SitesBLAST
Comparing WP_106714899.1 NCBI__GCF_003010935.1:WP_106714899.1 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)
3ijpB Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
59% identity, 97% coverage: 9:276/277 of query aligns to 1:267/267 of 3ijpB
3ijpA Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
59% identity, 96% coverage: 9:275/277 of query aligns to 1:266/266 of 3ijpA
- active site: H155 (= H164), K159 (= K168)
- binding sodium ion: I21 (= I29), Q22 (≠ H30), R24 (≠ T32), V27 (≠ A35)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G16), N10 (≠ A18), G11 (= G19), R12 (= R20), M13 (= M21), R35 (= R43), F75 (= F83), S76 (≠ T84), Q77 (≠ T85), A80 (= A88), G98 (= G106), T100 (= T108), G123 (= G131), N124 (= N132), M125 (= M133), F239 (= F248)
4ywjA Crystal structure of 4-hydroxy-tetrahydrodipicolinate reductase (htpa reductase) from pseudomonas aeruginosa
47% identity, 96% coverage: 11:275/277 of query aligns to 3:267/268 of 4ywjA
- active site: H156 (= H164), K160 (= K168)
- binding nicotinamide-adenine-dinucleotide: G11 (= G19), R12 (= R20), M13 (= M21), D35 (≠ E42), R36 (= R43), F76 (= F83), T77 (= T84), V81 (≠ A88), G99 (= G106), T101 (= T108), A124 (≠ G131), N125 (= N132), F126 (≠ M133), R237 (= R245), F240 (= F248)
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
44% identity, 96% coverage: 10:276/277 of query aligns to 2:267/269 of 5tejB
- active site: H155 (= H164), K159 (= K168)
- binding 2,5 Furan Dicarboxylic Acid: T100 (= T108), H156 (= H165), K159 (= K168), S164 (= S173), G165 (= G174), T166 (= T175)
- binding nicotinamide-adenine-dinucleotide: G8 (= G16), G11 (= G19), R12 (= R20), M13 (= M21), E34 (= E42), R35 (= R43), F75 (= F83), T76 (= T84), S80 (≠ A88), G98 (= G106), T100 (= T108), P123 (≠ G131), N124 (= N132), Y125 (≠ M133), F239 (= F248)
5tejA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
44% identity, 96% coverage: 10:276/277 of query aligns to 2:267/269 of 5tejA
- active site: H155 (= H164), K159 (= K168)
- binding nicotinamide-adenine-dinucleotide: G8 (= G16), G11 (= G19), R12 (= R20), M13 (= M21), E34 (= E42), R35 (= R43), F75 (= F83), T76 (= T84), S80 (≠ A88), G98 (= G106), T100 (= T108), P123 (≠ G131)
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
44% identity, 96% coverage: 10:275/277 of query aligns to 2:266/266 of 5temA
- active site: H155 (= H164), K159 (= K168)
- binding nicotinamide-adenine-dinucleotide: G8 (= G16), G11 (= G19), R12 (= R20), M13 (= M21), E34 (= E42), R35 (= R43), F75 (= F83), T76 (= T84), S80 (≠ A88), G98 (= G106), T100 (= T108), P123 (≠ G131), N124 (= N132), Y125 (≠ M133), F239 (= F248)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T108), P123 (≠ G131), H156 (= H165), K159 (= K168), S164 (= S173), G165 (= G174), T166 (= T175)
1drvA Escherichia coli dhpr/acnadh complex (see paper)
44% identity, 97% coverage: 10:277/277 of query aligns to 3:269/270 of 1drvA
- active site: H156 (= H164), K160 (= K168)
- binding 3-acetylpyridine adenine dinucleotide: G9 (= G16), G12 (= G19), R13 (= R20), M14 (= M21), E35 (= E42), F76 (= F83), T77 (= T84), R78 (≠ T85), G81 (≠ A88), G99 (= G106), A124 (≠ G131), F126 (≠ M133), R237 (= R245)
1druA Escherichia coli dhpr/nadh complex (see paper)
44% identity, 97% coverage: 10:277/277 of query aligns to 3:269/270 of 1druA
- active site: H156 (= H164), K160 (= K168)
- binding nicotinamide-adenine-dinucleotide: G9 (= G16), G12 (= G19), R13 (= R20), M14 (= M21), E35 (= E42), R36 (= R43), F76 (= F83), T77 (= T84), R78 (≠ T85), G81 (≠ A88), G99 (= G106), T100 (= T107), T101 (= T108), A124 (≠ G131), N125 (= N132), F126 (≠ M133), F240 (= F248)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
44% identity, 97% coverage: 10:277/277 of query aligns to 3:269/270 of 1arzA
