SitesBLAST
Comparing WP_009567628.1 NCBI__GCF_000021485.1:WP_009567628.1 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, 96% coverage: 6:270/276 of query aligns to 3:268/268 of 4ywjA
- active site: H156 (= H158), K160 (= K162)
- binding nicotinamide-adenine-dinucleotide: G11 (= G14), R12 (= R15), M13 (= M16), D35 (≠ G37), R36 (= R38), F76 (= F78), T77 (≠ G79), V81 (≠ A83), G99 (= G101), T101 (= T103), A124 (≠ P126), N125 (= N127), F126 (≠ M128), R237 (= R239), F240 (= F242)
1arzB Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
49% identity, 97% coverage: 6:272/276 of query aligns to 3:269/269 of 1arzB
- active site: H155 (= H158), K159 (= K162)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (≠ A11), G10 (≠ A13), G11 (= G14), R12 (= R15), M13 (= M16), E34 (≠ G37), F75 (= F78), T76 (≠ G79), R77 (≠ P80), G80 (≠ A83), H84 (= H87), G98 (= G101), T100 (= T103), A123 (≠ P126), N124 (= N127), F125 (≠ M128), F239 (= F242)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T103), H156 (= H159), K159 (= K162), S164 (= S167), G165 (= G168), T166 (= T169), F239 (= F242)
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
49% identity, 97% coverage: 6:272/276 of query aligns to 7:273/273 of P04036
- G12 (≠ A11) binding NADP(+)
- GRM 15:17 (= GRM 14:16) binding NAD(+)
- RM 16:17 (= RM 15:16) binding NADP(+)
- E38 (≠ G37) binding NAD(+)
- R39 (= R38) binding NADP(+)
- TR 80:81 (≠ GP 79:80) binding NAD(+)
- GTT 102:104 (= GTT 101:103) binding NAD(+); binding NADP(+)
- AANF 126:129 (≠ APNM 125:128) binding NAD(+)
- F129 (≠ M128) binding NADP(+)
- H159 (= H158) mutation H->A,Q: 135 to 200-fold reduction in catalytic activity.
- K163 (= K162) binding NAD(+); mutation K->A,C,Q: 625 to 830-fold reduction in catalytic activity.
- R240 (= R239) binding NADP(+)
- F243 (= F242) binding NAD(+)
1drvA Escherichia coli dhpr/acnadh complex (see paper)
49% identity, 97% coverage: 6:272/276 of query aligns to 4:270/270 of 1drvA
- active site: H156 (= H158), K160 (= K162)
- binding 3-acetylpyridine adenine dinucleotide: G9 (≠ A11), G12 (= G14), R13 (= R15), M14 (= M16), E35 (≠ G37), F76 (= F78), T77 (≠ G79), R78 (≠ P80), G81 (≠ A83), G99 (= G101), A124 (≠ P126), F126 (≠ M128), R237 (= R239)
1druA Escherichia coli dhpr/nadh complex (see paper)
49% identity, 97% coverage: 6:272/276 of query aligns to 4:270/270 of 1druA
- active site: H156 (= H158), K160 (= K162)
- binding nicotinamide-adenine-dinucleotide: G9 (≠ A11), G12 (= G14), R13 (= R15), M14 (= M16), E35 (≠ G37), R36 (= R38), F76 (= F78), T77 (≠ G79), R78 (≠ P80), G81 (≠ A83), G99 (= G101), T100 (= T102), T101 (= T103), A124 (≠ P126), N125 (= N127), F126 (≠ M128), F240 (= F242)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
49% identity, 97% coverage: 6:272/276 of query aligns to 4:270/270 of 1arzA
1drwA Escherichia coli dhpr/nhdh complex (see paper)
49% identity, 97% coverage: 6:272/276 of query aligns to 6:272/272 of 1drwA
- active site: H158 (= H158), K162 (= K162)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (≠ A11), G14 (= G14), R15 (= R15), M16 (= M16), E37 (≠ G37), R38 (= R38), F78 (= F78), T79 (≠ G79), R80 (≠ P80), G101 (= G101), T102 (= T102), T103 (= T103), A126 (≠ P126), N127 (= N127), F128 (≠ M128), F242 (= F242)
