SitesBLAST
Comparing WP_068167655.1 NCBI__GCF_001592305.1:WP_068167655.1 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)
4ywjA Crystal structure of 4-hydroxy-tetrahydrodipicolinate reductase (htpa reductase) from pseudomonas aeruginosa
58% identity, 97% coverage: 9:273/273 of query aligns to 2:268/268 of 4ywjA
- active site: H156 (= H161), K160 (= K165)
- binding nicotinamide-adenine-dinucleotide: G11 (= G18), R12 (= R19), M13 (= M20), D35 (= D41), R36 (= R42), F76 (= F81), T77 (= T82), V81 (≠ G86), G99 (= G104), T101 (= T106), A124 (≠ P129), N125 (= N130), F126 (≠ M131), R237 (= R242), F240 (≠ Y245)
1drwA Escherichia coli dhpr/nhdh complex (see paper)
60% identity, 97% coverage: 10:273/273 of query aligns to 6:270/272 of 1drwA
- active site: H158 (= H161), K162 (= K165)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (= G15), G14 (= G18), R15 (= R19), M16 (= M20), E37 (≠ D41), R38 (= R42), F78 (= F81), T79 (= T82), R80 (= R83), G101 (= G104), T102 (= T105), T103 (= T106), A126 (≠ P129), N127 (= N130), F128 (≠ M131), F242 (≠ Y245)
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
60% identity, 97% coverage: 10:273/273 of query aligns to 6:270/272 of 1dihA
- active site: H158 (= H161), K162 (= K165)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), G14 (= G18), R15 (= R19), M16 (= M20), R38 (= R42), F78 (= F81), T79 (= T82), R80 (= R83), G83 (= G86), G101 (= G104), T103 (= T106), N127 (= N130), F128 (≠ M131), R239 (= R242), F242 (≠ Y245)
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
60% identity, 97% coverage: 10:273/273 of query aligns to 7:271/273 of P04036
- G12 (= G15) binding
- GRM 15:17 (= GRM 18:20) binding
- RM 16:17 (= RM 19:20) binding
- E38 (≠ D41) binding
- R39 (= R42) binding
- TR 80:81 (= TR 82:83) binding
- GTT 102:104 (= GTT 104:106) binding ; binding
- AANF 126:129 (≠ APNM 128:131) binding
- F129 (≠ M131) binding
- H159 (= H161) mutation H->A,Q: 135 to 200-fold reduction in catalytic activity.
- K163 (= K165) binding ; mutation K->A,C,Q: 625 to 830-fold reduction in catalytic activity.
- R240 (= R242) binding
- F243 (≠ Y245) binding
1drvA Escherichia coli dhpr/acnadh complex (see paper)
60% identity, 97% coverage: 10:273/273 of query aligns to 4:268/270 of 1drvA
- active site: H156 (= H161), K160 (= K165)
- binding 3-acetylpyridine adenine dinucleotide: G9 (= G15), G12 (= G18), R13 (= R19), M14 (= M20), E35 (≠ D41), F76 (= F81), T77 (= T82), R78 (= R83), G81 (= G86), G99 (= G104), A124 (≠ P129), F126 (≠ M131), R237 (= R242)
1druA Escherichia coli dhpr/nadh complex (see paper)
60% identity, 97% coverage: 10:273/273 of query aligns to 4:268/270 of 1druA
- active site: H156 (= H161), K160 (= K165)
- binding nicotinamide-adenine-dinucleotide: G9 (= G15), G12 (= G18), R13 (= R19), M14 (= M20), E35 (≠ D41), R36 (= R42), F76 (= F81), T77 (= T82), R78 (= R83), G81 (= G86), G99 (= G104), T100 (= T105), T101 (= T106), A124 (≠ P129), N125 (= N130), F126 (≠ M131), F240 (≠ Y245)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
60% identity, 97% coverage: 10:273/273 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)
60% identity, 97% coverage: 10:273/273 of query aligns to 3:267/269 of 1arzB
- active site: H155 (= H161), K159 (= K165)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G15), G10 (≠ S17), G11 (= G18), R12 (= R19), M13 (= M20), E34 (≠ D41), F75 (= F81), T76 (= T82), R77 (= R83), G80 (= G86), H84 (= H90), G98 (= G104), T100 (= T106), A123 (≠ P129), N124 (= N130), F125 (≠ M131), F239 (≠ Y245)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T106), H156 (= H162), K159 (= K165), S164 (= S170), G165 (= G171), T166 (= T172), F239 (≠ Y245)
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
52% identity, 97% coverage: 10:273/273 of query aligns to 3:267/269 of 5tejB
- active site: H155 (= H161), K159 (= K165)
- binding 2,5 Furan Dicarboxylic Acid: T100 (= T106), H156 (= H162), K159 (= K165), S164 (= S170), G165 (= G171), T166 (= T172)
- binding nicotinamide-adenine-dinucleotide: G8 (= G15), G11 (= G18), R12 (= R19), M13 (= M20), E34 (≠ D41), R35 (= R42), F75 (= F81), T76 (= T82), S80 (≠ G86), G98 (= G104), T100 (= T106), P123 (= P129), N124 (= N130), Y125 (≠ M131), F239 (≠ Y245)
5tejA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
52% identity, 97% coverage: 10:273/273 of query aligns to 3:267/269 of 5tejA
- active site: H155 (= H161), K159 (= K165)
- binding nicotinamide-adenine-dinucleotide: G8 (= G15), G11 (= G18), R12 (= R19), M13 (= M20), E34 (≠ D41), R35 (= R42), F75 (= F81), T76 (= T82), S80 (≠ G86), G98 (= G104), T100 (= T106), P123 (= P129)
