SitesBLAST
Comparing AO356_07490 FitnessBrowser__pseudo5_N2C3_1:AO356_07490 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)
4ywjA Crystal structure of 4-hydroxy-tetrahydrodipicolinate reductase (htpa reductase) from pseudomonas aeruginosa
81% identity, 100% coverage: 1:268/268 of query aligns to 1:268/268 of 4ywjA
- active site: H156 (= H156), K160 (= K160)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), R12 (= R12), M13 (= M13), D35 (≠ V35), R36 (= R36), F76 (= F76), T77 (= T77), V81 (= V81), G99 (= G99), T101 (= T101), A124 (= A124), N125 (= N125), F126 (= F126), R237 (= R237), F240 (= F240)
1drvA Escherichia coli dhpr/acnadh complex (see paper)
65% identity, 99% coverage: 3:268/268 of query aligns to 4:268/270 of 1drvA
- active site: H156 (= H156), K160 (= K160)
- binding 3-acetylpyridine adenine dinucleotide: G9 (= G8), G12 (= G11), R13 (= R12), M14 (= M13), E35 (≠ V35), F76 (= F76), T77 (= T77), R78 (≠ L78), G81 (≠ V81), G99 (= G99), A124 (= A124), F126 (= F126), R237 (= R237)
1druA Escherichia coli dhpr/nadh complex (see paper)
65% identity, 99% coverage: 3:268/268 of query aligns to 4:268/270 of 1druA
- active site: H156 (= H156), K160 (= K160)
- binding nicotinamide-adenine-dinucleotide: G9 (= G8), G12 (= G11), R13 (= R12), M14 (= M13), E35 (≠ V35), R36 (= R36), F76 (= F76), T77 (= T77), R78 (≠ L78), G81 (≠ V81), G99 (= G99), T100 (= T100), T101 (= T101), A124 (= A124), N125 (= N125), F126 (= F126), F240 (= F240)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
65% identity, 99% coverage: 3:268/268 of query aligns to 4:268/270 of 1arzA
1arzB Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
65% identity, 99% coverage: 3:268/268 of query aligns to 3:267/269 of 1arzB
- active site: H155 (= H156), K159 (= K160)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G8), G10 (≠ A10), G11 (= G11), R12 (= R12), M13 (= M13), E34 (≠ V35), F75 (= F76), T76 (= T77), R77 (≠ L78), G80 (≠ V81), H84 (≠ N85), G98 (= G99), T100 (= T101), A123 (= A124), N124 (= N125), F125 (= F126), F239 (= F240)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T101), H156 (= H157), K159 (= K160), S164 (= S165), G165 (= G166), T166 (= T167), F239 (= F240)
1drwA Escherichia coli dhpr/nhdh complex (see paper)
65% identity, 99% coverage: 3:268/268 of query aligns to 6:270/272 of 1drwA
- active site: H158 (= H156), K162 (= K160)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (= G8), G14 (= G11), R15 (= R12), M16 (= M13), E37 (≠ V35), R38 (= R36), F78 (= F76), T79 (= T77), R80 (≠ L78), G101 (= G99), T102 (= T100), T103 (= T101), A126 (= A124), N127 (= N125), F128 (= F126), F242 (= F240)
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
65% identity, 99% coverage: 3:268/268 of query aligns to 6:270/272 of 1dihA
- active site: H158 (= H156), K162 (= K160)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G8), G14 (= G11), R15 (= R12), M16 (= M13), R38 (= R36), F78 (= F76), T79 (= T77), R80 (≠ L78), G83 (≠ V81), G101 (= G99), T103 (= T101), N127 (= N125), F128 (= F126), R239 (= R237), F242 (= F240)
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
65% identity, 99% coverage: 3:268/268 of query aligns to 7:271/273 of P04036
- G12 (= G8) binding
- GRM 15:17 (= GRM 11:13) binding
- RM 16:17 (= RM 12:13) binding
- E38 (≠ V35) binding
- R39 (= R36) binding
- TR 80:81 (≠ TL 77:78) binding
- GTT 102:104 (= GTT 99:101) binding ; binding
- AANF 126:129 (= AANF 123:126) binding
- F129 (= F126) binding
- H159 (= H156) mutation H->A,Q: 135 to 200-fold reduction in catalytic activity.
- K163 (= K160) binding ; mutation K->A,C,Q: 625 to 830-fold reduction in catalytic activity.
