SitesBLAST
Comparing N515DRAFT_2152 FitnessBrowser__Dyella79:N515DRAFT_2152 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)
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
34% identity, 99% coverage: 3:267/267 of query aligns to 1:244/245 of 1p9lA
- active site: H132 (≠ A153), K136 (= K157)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (= G9), G10 (= G12), K11 (≠ W13), V12 (≠ A14), D33 (≠ S35), A34 (= A39), F52 (≠ Y74), T53 (= T75), V57 (≠ S79), G75 (= G97), T77 (≠ S99), P103 (≠ G124), N104 (= N125), F105 (= F126), F217 (≠ Y239)
- binding pyridine-2,6-dicarboxylic acid: H133 (≠ Y154), K136 (= K157), S141 (= S162), G142 (= G163), T143 (= T164), A192 (≠ L213)
1c3vA Dihydrodipicolinate reductase from mycobacterium tuberculosis complexed with NADPH and pdc (see paper)
34% identity, 99% coverage: 3:267/267 of query aligns to 1:244/245 of 1c3vA
- active site: H132 (≠ A153), K136 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K9 (≠ T11), G10 (= G12), K11 (≠ W13), V12 (≠ A14), D33 (≠ S35), A34 (= A39), F52 (≠ Y74), T53 (= T75), V57 (≠ S79), G75 (= G97), T77 (≠ S99), P103 (≠ G124), N104 (= N125), F217 (≠ Y239)
- binding pyridine-2,6-dicarboxylic acid: T77 (≠ S99), N104 (= N125), K136 (= K157), S141 (= S162), G142 (= G163), T143 (= T164), A192 (≠ L213)
5ugvA Dapb from mycobacterium tuberculosis (see paper)
34% identity, 99% coverage: 3:267/267 of query aligns to 2:245/245 of 5ugvA
5tjzA Structure of 4-hydroxytetrahydrodipicolinate reductase from mycobacterium tuberculosis with NADPH and 2,6 pyridine dicarboxylic acid (see paper)
34% identity, 99% coverage: 3:267/267 of query aligns to 2:245/245 of 5tjzA
- active site: H133 (≠ A153), K137 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), G11 (= G12), K12 (≠ W13), V13 (≠ A14), D34 (≠ S35), A35 (= A39), F53 (≠ Y74), T54 (= T75), G76 (= G97), T77 (= T98), T78 (≠ S99), P104 (≠ G124), N105 (= N125), F106 (= F126), F218 (≠ Y239)
- binding pyridine-2,6-dicarboxylic acid: T78 (≠ S99), P104 (≠ G124), H134 (≠ Y154), K137 (= K157), S142 (= S162), G143 (= G163), T144 (= T164), A193 (≠ L213)
P9WP23 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
34% identity, 99% coverage: 3:267/267 of query aligns to 1:244/245 of P9WP23
- K9 (≠ T11) 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 (≠ W13) 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 (≠ WA 13:14) binding ; binding
- D33 (≠ S35) binding
- GTT 75:77 (≠ GTS 97:99) binding ; binding
- APNF 102:105 (≠ CGNF 123:126) binding ; binding
- K136 (= K157) binding ; binding
1yl5A Crystal structure of mycobacterium tuberculosis dihydrodipicolinate reductase (rv2773c) (crystal form a) (see paper)
34% identity, 99% coverage: 5:267/267 of query aligns to 5:246/247 of 1yl5A
5z2fA NADPH/pda bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
30% identity, 99% coverage: 1:265/267 of query aligns to 1:265/265 of 5z2fA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R11 (≠ T11), G12 (= G12), K13 (≠ W13), M14 (≠ A14), D35 (≠ S35), H36 (≠ R36), K37 (= K37), L76 (≠ Y74), T77 (= T75), G99 (= G97), T100 (= T98), T101 (≠ S99), P126 (≠ G124), N127 (= N125), F128 (= F126)
