SitesBLAST
Comparing WP_015738385.1 NCBI__GCF_000024605.1:WP_015738385.1 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)
5z2fA NADPH/pda bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
47% identity, 99% coverage: 1:263/265 of query aligns to 2:265/265 of 5z2fA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R11 (≠ A10), G12 (= G11), K13 (≠ R12), M14 (= M13), D35 (= D34), H36 (≠ G39), K37 (≠ Q40), L76 (≠ F74), T77 (= T75), G99 (= G97), T100 (= T98), T101 (= T99), P126 (= P124), N127 (= N125), F128 (= F126)
- binding pyridine-2,6-dicarboxylic acid: P126 (= P124), H155 (= H153), H156 (= H154), K159 (= K157), S164 (= S162), G165 (= G163), T166 (= T164), A215 (= A213)
5z2eA Dipicolinate bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
47% identity, 99% coverage: 1:263/265 of query aligns to 2:265/265 of 5z2eA
5wolA Crystal structure of dihydrodipicolinate reductase dapb from coxiella burnetii
46% identity, 99% coverage: 2:263/265 of query aligns to 2:230/230 of 5wolA
- active site: H133 (= H153), K137 (= K157)
- binding pyridine-2-carboxylic acid: P104 (= P124), T144 (= T164), K147 (≠ Q167)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N7 (≠ T7), G11 (= G11), K12 (≠ R12), M13 (= M13), G34 (= G39), R35 (≠ Q40), F54 (= F74), T55 (= T75), T56 (= T76), S59 (≠ A79), G77 (= G97), T78 (= T98), T79 (= T99), P104 (= P124), N105 (= N125), F106 (= F126)
1yl5A Crystal structure of mycobacterium tuberculosis dihydrodipicolinate reductase (rv2773c) (crystal form a) (see paper)
42% identity, 99% coverage: 1:263/265 of query aligns to 2:244/247 of 1yl5A
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
41% identity, 99% coverage: 2:263/265 of query aligns to 1:242/245 of 1p9lA
- active site: H132 (= H153), K136 (= K157)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (= G8), G10 (= G11), K11 (≠ R12), V12 (≠ M13), D33 (= D34), A34 (≠ P35), F52 (= F74), T53 (= T75), V57 (≠ A79), G75 (= G97), T77 (= T99), P103 (= P124), N104 (= N125), F105 (= F126), F217 (= F238)
- binding pyridine-2,6-dicarboxylic acid: H133 (= H154), K136 (= K157), S141 (= S162), G142 (= G163), T143 (= T164), A192 (= A213)
1c3vA Dihydrodipicolinate reductase from mycobacterium tuberculosis complexed with NADPH and pdc (see paper)
41% identity, 99% coverage: 2:263/265 of query aligns to 1:242/245 of 1c3vA
- active site: H132 (= H153), K136 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K9 (≠ A10), G10 (= G11), K11 (≠ R12), V12 (≠ M13), D33 (= D34), A34 (≠ P35), F52 (= F74), T53 (= T75), V57 (≠ A79), G75 (= G97), T77 (= T99), P103 (= P124), N104 (= N125), F217 (= F238)
- binding pyridine-2,6-dicarboxylic acid: T77 (= T99), N104 (= N125), K136 (= K157), S141 (= S162), G142 (= G163), T143 (= T164), A192 (= A213)
5ugvA Dapb from mycobacterium tuberculosis (see paper)
41% identity, 99% coverage: 2:263/265 of query aligns to 2:243/245 of 5ugvA
5tjzA Structure of 4-hydroxytetrahydrodipicolinate reductase from mycobacterium tuberculosis with NADPH and 2,6 pyridine dicarboxylic acid (see paper)
41% identity, 99% coverage: 2:263/265 of query aligns to 2:243/245 of 5tjzA
- active site: H133 (= H153), K137 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G8), G11 (= G11), K12 (≠ R12), V13 (≠ M13), D34 (= D34), A35 (≠ P35), F53 (= F74), T54 (= T75), G76 (= G97), T77 (= T98), T78 (= T99), P104 (= P124), N105 (= N125), F106 (= F126), F218 (= F238)
- binding pyridine-2,6-dicarboxylic acid: T78 (= T99), P104 (= P124), H134 (= H154), K137 (= K157), S142 (= S162), G143 (= G163), T144 (= T164), A193 (= A213)
P9WP23 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
41% identity, 99% coverage: 2:263/265 of query aligns to 1:242/245 of P9WP23
- K9 (≠ A10) 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 (≠ R12) 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 12:13) binding ; binding
- D33 (= D34) binding
- GTT 75:77 (= GTT 97:99) binding ; binding
- APNF 102:105 (= APNF 123:126) binding ; binding
- K136 (= K157) binding ; binding
5eesA Crystal structure of dapb in complex with NADP+ from corynebacterium glutamicum (see paper)
42% identity, 99% coverage: 2:263/265 of query aligns to 2:245/247 of 5eesA
- active site: H133 (= H153), K137 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G8), G11 (= G11), R12 (= R12), V13 (≠ M13), G34 (= G49), V35 (= V55), F53 (= F74), T54 (= T75), G76 (= G97), T78 (= T99), P104 (= P124), N105 (= N125), F106 (= F126), F220 (= F238)
- binding sulfate ion: H134 (= H154), K137 (= K157), K137 (= K157), G143 (= G163), T144 (= T164)
5eerA Crystal structure of dapb from corynebacterium glutamicum (see paper)
