SitesBLAST
Comparing WP_013536943.1 NCBI__GCF_000185805.1:WP_013536943.1 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
49% identity, 100% coverage: 1:260/260 of query aligns to 1:267/268 of 4ywjA
- active site: H156 (= H149), K160 (= K153)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), R12 (= R12), M13 (= M13), D35 (≠ E34), R36 (= R35), F76 (= F68), T77 (= T69), V81 (≠ A73), G99 (= G91), T101 (= T93), A124 (≠ P116), N125 (= N117), F126 (≠ M118), R237 (= R230), F240 (= F233)
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
45% identity, 100% coverage: 1:260/260 of query aligns to 1:266/269 of 5tejB
- active site: H155 (= H149), K159 (= K153)
- binding 2,5 Furan Dicarboxylic Acid: T100 (= T93), H156 (= H150), K159 (= K153), S164 (= S158), G165 (= G159), T166 (= T160)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G11 (= G11), R12 (= R12), M13 (= M13), E34 (= E34), R35 (= R35), F75 (= F68), T76 (= T69), S80 (≠ A73), G98 (= G91), T100 (= T93), P123 (= P116), N124 (= N117), Y125 (≠ M118), F239 (= F233)
5tejA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
45% identity, 100% coverage: 1:260/260 of query aligns to 1:266/269 of 5tejA
- active site: H155 (= H149), K159 (= K153)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G11 (= G11), R12 (= R12), M13 (= M13), E34 (= E34), R35 (= R35), F75 (= F68), T76 (= T69), S80 (≠ A73), G98 (= G91), T100 (= T93), P123 (= P116)
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
45% identity, 100% coverage: 1:260/260 of query aligns to 1:266/266 of 5temA
- active site: H155 (= H149), K159 (= K153)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G11 (= G11), R12 (= R12), M13 (= M13), E34 (= E34), R35 (= R35), F75 (= F68), T76 (= T69), S80 (≠ A73), G98 (= G91), T100 (= T93), P123 (= P116), N124 (= N117), Y125 (≠ M118), F239 (= F233)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T93), P123 (= P116), H156 (= H150), K159 (= K153), S164 (= S158), G165 (= G159), T166 (= T160)
1drvA Escherichia coli dhpr/acnadh complex (see paper)
45% identity, 99% coverage: 2:258/260 of query aligns to 3:265/270 of 1drvA
- active site: H156 (= H149), K160 (= K153)
- binding 3-acetylpyridine adenine dinucleotide: G9 (= G8), G12 (= G11), R13 (= R12), M14 (= M13), E35 (= E34), F76 (= F68), T77 (= T69), R78 (≠ T70), G81 (≠ A73), G99 (= G91), A124 (≠ P116), F126 (≠ M118), R237 (= R230)
1druA Escherichia coli dhpr/nadh complex (see paper)
45% identity, 99% coverage: 2:258/260 of query aligns to 3:265/270 of 1druA
- active site: H156 (= H149), K160 (= K153)
- binding nicotinamide-adenine-dinucleotide: G9 (= G8), G12 (= G11), R13 (= R12), M14 (= M13), E35 (= E34), R36 (= R35), F76 (= F68), T77 (= T69), R78 (≠ T70), G81 (≠ A73), G99 (= G91), T100 (= T92), T101 (= T93), A124 (≠ P116), N125 (= N117), F126 (≠ M118), F240 (= F233)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
45% identity, 99% coverage: 2:258/260 of query aligns to 3:265/270 of 1arzA
1drwA Escherichia coli dhpr/nhdh complex (see paper)
45% identity, 99% coverage: 2:258/260 of query aligns to 5:267/272 of 1drwA
- active site: H158 (= H149), K162 (= K153)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (= G8), G14 (= G11), R15 (= R12), M16 (= M13), E37 (= E34), R38 (= R35), F78 (= F68), T79 (= T69), R80 (≠ T70), G101 (= G91), T102 (= T92), T103 (= T93), A126 (≠ P116), N127 (= N117), F128 (≠ M118), F242 (= F233)
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
45% identity, 99% coverage: 2:258/260 of query aligns to 5:267/272 of 1dihA
- active site: H158 (= H149), K162 (= K153)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G8), G14 (= G11), R15 (= R12), M16 (= M13), R38 (= R35), F78 (= F68), T79 (= T69), R80 (≠ T70), G83 (≠ A73), G101 (= G91), T103 (= T93), N127 (= N117), F128 (≠ M118), R239 (= R230), F242 (= F233)
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
45% identity, 99% coverage: 2:258/260 of query aligns to 6:268/273 of P04036
- G12 (= G8) binding NADP(+)
- GRM 15:17 (= GRM 11:13) binding NAD(+)
- RM 16:17 (= RM 12:13) binding NADP(+)
- E38 (= E34) binding NAD(+)
- R39 (= R35) binding NADP(+)
- TR 80:81 (≠ TT 69:70) binding NAD(+)
- GTT 102:104 (= GTT 91:93) binding NAD(+); binding NADP(+)
- AANF 126:129 (≠ SPNM 115:118) binding NAD(+)
- F129 (≠ M118) binding NADP(+)
- H159 (= H149) mutation H->A,Q: 135 to 200-fold reduction in catalytic activity.
- K163 (= K153) binding NAD(+); mutation K->A,C,Q: 625 to 830-fold reduction in catalytic activity.
