SitesBLAST
Comparing 207060 DVU1609 dihydrodipicolinate reductase 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)
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
44% identity, 98% coverage: 5:259/259 of query aligns to 4:264/266 of 5temA
- active site: H155 (= H149), K159 (= K153)
- binding nicotinamide-adenine-dinucleotide: G8 (= G9), G11 (= G12), R12 (= R13), M13 (= M14), E34 (= E35), R35 (= R36), F75 (= F69), T76 (= T70), S80 (≠ A74), G98 (= G92), T100 (= T94), P123 (= P117), N124 (= N118), Y125 (≠ M119), F239 (= F233)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T94), P123 (= P117), H156 (= H150), K159 (= K153), S164 (= S158), G165 (= G159), T166 (= T160)
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
44% identity, 98% coverage: 5:259/259 of query aligns to 4:264/269 of 5tejB
- active site: H155 (= H149), K159 (= K153)
- binding 2,5 Furan Dicarboxylic Acid: T100 (= T94), H156 (= H150), K159 (= K153), S164 (= S158), G165 (= G159), T166 (= T160)
- binding nicotinamide-adenine-dinucleotide: G8 (= G9), G11 (= G12), R12 (= R13), M13 (= M14), E34 (= E35), R35 (= R36), F75 (= F69), T76 (= T70), S80 (≠ A74), G98 (= G92), T100 (= T94), P123 (= P117), N124 (= N118), Y125 (≠ M119), F239 (= F233)
5tejA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
44% identity, 98% coverage: 5:259/259 of query aligns to 4:264/269 of 5tejA
- active site: H155 (= H149), K159 (= K153)
- binding nicotinamide-adenine-dinucleotide: G8 (= G9), G11 (= G12), R12 (= R13), M13 (= M14), E34 (= E35), R35 (= R36), F75 (= F69), T76 (= T70), S80 (≠ A74), G98 (= G92), T100 (= T94), P123 (= P117)
4ywjA Crystal structure of 4-hydroxy-tetrahydrodipicolinate reductase (htpa reductase) from pseudomonas aeruginosa
43% identity, 98% coverage: 5:259/259 of query aligns to 4:265/268 of 4ywjA
- active site: H156 (= H149), K160 (= K153)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), R12 (= R13), M13 (= M14), D35 (≠ E35), R36 (= R36), F76 (= F69), T77 (= T70), V81 (≠ A74), G99 (= G92), T101 (= T94), A124 (≠ P117), N125 (= N118), F126 (≠ M119), R237 (= R230), F240 (= F233)
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
41% identity, 98% coverage: 5:259/259 of query aligns to 8:268/273 of P04036
- G12 (= G9) binding
- GRM 15:17 (= GRM 12:14) binding
- RM 16:17 (= RM 13:14) binding
- E38 (= E35) binding
- R39 (= R36) binding
- TR 80:81 (≠ TA 70:71) binding
- GTT 102:104 (= GTT 92:94) binding ; binding
- AANF 126:129 (≠ APNM 116:119) binding
- F129 (≠ M119) binding
- H159 (= H149) mutation H->A,Q: 135 to 200-fold reduction in catalytic activity.
- K163 (= K153) binding ; mutation K->A,C,Q: 625 to 830-fold reduction in catalytic activity.
- R240 (= R230) binding
- F243 (= F233) binding
1drvA Escherichia coli dhpr/acnadh complex (see paper)
41% identity, 98% coverage: 5:259/259 of query aligns to 5:265/270 of 1drvA
- active site: H156 (= H149), K160 (= K153)
- binding 3-acetylpyridine adenine dinucleotide: G9 (= G9), G12 (= G12), R13 (= R13), M14 (= M14), E35 (= E35), F76 (= F69), T77 (= T70), R78 (≠ A71), G81 (≠ A74), G99 (= G92), A124 (≠ P117), F126 (≠ M119), R237 (= R230)
1druA Escherichia coli dhpr/nadh complex (see paper)
41% identity, 98% coverage: 5:259/259 of query aligns to 5:265/270 of 1druA
- active site: H156 (= H149), K160 (= K153)
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), G12 (= G12), R13 (= R13), M14 (= M14), E35 (= E35), R36 (= R36), F76 (= F69), T77 (= T70), R78 (≠ A71), G81 (≠ A74), G99 (= G92), T100 (= T93), T101 (= T94), A124 (≠ P117), N125 (= N118), F126 (≠ M119), F240 (= F233)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
41% identity, 98% coverage: 5:259/259 of query aligns to 5:265/270 of 1arzA
1arzB Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
41% identity, 98% coverage: 5:259/259 of query aligns to 4:264/269 of 1arzB
- active site: H155 (= H149), K159 (= K153)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G9), G10 (= G11), G11 (= G12), R12 (= R13), M13 (= M14), E34 (= E35), F75 (= F69), T76 (= T70), R77 (≠ A71), G80 (≠ A74), H84 (≠ T78), G98 (= G92), T100 (= T94), A123 (≠ P117), N124 (= N118), F125 (≠ M119), F239 (= F233)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T94), H156 (= H150), K159 (= K153), S164 (= S158), G165 (= G159), T166 (= T160), F239 (= F233)
1drwA Escherichia coli dhpr/nhdh complex (see paper)
41% identity, 98% coverage: 5:259/259 of query aligns to 7:267/272 of 1drwA
- active site: H158 (= H149), K162 (= K153)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (= G9), G14 (= G12), R15 (= R13), M16 (= M14), E37 (= E35), R38 (= R36), F78 (= F69), T79 (= T70), R80 (≠ A71), G101 (= G92), T102 (= T93), T103 (= T94), A126 (≠ P117), N127 (= N118), F128 (≠ M119), F242 (= F233)