- binding pyridine-2,6-dicarboxylic acid: P126 (≠ G124), H155 (≠ A153), H156 (≠ Y154), K159 (= K157), S164 (= S162), G165 (= G163), T166 (= T164), A215 (≠ L213)
5z2eA Dipicolinate bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
30% identity, 99% coverage: 1:265/267 of query aligns to 1:265/265 of 5z2eA
5wolA Crystal structure of dihydrodipicolinate reductase dapb from coxiella burnetii
31% identity, 94% coverage: 3:253/267 of query aligns to 2:219/230 of 5wolA
- active site: H133 (≠ A153), K137 (= K157)
- binding pyridine-2-carboxylic acid: P104 (≠ G124), T144 (= T164), K147 (≠ E167)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N7 (≠ A8), G11 (= G12), K12 (≠ W13), M13 (≠ A14), G34 (≠ S35), R35 (= R36), F54 (≠ Y74), T55 (= T75), T56 (≠ R76), S59 (= S79), G77 (= G97), T78 (= T98), T79 (≠ S99), P104 (≠ G124), N105 (= N125), F106 (= F126)
5eesA Crystal structure of dapb in complex with NADP+ from corynebacterium glutamicum (see paper)
33% identity, 75% coverage: 69:267/267 of query aligns to 48:247/247 of 5eesA
- active site: H133 (≠ A153), K137 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F53 (≠ Y74), T54 (= T75), G76 (= G97), T78 (≠ S99), P104 (≠ G124), N105 (= N125), F106 (= F126), F220 (≠ Y239)
- binding sulfate ion: H134 (≠ Y154), K137 (= K157), K137 (= K157), G143 (= G163), T144 (= T164)
Sites not aligning to the query:
5eerA Crystal structure of dapb from corynebacterium glutamicum (see paper)
33% identity, 75% coverage: 69:267/267 of query aligns to 48:247/247 of 5eerA
1arzB Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
29% identity, 100% coverage: 2:267/267 of query aligns to 1:266/269 of 1arzB
- active site: H155 (≠ A153), K159 (= K157)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G9), G10 (≠ T11), G11 (= G12), R12 (≠ W13), M13 (≠ A14), E34 (≠ S35), F75 (≠ Y74), T76 (= T75), R77 (= R76), G80 (≠ S79), H84 (≠ N83), G98 (= G97), T100 (≠ S99), A123 (≠ C123), N124 (= N125), F125 (= F126), F239 (≠ Y239)
- binding pyridine-2,6-dicarboxylic acid: T100 (≠ S99), H156 (≠ Y154), K159 (= K157), S164 (= S162), G165 (= G163), T166 (= T164), F239 (≠ Y239)
1drvA Escherichia coli dhpr/acnadh complex (see paper)
29% identity, 100% coverage: 2:267/267 of query aligns to 2:267/270 of 1drvA
- active site: H156 (≠ A153), K160 (= K157)
- binding 3-acetylpyridine adenine dinucleotide: G9 (= G9), G12 (= G12), R13 (≠ W13), M14 (≠ A14), E35 (≠ S35), F76 (≠ Y74), T77 (= T75), R78 (= R76), G81 (≠ S79), G99 (= G97), A124 (≠ C123), F126 (= F126), R237 (≠ A236)
1druA Escherichia coli dhpr/nadh complex (see paper)
29% identity, 100% coverage: 2:267/267 of query aligns to 2:267/270 of 1druA
- active site: H156 (≠ A153), K160 (= K157)
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), G12 (= G12), R13 (≠ W13), M14 (≠ A14), E35 (≠ S35), R36 (= R36), F76 (≠ Y74), T77 (= T75), R78 (= R76), G81 (≠ S79), G99 (= G97), T100 (= T98), T101 (≠ S99), A124 (≠ C123), N125 (= N125), F126 (= F126), F240 (≠ Y239)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
