SitesBLAST
Comparing WP_013075686.1 NCBI__GCF_000092905.1:WP_013075686.1 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)
5z2fA NADPH/pda bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
47% identity, 98% coverage: 6:266/267 of query aligns to 3:265/265 of 5z2fA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R11 (≠ T14), G12 (= G15), K13 (= K16), M14 (= M17), D35 (≠ A38), H36 (≠ S39), K37 (≠ R40), L76 (≠ F77), T77 (= T78), G99 (= G100), T100 (= T101), T101 (≠ S102), P126 (= P127), N127 (= N128), F128 (= F129)
- binding pyridine-2,6-dicarboxylic acid: P126 (= P127), H155 (= H156), H156 (= H157), K159 (= K160), S164 (= S165), G165 (= G166), T166 (= T167), A215 (= A216)
5z2eA Dipicolinate bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
47% identity, 98% coverage: 6:266/267 of query aligns to 3:265/265 of 5z2eA
5wolA Crystal structure of dihydrodipicolinate reductase dapb from coxiella burnetii
44% identity, 98% coverage: 6:266/267 of query aligns to 2:230/230 of 5wolA
- active site: H133 (= H156), K137 (= K160)
- binding pyridine-2-carboxylic acid: P104 (= P127), T144 (= T167), K147 (= K170)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N7 (≠ S11), G11 (= G15), K12 (= K16), M13 (= M17), G34 (≠ A38), R35 (= R42), F54 (= F77), T55 (= T78), T56 (= T79), S59 (≠ A82), G77 (= G100), T78 (= T101), T79 (≠ S102), P104 (= P127), N105 (= N128), F106 (= F129)
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
44% identity, 98% coverage: 6:266/267 of query aligns to 1:242/245 of 1p9lA
- active site: H132 (= H156), K136 (= K160)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (= G12), G10 (= G15), K11 (= K16), V12 (≠ M17), D33 (= D44), A34 (= A45), F52 (= F77), T53 (= T78), V57 (≠ A82), G75 (= G100), T77 (≠ S102), P103 (= P127), N104 (= N128), F105 (= F129), F217 (= F241)
- binding pyridine-2,6-dicarboxylic acid: H133 (= H157), K136 (= K160), S141 (= S165), G142 (= G166), T143 (= T167), A192 (= A216)
1c3vA Dihydrodipicolinate reductase from mycobacterium tuberculosis complexed with NADPH and pdc (see paper)
44% identity, 98% coverage: 6:266/267 of query aligns to 1:242/245 of 1c3vA
- active site: H132 (= H156), K136 (= K160)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K9 (≠ T14), G10 (= G15), K11 (= K16), V12 (≠ M17), D33 (= D44), A34 (= A45), F52 (= F77), T53 (= T78), V57 (≠ A82), G75 (= G100), T77 (≠ S102), P103 (= P127), N104 (= N128), F217 (= F241)
- binding pyridine-2,6-dicarboxylic acid: T77 (≠ S102), N104 (= N128), K136 (= K160), S141 (= S165), G142 (= G166), T143 (= T167), A192 (= A216)
5ugvA Dapb from mycobacterium tuberculosis (see paper)
44% identity, 98% coverage: 6:266/267 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)
44% identity, 98% coverage: 6:266/267 of query aligns to 2:243/245 of 5tjzA
- active site: H133 (= H156), K137 (= K160)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), G11 (= G15), K12 (= K16), V13 (≠ M17), D34 (= D44), A35 (= A45), F53 (= F77), T54 (= T78), G76 (= G100), T77 (= T101), T78 (≠ S102), P104 (= P127), N105 (= N128), F106 (= F129), F218 (= F241)