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
49% identity, 97% coverage: 6:272/276 of query aligns to 6:272/272 of 1dihA
- active site: H158 (= H158), K162 (= K162)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (≠ A11), G14 (= G14), R15 (= R15), M16 (= M16), R38 (= R38), F78 (= F78), T79 (≠ G79), R80 (≠ P80), G83 (≠ A83), G101 (= G101), T103 (= T103), N127 (= N127), F128 (≠ M128), R239 (= R239), F242 (= F242)
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
44% identity, 97% coverage: 6:272/276 of query aligns to 3:269/269 of 5tejB
- active site: H155 (= H158), K159 (= K162)
- binding 2,5 Furan Dicarboxylic Acid: T100 (= T103), H156 (= H159), K159 (= K162), S164 (= S167), G165 (= G168), T166 (= T169)
- binding nicotinamide-adenine-dinucleotide: G8 (≠ A11), G11 (= G14), R12 (= R15), M13 (= M16), E34 (≠ G37), R35 (= R38), F75 (= F78), T76 (≠ G79), S80 (≠ A83), G98 (= G101), T100 (= T103), P123 (= P126), N124 (= N127), Y125 (≠ M128), F239 (= F242)
5tejA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
44% identity, 97% coverage: 6:272/276 of query aligns to 3:269/269 of 5tejA
- active site: H155 (= H158), K159 (= K162)
- binding nicotinamide-adenine-dinucleotide: G8 (≠ A11), G11 (= G14), R12 (= R15), M13 (= M16), E34 (≠ G37), R35 (= R38), F75 (= F78), T76 (≠ G79), S80 (≠ A83), G98 (= G101), T100 (= T103), P123 (= P126)
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
44% identity, 96% coverage: 6:269/276 of query aligns to 3:266/266 of 5temA
- active site: H155 (= H158), K159 (= K162)
- binding nicotinamide-adenine-dinucleotide: G8 (≠ A11), G11 (= G14), R12 (= R15), M13 (= M16), E34 (≠ G37), R35 (= R38), F75 (= F78), T76 (≠ G79), S80 (≠ A83), G98 (= G101), T100 (= T103), P123 (= P126), N124 (= N127), Y125 (≠ M128), F239 (= F242)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T103), P123 (= P126), H156 (= H159), K159 (= K162), S164 (= S167), G165 (= G168), T166 (= T169)
3ijpB Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
39% identity, 96% coverage: 6:270/276 of query aligns to 3:267/267 of 3ijpB
3ijpA Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
39% identity, 96% coverage: 6:269/276 of query aligns to 3:266/266 of 3ijpA
- active site: H155 (= H158), K159 (= K162)
- binding sodium ion: I21 (= I24), Q22 (≠ V25), R24 (≠ H27), V27 (≠ L30)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (≠ A11), N10 (≠ A13), G11 (= G14), R12 (= R15), M13 (= M16), R35 (= R38), F75 (= F78), S76 (≠ G79), Q77 (≠ P80), A80 (= A83), G98 (= G101), T100 (= T103), G123 (≠ P126), N124 (= N127), M125 (= M128), F239 (= F242)
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)
33% identity, 95% coverage: 6:267/276 of query aligns to 2:212/216 of Q9X1K8
1vm6B Crystal structure of dihydrodipicolinate reductase (tm1520) from thermotoga maritima at 2.27 a resolution
33% identity, 95% coverage: 6:267/276 of query aligns to 7:217/218 of 1vm6B
- active site: H132 (= H158), K136 (= K162)