42% identity, 99% coverage: 2:263/265 of query aligns to 2:245/247 of 5eerA
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
34% identity, 96% coverage: 1:254/265 of query aligns to 1:252/269 of 5tejB
- active site: H155 (= H153), K159 (= K157)
- binding 2,5 Furan Dicarboxylic Acid: T100 (= T99), H156 (= H154), K159 (= K157), S164 (= S162), G165 (= G163), T166 (= T164)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G11 (= G11), R12 (= R12), M13 (= M13), E34 (≠ V33), R35 (≠ D34), F75 (= F74), T76 (= T75), S80 (≠ A79), G98 (= G97), T100 (= T99), P123 (= P124), N124 (= N125), Y125 (≠ F126), F239 (= F238)
5tejA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
34% identity, 96% coverage: 1:254/265 of query aligns to 1:252/269 of 5tejA
- active site: H155 (= H153), K159 (= K157)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G11 (= G11), R12 (= R12), M13 (= M13), E34 (≠ V33), R35 (≠ D34), F75 (= F74), T76 (= T75), S80 (≠ A79), G98 (= G97), T100 (= T99), P123 (= P124)
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
34% identity, 96% coverage: 1:254/265 of query aligns to 1:252/266 of 5temA
- active site: H155 (= H153), K159 (= K157)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G11 (= G11), R12 (= R12), M13 (= M13), E34 (≠ V33), R35 (≠ D34), F75 (= F74), T76 (= T75), S80 (≠ A79), G98 (= G97), T100 (= T99), P123 (= P124), N124 (= N125), Y125 (≠ F126), F239 (= F238)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T99), P123 (= P124), H156 (= H154), K159 (= K157), S164 (= S162), G165 (= G163), T166 (= T164)
4ywjA Crystal structure of 4-hydroxy-tetrahydrodipicolinate reductase (htpa reductase) from pseudomonas aeruginosa
36% identity, 98% coverage: 1:259/265 of query aligns to 1:258/268 of 4ywjA
- active site: H156 (= H153), K160 (= K157)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), R12 (= R12), M13 (= M13), D35 (= D34), R36 (vs. gap), F76 (= F74), T77 (= T75), V81 (≠ A79), G99 (= G97), T101 (= T99), A124 (≠ P124), N125 (= N125), F126 (= F126), R237 (= R235), F240 (= F238)
1drvA Escherichia coli dhpr/acnadh complex (see paper)
32% identity, 97% coverage: 2:259/265 of query aligns to 3:258/270 of 1drvA
- active site: H156 (= H153), K160 (= K157)
- binding 3-acetylpyridine adenine dinucleotide: G9 (= G8), G12 (= G11), R13 (= R12), M14 (= M13), E35 (≠ D34), F76 (= F74), T77 (= T75), R78 (≠ T76), G81 (≠ A79), G99 (= G97), A124 (≠ P124), F126 (= F126), R237 (= R235)
1druA Escherichia coli dhpr/nadh complex (see paper)
32% identity, 97% coverage: 2:259/265 of query aligns to 3:258/270 of 1druA
- active site: H156 (= H153), K160 (= K157)
- binding nicotinamide-adenine-dinucleotide: G9 (= G8), G12 (= G11), R13 (= R12), M14 (= M13), E35 (≠ D34), R36 (vs. gap), F76 (= F74), T77 (= T75), R78 (≠ T76), G81 (≠ A79), G99 (= G97), T100 (= T98), T101 (= T99), A124 (≠ P124), N125 (= N125), F126 (= F126), F240 (= F238)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
32% identity, 97% coverage: 2:259/265 of query aligns to 3:258/270 of 1arzA
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
32% identity, 97% coverage: 2:259/265 of query aligns to 6:261/273 of P04036
- G12 (= G8) binding
- GRM 15:17 (= GRM 11:13) binding
- RM 16:17 (= RM 12:13) binding
- E38 (≠ D34) binding
- R39 (vs. gap) binding
- TR 80:81 (≠ TT 75:76) binding
- GTT 102:104 (= GTT 97:99) binding ; binding
- AANF 126:129 (≠ APNF 123:126) binding
- F129 (= F126) binding
- H159 (= H153) mutation H->A,Q: 135 to 200-fold reduction in catalytic activity.
- K163 (= K157) binding ; mutation K->A,C,Q: 625 to 830-fold reduction in catalytic activity.
- R240 (= R235) binding
- F243 (= F238) binding
1drwA Escherichia coli dhpr/nhdh complex (see paper)
32% identity, 97% coverage: 2:259/265 of query aligns to 5:260/272 of 1drwA
- active site: H158 (= H153), K162 (= K157)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (= G8), G14 (= G11), R15 (= R12), M16 (= M13), E37 (≠ D34), R38 (vs. gap), F78 (= F74), T79 (= T75), R80 (≠ T76), G101 (= G97), T102 (= T98), T103 (= T99), A126 (≠ P124), N127 (= N125), F128 (= F126), F242 (= F238)
Query Sequence
>WP_015738385.1 NCBI__GCF_000024605.1:WP_015738385.1
MIRVVVTGAAGRMGREVVKAVSRTPGMQLVGAVDPGHTGQDIGLLAGIGPLGVVVRDDLA
NVLRETEASVMVDFTTPHAAVANIKTALACGVRPVVGTTGIPQEEIEEIKNICREKRLGG
LIAPNFALGAVLMMHFAGIAARYFPDVEIIEYHHHQKLDAPSGTALQTAEIIARSRQGGP
TGDRTEVEKLDGARGGNLEGIRIHSIRLPGFVAHQEVIFGGLGQTLTIRHDSTSRESFMP
GVIMAIKKVLELEELVYGLDKLIFG
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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