- binding pyridine-2,6-dicarboxylic acid: T78 (≠ S102), P104 (= P127), H134 (= H157), K137 (= K160), S142 (= S165), G143 (= G166), T144 (= T167), A193 (= A216)
P9WP23 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
44% identity, 98% coverage: 6:266/267 of query aligns to 1:242/245 of P9WP23
- K9 (≠ T14) 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 (= K16) 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 (≠ KM 16:17) binding NAD(+); binding NADP(+)
- D33 (= D44) binding NAD(+)
- GTT 75:77 (≠ GTS 100:102) binding NAD(+); binding NADP(+)
- APNF 102:105 (= APNF 126:129) binding NAD(+); binding NADP(+)
- K136 (= K160) binding NAD(+); binding NADP(+)
1yl5A Crystal structure of mycobacterium tuberculosis dihydrodipicolinate reductase (rv2773c) (crystal form a) (see paper)
44% identity, 97% coverage: 7:266/267 of query aligns to 4:244/247 of 1yl5A
5eesA Crystal structure of dapb in complex with NADP+ from corynebacterium glutamicum (see paper)
41% identity, 98% coverage: 6:267/267 of query aligns to 2:246/247 of 5eesA
- active site: H133 (= H156), K137 (= K160)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), G11 (= G15), R12 (≠ K16), V13 (≠ M17), G34 (= G55), V35 (≠ I56), F53 (= F77), T54 (= T78), G76 (= G100), T78 (≠ S102), P104 (= P127), N105 (= N128), F106 (= F129), F220 (= F241)
- binding sulfate ion: H134 (= H157), K137 (= K160), K137 (= K160), G143 (= G166), T144 (= T167)
5eerA Crystal structure of dapb from corynebacterium glutamicum (see paper)
41% identity, 98% coverage: 6:267/267 of query aligns to 2:246/247 of 5eerA
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
31% identity, 98% coverage: 1:262/267 of query aligns to 1:261/273 of P04036
- G12 (= G12) binding NADP(+)
- GRM 15:17 (≠ GKM 15:17) binding NAD(+)
- RM 16:17 (≠ KM 16:17) binding NADP(+)
- E38 (vs. gap) binding NAD(+)
- R39 (vs. gap) binding NADP(+)
- TR 80:81 (≠ TT 78:79) binding NAD(+)
- GTT 102:104 (≠ GTS 100:102) binding NAD(+); binding NADP(+)
- AANF 126:129 (≠ APNF 126:129) binding NAD(+)
- F129 (= F129) binding NADP(+)
- H159 (= H156) mutation H->A,Q: 135 to 200-fold reduction in catalytic activity.
- K163 (= K160) binding NAD(+); mutation K->A,C,Q: 625 to 830-fold reduction in catalytic activity.
- R240 (= R238) binding NADP(+)
- F243 (= F241) binding NAD(+)
1drwA Escherichia coli dhpr/nhdh complex (see paper)
31% identity, 97% coverage: 3:262/267 of query aligns to 2:260/272 of 1drwA
- active site: H158 (= H156), K162 (= K160)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (= G12), G14 (= G15), R15 (≠ K16), M16 (= M17), E37 (vs. gap), R38 (vs. gap), F78 (= F77), T79 (= T78), R80 (≠ T79), G101 (= G100), T102 (= T101), T103 (≠ S102), A126 (≠ P127), N127 (= N128), F128 (= F129), F242 (= F241)
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
31% identity, 97% coverage: 3:262/267 of query aligns to 2:260/272 of 1dihA
- active site: H158 (= H156), K162 (= K160)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G12), G14 (= G15), R15 (≠ K16), M16 (= M17), R38 (vs. gap), F78 (= F77), T79 (= T78), R80 (≠ T79), G83 (≠ A82), G101 (= G100), T103 (≠ S102), N127 (= N128), F128 (= F129), R239 (= R238), F242 (= F241)