- binding nicotinamide-adenine-dinucleotide: G12 (≠ A11), S14 (≠ A13), G15 (= G14), R16 (= R15), M17 (= M16), D37 (≠ G37), V38 (≠ L51), F53 (= F78), S54 (≠ G79), S55 (≠ P80), E57 (= E82), A58 (= A83), G76 (= G101), T78 (= T103), Y101 (≠ P126), N102 (= N127), F103 (≠ M128), F192 (= F242)
5z2fA NADPH/pda bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
23% identity, 95% coverage: 6:267/276 of query aligns to 4:265/265 of 5z2fA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R11 (≠ A13), G12 (= G14), K13 (≠ R15), M14 (= M16), D35 (≠ G37), H36 (≠ R38), K37 (≠ S39), L76 (≠ F78), T77 (≠ G79), G99 (= G101), T100 (= T102), T101 (= T103), P126 (= P126), N127 (= N127), F128 (≠ M128)
- binding pyridine-2,6-dicarboxylic acid: P126 (= P126), H155 (= H158), H156 (= H159), K159 (= K162), S164 (= S167), G165 (= G168), T166 (= T169), A215 (≠ G217)
5z2eA Dipicolinate bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
23% identity, 95% coverage: 6:267/276 of query aligns to 4:265/265 of 5z2eA
5wolA Crystal structure of dihydrodipicolinate reductase dapb from coxiella burnetii
26% identity, 85% coverage: 6:239/276 of query aligns to 3:202/230 of 5wolA
- active site: H133 (= H158), K137 (= K162)
- binding pyridine-2-carboxylic acid: P104 (= P126), T144 (= T169), K147 (≠ A172)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N7 (≠ T10), G11 (= G14), K12 (≠ R15), M13 (= M16), G34 (= G37), R35 (= R38), F54 (= F78), T55 (≠ G79), T56 (≠ P80), S59 (≠ A83), G77 (= G101), T78 (= T102), T79 (= T103), P104 (= P126), N105 (= N127), F106 (≠ M128)
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
29% identity, 92% coverage: 6:260/276 of query aligns to 2:234/245 of 1p9lA
- active site: H132 (= H158), K136 (= K162)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (≠ A11), G10 (= G14), K11 (≠ R15), V12 (≠ M16), D33 (= D47), A34 (= A48), F52 (= F78), T53 (≠ G79), V57 (≠ A83), G75 (= G101), T77 (= T103), P103 (= P126), N104 (= N127), F105 (≠ M128), F217 (= F242)
- binding pyridine-2,6-dicarboxylic acid: H133 (= H159), K136 (= K162), S141 (= S167), G142 (= G168), T143 (= T169), A192 (vs. gap)
1c3vA Dihydrodipicolinate reductase from mycobacterium tuberculosis complexed with NADPH and pdc (see paper)
29% identity, 92% coverage: 6:260/276 of query aligns to 2:234/245 of 1c3vA
- active site: H132 (= H158), K136 (= K162)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K9 (≠ A13), G10 (= G14), K11 (≠ R15), V12 (≠ M16), D33 (= D47), A34 (= A48), F52 (= F78), T53 (≠ G79), V57 (≠ A83), G75 (= G101), T77 (= T103), P103 (= P126), N104 (= N127), F217 (= F242)
- binding pyridine-2,6-dicarboxylic acid: T77 (= T103), N104 (= N127), K136 (= K162), S141 (= S167), G142 (= G168), T143 (= T169), A192 (vs. gap)
Query Sequence
>WP_009567628.1 NCBI__GCF_000021485.1:WP_009567628.1
MAGVWRVGVTAVAGRMGRALVQAIVAHPELQLVAAIGRSGAAYLGEDAGRLAGVQALGLP
VTADLGGALADLDVLIEFGPVEAALAHVAACVAVAKPVVVGTTGFSMNQRAELENASRHI
PLVLAPNMSVGVNVLLAFLPAITAALGDGYDVEIVEAHHRHKMDAPSGTALALGRAVAKG
RGQRLDEVQCLDRNGIPGPRMAGSIGFATLRGADVVGEHTVWMAGTGERLELTHRASSRL
NFAEGALRAASWLRGRAPGLYDMQDVLGLKGLTALQ
Or try a new SitesBLAST search
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