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
52% identity, 96% coverage: 10:272/273 of query aligns to 3:266/266 of 5temA
- active site: H155 (= H161), K159 (= K165)
- binding nicotinamide-adenine-dinucleotide: G8 (= G15), G11 (= G18), R12 (= R19), M13 (= M20), E34 (≠ D41), R35 (= R42), F75 (= F81), T76 (= T82), S80 (≠ G86), G98 (= G104), T100 (= T106), P123 (= P129), N124 (= N130), Y125 (≠ M131), F239 (≠ Y245)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T106), P123 (= P129), H156 (= H162), K159 (= K165), S164 (= S170), G165 (= G171), T166 (= T172)
3ijpB Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
43% identity, 97% coverage: 8:273/273 of query aligns to 1:267/267 of 3ijpB
3ijpA Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
43% identity, 97% coverage: 8:272/273 of query aligns to 1:266/266 of 3ijpA
- active site: H155 (= H161), K159 (= K165)
- binding sodium ion: I21 (≠ V28), Q22 (≠ R29), R24 (≠ S31), V27 (≠ C34)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G15), N10 (≠ S17), G11 (= G18), R12 (= R19), M13 (= M20), R35 (= R42), F75 (= F81), S76 (≠ T82), Q77 (≠ R83), A80 (≠ G86), G98 (= G104), T100 (= T106), G123 (≠ P129), N124 (= N130), M125 (= M131), F239 (≠ Y245)
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)
30% identity, 95% coverage: 13:270/273 of query aligns to 5:212/216 of Q9X1K8
1vm6B Crystal structure of dihydrodipicolinate reductase (tm1520) from thermotoga maritima at 2.27 a resolution
30% identity, 95% coverage: 13:270/273 of query aligns to 10:217/218 of 1vm6B
- active site: H132 (= H161), K136 (= K165)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), S14 (= S17), G15 (= G18), R16 (= R19), M17 (= M20), D37 (≠ N65), V38 (≠ A66), F53 (= F81), S54 (≠ T82), S55 (≠ R83), E57 (= E85), A58 (≠ G86), G76 (= G104), T78 (= T106), Y101 (≠ P129), N102 (= N130), F103 (≠ M131), F192 (≠ Y245)
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
29% identity, 95% coverage: 10:269/273 of query aligns to 2:244/245 of 1p9lA
- active site: H132 (= H161), K136 (= K165)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (= G15), G10 (= G18), K11 (≠ R19), V12 (≠ M20), D33 (= D41), A34 (= A43), F52 (= F81), T53 (= T82), V57 (≠ G86), G75 (= G104), T77 (= T106), P103 (= P129), N104 (= N130), F105 (≠ M131), F217 (≠ Y245)
- binding pyridine-2,6-dicarboxylic acid: H133 (= H162), K136 (= K165), S141 (= S170), G142 (= G171), T143 (= T172), A192 (≠ G220)
1c3vA Dihydrodipicolinate reductase from mycobacterium tuberculosis complexed with NADPH and pdc (see paper)
29% identity, 95% coverage: 10:269/273 of query aligns to 2:244/245 of 1c3vA
- active site: H132 (= H161), K136 (= K165)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K9 (≠ S17), G10 (= G18), K11 (≠ R19), V12 (≠ M20), D33 (= D41), A34 (= A43), F52 (= F81), T53 (= T82), V57 (≠ G86), G75 (= G104), T77 (= T106), P103 (= P129), N104 (= N130), F217 (≠ Y245)
- binding pyridine-2,6-dicarboxylic acid: T77 (= T106), N104 (= N130), K136 (= K165), S141 (= S170), G142 (= G171), T143 (= T172), A192 (≠ G220)
1yl5A Crystal structure of mycobacterium tuberculosis dihydrodipicolinate reductase (rv2773c) (crystal form a) (see paper)
29% identity, 95% coverage: 10:269/273 of query aligns to 4:246/247 of 1yl5A
5ugvA Dapb from mycobacterium tuberculosis (see paper)
29% identity, 95% coverage: 10:269/273 of query aligns to 3:245/245 of 5ugvA
5tjzA Structure of 4-hydroxytetrahydrodipicolinate reductase from mycobacterium tuberculosis with NADPH and 2,6 pyridine dicarboxylic acid (see paper)
29% identity, 95% coverage: 10:269/273 of query aligns to 3:245/245 of 5tjzA
- active site: H133 (= H161), K137 (= K165)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G15), G11 (= G18), K12 (≠ R19), V13 (≠ M20), D34 (= D41), A35 (= A43), F53 (= F81), T54 (= T82), G76 (= G104), T77 (= T105), T78 (= T106), P104 (= P129), N105 (= N130), F106 (≠ M131), F218 (≠ Y245)
- binding pyridine-2,6-dicarboxylic acid: T78 (= T106), P104 (= P129), H134 (= H162), K137 (= K165), S142 (= S170), G143 (= G171), T144 (= T172), A193 (≠ G220)
Query Sequence
>WP_068167655.1 NCBI__GCF_001592305.1:WP_068167655.1
MSAVSQGSHRVCVAGASGRMGQMLVEAVRDSTDCVLSGALDRAGSPAIGQDAGAFAGHTT
GVAINADLGAGLSGSRFLIDFTRPEGTLAHLRECVKLGVNVVIGTTGFSEAQKAEIADAA
KQIAIVMAPNMSVGVNVTLKLLEMAAKALATGYDIEIIEAHHRHKVDAPSGTALKMGEVI
AGALGRDLKDCAVYAREGVTGERDPSSIGFATIRGGDIVGDHTVLFAGTGERIEVTHKSS
SRVTYAQGSLRAVRFLADKRSGLYDMFDVLGLR
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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