1drvA Escherichia coli dhpr/acnadh complex (see paper)
31% identity, 97% coverage: 5:262/267 of query aligns to 2:258/270 of 1drvA
- active site: H156 (= H156), K160 (= K160)
- binding 3-acetylpyridine adenine dinucleotide: G9 (= G12), G12 (= G15), R13 (≠ K16), M14 (= M17), E35 (vs. gap), F76 (= F77), T77 (= T78), R78 (≠ T79), G81 (≠ A82), G99 (= G100), A124 (≠ P127), F126 (= F129), R237 (= R238)
1druA Escherichia coli dhpr/nadh complex (see paper)
31% identity, 97% coverage: 5:262/267 of query aligns to 2:258/270 of 1druA
- active site: H156 (= H156), K160 (= K160)
- binding nicotinamide-adenine-dinucleotide: G9 (= G12), G12 (= G15), R13 (≠ K16), M14 (= M17), E35 (vs. gap), R36 (vs. gap), F76 (= F77), T77 (= T78), R78 (≠ T79), G81 (≠ A82), G99 (= G100), T100 (= T101), T101 (≠ S102), A124 (≠ P127), N125 (= N128), F126 (= F129), F240 (= F241)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
31% identity, 97% coverage: 5:262/267 of query aligns to 2:258/270 of 1arzA
1arzB Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
31% identity, 97% coverage: 5:262/267 of query aligns to 1:257/269 of 1arzB
- active site: H155 (= H156), K159 (= K160)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G12), G10 (≠ T14), G11 (= G15), R12 (≠ K16), M13 (= M17), E34 (vs. gap), F75 (= F77), T76 (= T78), R77 (≠ T79), G80 (≠ A82), H84 (= H86), G98 (= G100), T100 (≠ S102), A123 (≠ P127), N124 (= N128), F125 (= F129), F239 (= F241)
- binding pyridine-2,6-dicarboxylic acid: T100 (≠ S102), H156 (= H157), K159 (= K160), S164 (= S165), G165 (= G166), T166 (= T167), F239 (= F241)
4ywjA Crystal structure of 4-hydroxy-tetrahydrodipicolinate reductase (htpa reductase) from pseudomonas aeruginosa
31% identity, 98% coverage: 7:267/267 of query aligns to 3:266/268 of 4ywjA
- active site: H156 (= H156), K160 (= K160)
- binding nicotinamide-adenine-dinucleotide: G11 (= G15), R12 (≠ K16), M13 (= M17), D35 (≠ S39), R36 (= R40), F76 (= F77), T77 (= T78), V81 (≠ A82), G99 (= G100), T101 (≠ S102), A124 (≠ P127), N125 (= N128), F126 (= F129), R237 (= R238), F240 (= F241)
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
29% identity, 91% coverage: 6:248/267 of query aligns to 2:246/266 of 5temA
- active site: H155 (= H156), K159 (= K160)
- binding nicotinamide-adenine-dinucleotide: G8 (= G12), G11 (= G15), R12 (≠ K16), M13 (= M17), E34 (≠ S39), R35 (= R40), F75 (= F77), T76 (= T78), S80 (≠ A82), G98 (= G100), T100 (≠ S102), P123 (= P127), N124 (= N128), Y125 (≠ F129), F239 (= F241)
- binding pyridine-2,6-dicarboxylic acid: T100 (≠ S102), P123 (= P127), H156 (= H157), K159 (= K160), S164 (= S165), G165 (= G166), T166 (= T167)
Query Sequence
>WP_013075686.1 NCBI__GCF_000092905.1:WP_013075686.1
MTEGEIRVVVSGATGKMGREVIRTMVAETGLRLVGAVASRAREDAGVAAGMEPLGIPVSA
NLRETLVSAEPDVLVDFTTPDAVERHVQEALEFGVRPVVGTSGVTREQVRRWDGLCRERS
VGGIVAPNFAVGAVLMMRFVREAARYLPHVEIIEMHHDGKLDAPSGTAVKTAEELAEAGI
DLSSGKPDERELFPGARGAAIGGVRVHSVRLPGLVAHQEVILGGPGQILTVRHDSLDRVS
FMPGVVLAVRAVMGYVGMMYGLEALLG
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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