- R240 (= R237) binding
- F243 (= F240) binding
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
56% identity, 100% coverage: 1:267/268 of query aligns to 1:266/266 of 5temA
- active site: H155 (= H156), K159 (= K160)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G11 (= G11), R12 (= R12), M13 (= M13), E34 (≠ V35), R35 (= R36), F75 (= F76), T76 (= T77), S80 (≠ V81), G98 (= G99), T100 (= T101), P123 (≠ A124), N124 (= N125), Y125 (≠ F126), F239 (= F240)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T101), P123 (≠ A124), H156 (= H157), K159 (= K160), S164 (= S165), G165 (= G166), T166 (= T167)
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
56% identity, 100% coverage: 1:268/268 of query aligns to 1:267/269 of 5tejB
- active site: H155 (= H156), K159 (= K160)
- binding 2,5 Furan Dicarboxylic Acid: T100 (= T101), H156 (= H157), K159 (= K160), S164 (= S165), G165 (= G166), T166 (= T167)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G11 (= G11), R12 (= R12), M13 (= M13), E34 (≠ V35), R35 (= R36), F75 (= F76), T76 (= T77), S80 (≠ V81), G98 (= G99), T100 (= T101), P123 (≠ A124), N124 (= N125), Y125 (≠ F126), F239 (= F240)
5tejA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
56% identity, 100% coverage: 1:268/268 of query aligns to 1:267/269 of 5tejA
- active site: H155 (= H156), K159 (= K160)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G11 (= G11), R12 (= R12), M13 (= M13), E34 (≠ V35), R35 (= R36), F75 (= F76), T76 (= T77), S80 (≠ V81), G98 (= G99), T100 (= T101), P123 (≠ A124)
3ijpB Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
42% identity, 99% coverage: 3:268/268 of query aligns to 3:267/267 of 3ijpB
3ijpA Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
42% identity, 99% coverage: 3:267/268 of query aligns to 3:266/266 of 3ijpA
- active site: H155 (= H156), K159 (= K160)
- binding sodium ion: I21 (≠ V21), Q22 (= Q22), R24 (= R24), V27 (≠ L27)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G8), N10 (≠ A10), G11 (= G11), R12 (= R12), M13 (= M13), R35 (= R36), F75 (= F76), S76 (≠ T77), Q77 (≠ L78), A80 (≠ V81), G98 (= G99), T100 (= T101), G123 (≠ A124), N124 (= N125), M125 (≠ F126), F239 (= F240)
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)
38% identity, 74% coverage: 67:265/268 of query aligns to 39:212/216 of Q9X1K8
Sites not aligning to the query:
1vm6B Crystal structure of dihydrodipicolinate reductase (tm1520) from thermotoga maritima at 2.27 a resolution
38% identity, 76% coverage: 61:265/268 of query aligns to 39:217/218 of 1vm6B
- active site: H132 (= H156), K136 (= K160)
- binding nicotinamide-adenine-dinucleotide: F53 (= F76), S54 (≠ T77), S55 (≠ L78), E57 (≠ D80), A58 (≠ V81), G76 (= G99), T78 (= T101), Y101 (≠ A124), N102 (= N125), F103 (= F126), F192 (= F240)
Sites not aligning to the query:
1yl5A Crystal structure of mycobacterium tuberculosis dihydrodipicolinate reductase (rv2773c) (crystal form a) (see paper)
35% identity, 100% coverage: 1:268/268 of query aligns to 2:247/247 of 1yl5A
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
35% identity, 99% coverage: 3:268/268 of query aligns to 2:245/245 of 1p9lA
- active site: H132 (= H156), K136 (= K160)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (= G8), G10 (= G11), K11 (≠ R12), V12 (≠ M13), D33 (= D45), A34 (= A46), F52 (= F76), T53 (= T77), V57 (= V81), G75 (= G99), T77 (= T101), P103 (≠ A124), N104 (= N125), F105 (= F126), F217 (= F240)
- binding pyridine-2,6-dicarboxylic acid: H133 (= H157), K136 (= K160), S141 (= S165), G142 (= G166), T143 (= T167), A192 (≠ G215)
1c3vA Dihydrodipicolinate reductase from mycobacterium tuberculosis complexed with NADPH and pdc (see paper)
35% identity, 99% coverage: 3:268/268 of query aligns to 2:245/245 of 1c3vA
- active site: H132 (= H156), K136 (= K160)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K9 (≠ A10), G10 (= G11), K11 (≠ R12), V12 (≠ M13), D33 (= D45), A34 (= A46), F52 (= F76), T53 (= T77), V57 (= V81), G75 (= G99), T77 (= T101), P103 (≠ A124), N104 (= N125), F217 (= F240)
- binding pyridine-2,6-dicarboxylic acid: T77 (= T101), N104 (= N125), K136 (= K160), S141 (= S165), G142 (= G166), T143 (= T167), A192 (≠ G215)
P9WP23 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
35% identity, 99% coverage: 3:268/268 of query aligns to 2:245/245 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 (= D45) binding
- GTT 75:77 (= GTT 99:101) binding ; binding
- APNF 102:105 (≠ AANF 123:126) binding ; binding
- K136 (= K160) binding ; binding
5ugvA Dapb from mycobacterium tuberculosis (see paper)
35% identity, 99% coverage: 3:267/268 of query aligns to 3:245/245 of 5ugvA
Query Sequence
>AO356_07490 FitnessBrowser__pseudo5_N2C3_1:AO356_07490
MRRIAVMGAAGRMGKALVEAVQQRSPLSGLTAAIVRPDSTLVGADAGELASLGRIGVPMS
GGLEKVLDEFDVLIDFTLPDVMLKNLAICRKHGKAMVIGTTGLDAAQKQLLAEAGNDIAI
VFAANFSVGVNLSLKLLDMAARVLGDDADIEIIEAHHRHKIDAPSGTALRMGEVIADALG
RDLQKVAVYGREGHTGARERDTIGFATVRGGDVVGDHTVLFATEGERLEITHKASSRMTF
AKGAVRAALWLDGREPGLYDMQDVLDLR
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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