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
41% identity, 98% coverage: 5:259/259 of query aligns to 7:267/272 of 1dihA
- active site: H158 (= H149), K162 (= K153)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G9), G14 (= G12), R15 (= R13), M16 (= M14), R38 (= R36), F78 (= F69), T79 (= T70), R80 (≠ A71), G83 (≠ A74), G101 (= G92), T103 (= T94), N127 (= N118), F128 (≠ M119), R239 (= R230), F242 (= F233)
3ijpA Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
38% identity, 100% coverage: 2:259/259 of query aligns to 1:264/266 of 3ijpA
- active site: H155 (= H149), K159 (= K153)
- binding sodium ion: I21 (≠ V22), Q22 (= Q23), R24 (≠ E25), V27 (≠ L28)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), N10 (≠ G11), G11 (= G12), R12 (= R13), M13 (= M14), R35 (= R36), F75 (= F69), S76 (≠ T70), Q77 (≠ A71), A80 (= A74), G98 (= G92), T100 (= T94), G123 (≠ P117), N124 (= N118), M125 (= M119), F239 (= F233)
3ijpB Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
38% identity, 100% coverage: 2:259/259 of query aligns to 1:264/267 of 3ijpB
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)
34% identity, 97% coverage: 7:258/259 of query aligns to 5:211/216 of Q9X1K8
1vm6B Crystal structure of dihydrodipicolinate reductase (tm1520) from thermotoga maritima at 2.27 a resolution
34% identity, 97% coverage: 7:258/259 of query aligns to 10:216/218 of 1vm6B
- active site: H132 (= H149), K136 (= K153)
- binding nicotinamide-adenine-dinucleotide: G12 (= G9), S14 (≠ G11), G15 (= G12), R16 (= R13), M17 (= M14), D37 (≠ A44), V38 (≠ R45), F53 (= F69), S54 (≠ T70), S55 (≠ A71), E57 (= E73), A58 (= A74), G76 (= G92), T78 (= T94), Y101 (≠ P117), N102 (= N118), F103 (≠ M119), F192 (= F233)
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
31% identity, 94% coverage: 7:250/259 of query aligns to 5:233/245 of 1p9lA
- active site: H132 (= H149), K136 (= K153)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (= G9), G10 (= G12), K11 (≠ R13), V12 (≠ M14), D33 (≠ E35), A34 (≠ R36), F52 (= F69), T53 (= T70), V57 (≠ A74), G75 (= G92), T77 (= T94), P103 (= P117), N104 (= N118), F105 (≠ M119), F217 (= F233)
- binding pyridine-2,6-dicarboxylic acid: H133 (= H150), K136 (= K153), S141 (= S158), G142 (= G159), T143 (= T160), A192 (≠ G208)
1c3vA Dihydrodipicolinate reductase from mycobacterium tuberculosis complexed with NADPH and pdc (see paper)
31% identity, 94% coverage: 7:250/259 of query aligns to 5:233/245 of 1c3vA
- active site: H132 (= H149), K136 (= K153)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K9 (≠ G11), G10 (= G12), K11 (≠ R13), V12 (≠ M14), D33 (≠ E35), A34 (≠ R36), F52 (= F69), T53 (= T70), V57 (≠ A74), G75 (= G92), T77 (= T94), P103 (= P117), N104 (= N118), F217 (= F233)
- binding pyridine-2,6-dicarboxylic acid: T77 (= T94), N104 (= N118), K136 (= K153), S141 (= S158), G142 (= G159), T143 (= T160), A192 (≠ G208)
P9WP23 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
31% identity, 94% coverage: 7:250/259 of query aligns to 5:233/245 of P9WP23
- K9 (≠ G11) mutation to A: Increases the nucleotide specificity from 6:1 for the wild-type enzyme to 34:1, due to a 4-fold decrease in NADPH affinity while the affinity for NADH remains nearly unchanged.
- K11 (≠ R13) mutation to A: 2.8-fold increase in catalytic activity with NADH as substrate, while the affinity for NADH is essentially unaffected. 70-fold decrease in affinity for NADPH, causing the nucleotide specificity to increase from 6:1 for the wild-type enzyme to 187:1.
- KV 11:12 (≠ RM 13:14) binding ; binding
- D33 (≠ E35) binding
- GTT 75:77 (= GTT 92:94) binding ; binding
- APNF 102:105 (≠ APNM 116:119) binding ; binding
- K136 (= K153) binding ; binding
1yl5A Crystal structure of mycobacterium tuberculosis dihydrodipicolinate reductase (rv2773c) (crystal form a) (see paper)
31% identity, 94% coverage: 7:250/259 of query aligns to 7:235/247 of 1yl5A
5ugvA Dapb from mycobacterium tuberculosis (see paper)
31% identity, 94% coverage: 7:250/259 of query aligns to 6:234/245 of 5ugvA
Query Sequence
>207060 DVU1609 dihydrodipicolinate reductase
MSTPIIVMGAGGRMGSTICRLVQEEPQLCLAAVLERPDRASGVARDGCIAGSDPDVVFPQ
VPGGVIIDFTAPEASMATARAAARHGNAVVIGTTGFNEEQKAELAELARQIRLFWAPNMS
VGVNVLLKVLPELVRLLGEKYDLEMVELHHNRKKDSPSGTALRLAECLAEARDWNLPDVA
CYHREGIIGERPQKEIGVQTIRGGDVVGVHTVYCLGPGERIEVTHQAHSRETFAQGALRA
AAWLATQKPGKLYNMADIF
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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