- R240 (= R230) binding NADP(+)
- F243 (= F233) binding NAD(+)
1arzB Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
45% identity, 99% coverage: 2:258/260 of query aligns to 2:264/269 of 1arzB
- active site: H155 (= H149), K159 (= K153)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G8), G10 (= G10), G11 (= G11), R12 (= R12), M13 (= M13), E34 (= E34), F75 (= F68), T76 (= T69), R77 (≠ T70), G80 (≠ A73), H84 (≠ L77), G98 (= G91), T100 (= T93), A123 (≠ P116), N124 (= N117), F125 (≠ M118), F239 (= F233)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T93), H156 (= H150), K159 (= K153), S164 (= S158), G165 (= G159), T166 (= T160), F239 (= F233)
3ijpA Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
39% identity, 100% coverage: 2:260/260 of query aligns to 2:266/266 of 3ijpA
- active site: H155 (= H149), K159 (= K153)
- binding sodium ion: I21 (≠ A21), Q22 (≠ L22), R24 (≠ D24), V27 (= V27)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G8), N10 (≠ G10), G11 (= G11), R12 (= R12), M13 (= M13), R35 (= R35), F75 (= F68), S76 (≠ T69), Q77 (≠ T70), A80 (= A73), G98 (= G91), T100 (= T93), G123 (≠ P116), N124 (= N117), M125 (= M118), F239 (= F233)
3ijpB Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
39% identity, 100% coverage: 2:260/260 of query aligns to 2:266/267 of 3ijpB
1vm6B Crystal structure of dihydrodipicolinate reductase (tm1520) from thermotoga maritima at 2.27 a resolution
38% identity, 99% coverage: 2:258/260 of query aligns to 6:217/218 of 1vm6B
- active site: H132 (= H149), K136 (= K153)
- binding nicotinamide-adenine-dinucleotide: G12 (= G8), S14 (≠ G10), G15 (= G11), R16 (= R12), M17 (= M13), D37 (≠ Y52), V38 (≠ P53), F53 (= F68), S54 (≠ T69), S55 (≠ T70), E57 (= E72), A58 (= A73), G76 (= G91), T78 (= T93), Y101 (≠ P116), N102 (= N117), F103 (≠ M118), F192 (= F233)
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, 99% coverage: 2:258/260 of query aligns to 1:212/216 of Q9X1K8
1yl5A Crystal structure of mycobacterium tuberculosis dihydrodipicolinate reductase (rv2773c) (crystal form a) (see paper)
31% identity, 97% coverage: 1:251/260 of query aligns to 2:236/247 of 1yl5A
5z2fA NADPH/pda bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
29% identity, 99% coverage: 1:258/260 of query aligns to 2:265/265 of 5z2fA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R11 (≠ G10), G12 (= G11), K13 (≠ R12), M14 (= M13), D35 (= D37), H36 (= H38), K37 (≠ P39), L76 (≠ F68), T77 (= T69), G99 (= G91), T100 (= T92), T101 (= T93), P126 (= P116), N127 (= N117), F128 (≠ M118)
- binding pyridine-2,6-dicarboxylic acid: P126 (= P116), H155 (= H149), H156 (= H150), K159 (= K153), S164 (= S158), G165 (= G159), T166 (= T160), A215 (≠ G208)
5z2eA Dipicolinate bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
29% identity, 99% coverage: 1:258/260 of query aligns to 2:265/265 of 5z2eA
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
31% identity, 96% coverage: 2:251/260 of query aligns to 1:234/245 of 1p9lA
- active site: H132 (= H149), K136 (= K153)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (= G8), G10 (= G11), K11 (≠ R12), V12 (≠ M13), D33 (≠ E34), A34 (≠ R35), F52 (= F68), T53 (= T69), V57 (≠ A73), G75 (= G91), T77 (= T93), P103 (= P116), N104 (= N117), F105 (≠ M118), F217 (= F233)
- binding pyridine-2,6-dicarboxylic acid: H133 (= H150), K136 (= K153), S141 (= S158), G142 (= G159), T143 (= T160), A192 (≠ G208)
1c3vA Dihydrodipicolinate reductase from mycobacterium tuberculosis complexed with NADPH and pdc (see paper)
31% identity, 96% coverage: 2:251/260 of query aligns to 1:234/245 of 1c3vA
- active site: H132 (= H149), K136 (= K153)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K9 (≠ G10), G10 (= G11), K11 (≠ R12), V12 (≠ M13), D33 (≠ E34), A34 (≠ R35), F52 (= F68), T53 (= T69), V57 (≠ A73), G75 (= G91), T77 (= T93), P103 (= P116), N104 (= N117), F217 (= F233)
- binding pyridine-2,6-dicarboxylic acid: T77 (= T93), N104 (= N117), K136 (= K153), S141 (= S158), G142 (= G159), T143 (= T160), A192 (≠ G208)
Query Sequence
>WP_013536943.1 NCBI__GCF_000185805.1:WP_013536943.1
MVKVAVTGAGGRMGSLIARLALEDEGVKLVGVTERPDHPLMGGEFAPGVKFYPSILQMEE
KPEVVIDFTTPEATLKLLEEAKELGTALVIGTTGFSAEQLSKVEEASKELPVLLSPNMSL
GVNLLFKLVAEAAKALKDKGYDVEIFEIHHRFKKDAPSGTAVKLGQIVAQAFGKSLKEMA
VYGRQGMVGPRKPDEMGILSARMGDVVGDHTVFFATLGERLELTHRATSRETFARGAIVA
AKWMAGKGPGLYSMFDVLGF
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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