29% identity, 100% coverage: 2:267/267 of query aligns to 2:267/270 of 1arzA
1drwA Escherichia coli dhpr/nhdh complex (see paper)
29% identity, 100% coverage: 2:267/267 of query aligns to 4:269/272 of 1drwA
- active site: H158 (≠ A153), K162 (= K157)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (= G9), G14 (= G12), R15 (≠ W13), M16 (≠ A14), E37 (≠ S35), R38 (= R36), F78 (≠ Y74), T79 (= T75), R80 (= R76), G101 (= G97), T102 (= T98), T103 (≠ S99), A126 (≠ C123), N127 (= N125), F128 (= F126), F242 (≠ Y239)
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
29% identity, 100% coverage: 2:267/267 of query aligns to 4:269/272 of 1dihA
- active site: H158 (≠ A153), K162 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G9), G14 (= G12), R15 (≠ W13), M16 (≠ A14), R38 (= R36), F78 (≠ Y74), T79 (= T75), R80 (= R76), G83 (≠ S79), G101 (= G97), T103 (≠ S99), N127 (= N125), F128 (= F126), R239 (≠ A236), F242 (≠ Y239)
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
29% identity, 100% coverage: 2:267/267 of query aligns to 5:270/273 of P04036
- G12 (= G9) binding
- GRM 15:17 (≠ GWA 12:14) binding
- RM 16:17 (≠ WA 13:14) binding
- E38 (≠ S35) binding
- R39 (= R36) binding
- TR 80:81 (= TR 75:76) binding
- GTT 102:104 (≠ GTS 97:99) binding ; binding
- AA-NF 126:129 (≠ ACGNF 122:126) binding
- F129 (= F126) binding
- H159 (≠ A153) 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 (≠ A236) binding
- F243 (≠ Y239) binding
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
27% identity, 61% coverage: 3:164/267 of query aligns to 2:166/266 of 5temA
- active site: H155 (≠ A153), K159 (= K157)
- binding nicotinamide-adenine-dinucleotide: G8 (= G9), G11 (= G12), R12 (≠ W13), M13 (≠ A14), E34 (≠ S35), R35 (= R36), F75 (≠ Y74), T76 (= T75), S80 (= S79), G98 (= G97), T100 (≠ S99), P123 (≠ G124), N124 (= N125), Y125 (≠ F126)
- binding pyridine-2,6-dicarboxylic acid: T100 (≠ S99), P123 (≠ G124), H156 (≠ Y154), K159 (= K157), S164 (= S162), G165 (= G163), T166 (= T164)
Sites not aligning to the query:
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
27% identity, 61% coverage: 3:164/267 of query aligns to 2:166/269 of 5tejB
- active site: H155 (≠ A153), K159 (= K157)
- binding 2,5 Furan Dicarboxylic Acid: T100 (≠ S99), H156 (≠ Y154), K159 (= K157), S164 (= S162), G165 (= G163), T166 (= T164)
- binding nicotinamide-adenine-dinucleotide: G8 (= G9), G11 (= G12), R12 (≠ W13), M13 (≠ A14), E34 (≠ S35), R35 (= R36), F75 (≠ Y74), T76 (= T75), S80 (= S79), G98 (= G97), T100 (≠ S99), P123 (≠ G124), N124 (= N125), Y125 (≠ F126)
Sites not aligning to the query:
Query Sequence
>N515DRAFT_2152 FitnessBrowser__Dyella79:N515DRAFT_2152
MTLNVCLAGATGWAGSELARGLAVADGLKLVSAVSRKHAGATLAQALGDERLDAPVFATA
AEALSKPVDVFMEYTRPDSAKANILAALEHGAHVVVGTSGLSDEDYARIDEAARAKGRAV
LACGNFALTMVLLQKFAEQAAKYIPSWEIIDYAYEGKPDAPSGTVRELAGRLGKVRQPEP
GLPLEKTNGVRETRGGTLGGAQVHAVRLPGFVLGAEVIFGMPDQTLTLRHNAGSSAKPYV
DGALLAIRKVSGLAPGLHRGLDKVLEL
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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