H84 (= H88), G98 (= G102), T100 (= T104), A123 (= A127), N124 (= N128), F125 (= F129), F239 (= F243)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T104), H156 (= H160), K159 (= K163), S164 (= S168), G165 (= G169), T166 (= T170), F239 (= F243)
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
63% identity, 98% coverage: 6:273/273 of query aligns to 2:269/269 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 (= G12), G11 (= G15), R12 (= R16), M13 (= M17), E34 (= E38), R35 (= R39), F75 (= F79), T76 (= T80), S80 (≠ G84), G98 (= G102), T100 (= T104), P123 (≠ A127), N124 (= N128), Y125 (≠ F129), F239 (= F243)
5tejA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
63% identity, 98% coverage: 6:273/273 of query aligns to 2:269/269 of 5tejA
- active site: H155 (= H159), K159 (= K163)
- binding nicotinamide-adenine-dinucleotide: G8 (= G12), G11 (= G15), R12 (= R16), M13 (= M17), E34 (= E38), R35 (= R39), F75 (= F79), T76 (= T80), S80 (≠ G84), G98 (= G102), T100 (= T104), P123 (≠ A127)
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
63% identity, 97% coverage: 6:270/273 of query aligns to 2:266/266 of 5temA
- active site: H155 (= H159), K159 (= K163)
- binding nicotinamide-adenine-dinucleotide: G8 (= G12), G11 (= G15), R12 (= R16), M13 (= M17), E34 (= E38), R35 (= R39), F75 (= F79), T76 (= T80), S80 (≠ G84), G98 (= G102), T100 (= T104), P123 (≠ A127), N124 (= N128), Y125 (≠ F129), F239 (= F243)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T104), P123 (≠ A127), H156 (= H160), K159 (= K163), S164 (= S168), G165 (= G169), T166 (= T170)
4ywjA Crystal structure of 4-hydroxy-tetrahydrodipicolinate reductase (htpa reductase) from pseudomonas aeruginosa
64% identity, 97% coverage: 7:271/273 of query aligns to 3:268/268 of 4ywjA
- active site: H156 (= H159), K160 (= K163)
- binding nicotinamide-adenine-dinucleotide: G11 (= G15), R12 (= R16), M13 (= M17), D35 (≠ E38), R36 (= R39), F76 (= F79), T77 (= T80), V81 (≠ G84), G99 (= G102), T101 (= T104), A124 (= A127), N125 (= N128), F126 (= F129), R237 (= R240), F240 (= F243)
3ijpB Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
44% identity, 97% coverage: 6:271/273 of query aligns to 2:267/267 of 3ijpB
3ijpA Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
43% identity, 97% coverage: 6:270/273 of query aligns to 2:266/266 of 3ijpA
- active site: H155 (= H159), K159 (= K163)
- binding sodium ion: I21 (≠ A25), Q22 (≠ L26), R24 (≠ M28), V27 (= V31)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), N10 (≠ G14), G11 (= G15), R12 (= R16), M13 (= M17), R35 (= R39), F75 (= F79), S76 (≠ T80), Q77 (≠ R81), A80 (≠ G84), G98 (= G102), T100 (= T104), G123 (≠ A127), N124 (= N128), M125 (≠ F129), F239 (= F243)
1vm6B Crystal structure of dihydrodipicolinate reductase (tm1520) from thermotoga maritima at 2.27 a resolution
33% identity, 98% coverage: 2:268/273 of query aligns to 2:217/218 of 1vm6B
- active site: H132 (= H159), K136 (= K163)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S14 (≠ G14), G15 (= G15), R16 (= R16), M17 (= M17), D37 (≠ E38), V38 (≠ R39), F53 (= F79), S54 (≠ T80), S55 (≠ R81), E57 (= E83), A58 (≠ G84), G76 (= G102), T78 (= T104), Y101 (≠ A127), N102 (= N128), F103 (= F129), F192 (= F243)
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)
37% identity, 73% coverage: 71:268/273 of query aligns to 40:212/216 of Q9X1K8
Sites not aligning to the query:
5z2fA NADPH/pda bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
27% identity, 96% coverage: 6:268/273 of query aligns to 3:265/265 of 5z2fA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R11 (≠ G14), G12 (= G15), K13 (≠ R16), M14 (= M17), D35 (≠ E38), H36 (≠ R39), K37 (≠ E40), L76 (≠ F79), T77 (= T80), G99 (= G102), T100 (= T103), T101 (= T104), P126 (≠ A127), N127 (= N128), F128 (= F129)
- binding pyridine-2,6-dicarboxylic acid: P126 (≠ A127), H155 (= H159), H156 (= H160), K159 (= K163), S164 (= S168), G165 (= G169), T166 (= T170), A215 (≠ G218)
5z2eA Dipicolinate bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
27% identity, 96% coverage: 6:268/273 of query aligns to 3:265/265 of 5z2eA
5eesA Crystal structure of dapb in complex with NADP+ from corynebacterium glutamicum (see paper)
30% identity, 89% coverage: 6:248/273 of query aligns to 2:225/247 of 5eesA
- active site: H133 (= H159), K137 (= K163)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), G11 (= G15), R12 (= R16), V13 (≠ M17), G34 (≠ A61), V35 (= V62), F53 (= F79), T54 (= T80), G76 (= G102), T78 (= T104), P104 (≠ A127), N105 (= N128), F106 (= F129), F220 (= F243)
- binding sulfate ion: H134 (= H160), K137 (= K163), K137 (= K163), G143 (= G169), T144 (= T170)
5eerA Crystal structure of dapb from corynebacterium glutamicum (see paper)
30% identity, 89% coverage: 6:248/273 of query aligns to 2:225/247 of 5eerA
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
28% identity, 97% coverage: 6:271/273 of query aligns to 1:245/245 of 1p9lA
- active site: H132 (= H159), K136 (= K163)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (= G12), G10 (= G15), K11 (≠ R16), V12 (≠ M17), D33 (= D48), A34 (= A49), F52 (= F79), T53 (= T80), V57 (≠ G84), G75 (= G102), T77 (= T104), P103 (≠ A127), N104 (= N128), F105 (= F129), F217 (= F243)
- binding pyridine-2,6-dicarboxylic acid: H133 (= H160), K136 (= K163), S141 (= S168), G142 (= G169), T143 (= T170), A192 (≠ G218)
Query Sequence
>WP_008807487.1 NCBI__GCF_000025465.1:WP_008807487.1
MHDAQIRVAIAGAGGRMGRQLIQAALQMEGVALGAALEREGSSLVGSDAGELAGAGKAGV
AVQSSLTAVKDDFDVLIDFTRPEGTLNHLAFCREHGKGMVIGTTGFDDAGKQAIRDAAQE
IAIVFAANFSVGVNVLLKLLEKAAKVMGDYTDIEIIEAHHRHKVDAPSGTALAMGEAIAG
ALNKDLKECAVYSREGHTGERVPGTIGFATVRAGDIVGEHTAMFADIGERIEITHKASSR
MTFANGAVRSALWLKDKKNGLFDMRDVLDLNSL
Or try a new SitesBLAST search
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