1arzB Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
44% identity, 97% coverage: 10:277/277 of query aligns to 2:268/269 of 1arzB
- active site: H155 (= H164), K159 (= K168)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G16), G10 (≠ A18), G11 (= G19), R12 (= R20), M13 (= M21), E34 (= E42), F75 (= F83), T76 (= T84), R77 (≠ T85), G80 (≠ A88), H84 (≠ F92), G98 (= G106), T100 (= T108), A123 (≠ G131), N124 (= N132), F125 (≠ M133), F239 (= F248)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T108), H156 (= H165), K159 (= K168), S164 (= S173), G165 (= G174), T166 (= T175), F239 (= F248)
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
44% identity, 97% coverage: 10:277/277 of query aligns to 6:272/273 of P04036
- G12 (= G16) binding NADP(+)
- GRM 15:17 (= GRM 19:21) binding NAD(+)
- RM 16:17 (= RM 20:21) binding NADP(+)
- E38 (= E42) binding NAD(+)
- R39 (= R43) binding NADP(+)
- TR 80:81 (≠ TT 84:85) binding NAD(+)
- GTT 102:104 (= GTT 106:108) binding NAD(+); binding NADP(+)
- AANF 126:129 (≠ SGNM 130:133) binding NAD(+)
- F129 (≠ M133) binding NADP(+)
- H159 (= H164) mutation H->A,Q: 135 to 200-fold reduction in catalytic activity.
- K163 (= K168) binding NAD(+); mutation K->A,C,Q: 625 to 830-fold reduction in catalytic activity.
- R240 (= R245) binding NADP(+)
- F243 (= F248) binding NAD(+)
1drwA Escherichia coli dhpr/nhdh complex (see paper)
44% identity, 97% coverage: 10:277/277 of query aligns to 5:271/272 of 1drwA
- active site: H158 (= H164), K162 (= K168)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (= G16), G14 (= G19), R15 (= R20), M16 (= M21), E37 (= E42), R38 (= R43), F78 (= F83), T79 (= T84), R80 (≠ T85), G101 (= G106), T102 (= T107), T103 (= T108), A126 (≠ G131), N127 (= N132), F128 (≠ M133), F242 (= F248)
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
44% identity, 97% coverage: 10:277/277 of query aligns to 5:271/272 of 1dihA
- active site: H158 (= H164), K162 (= K168)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G16), G14 (= G19), R15 (= R20), M16 (= M21), R38 (= R43), F78 (= F83), T79 (= T84), R80 (≠ T85), G83 (≠ A88), G101 (= G106), T103 (= T108), N127 (= N132), F128 (≠ M133), R239 (= R245), F242 (= F248)
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)
31% identity, 95% coverage: 10:273/277 of query aligns to 1:212/216 of Q9X1K8
1vm6B Crystal structure of dihydrodipicolinate reductase (tm1520) from thermotoga maritima at 2.27 a resolution
31% identity, 95% coverage: 10:273/277 of query aligns to 6:217/218 of 1vm6B
- active site: H132 (= H164), K136 (= K168)
- binding nicotinamide-adenine-dinucleotide: G12 (= G16), S14 (≠ A18), G15 (= G19), R16 (= R20), M17 (= M21), D37 (≠ E42), V38 (≠ L56), F53 (= F83), S54 (≠ T84), S55 (≠ T85), E57 (≠ A87), A58 (= A88), G76 (= G106), T78 (= T108), Y101 (≠ G131), N102 (= N132), F103 (≠ M133), F192 (= F248)
5eesA Crystal structure of dapb in complex with NADP+ from corynebacterium glutamicum (see paper)
30% identity, 96% coverage: 10:275/277 of query aligns to 2:247/247 of 5eesA
- active site: H133 (= H164), K137 (= K168)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G16), G11 (= G19), R12 (= R20), V13 (≠ M21), G34 (= G60), V35 (≠ I66), F53 (= F83), T54 (= T84), G76 (= G106), T78 (= T108), P104 (≠ G131), N105 (= N132), F106 (≠ M133), F220 (= F248)
- binding sulfate ion: H134 (= H165), K137 (= K168), K137 (= K168), G143 (= G174), T144 (= T175)
5eerA Crystal structure of dapb from corynebacterium glutamicum (see paper)
30% identity, 96% coverage: 10:275/277 of query aligns to 2:247/247 of 5eerA
5z2fA NADPH/pda bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
27% identity, 87% coverage: 10:251/277 of query aligns to 3:243/265 of 5z2fA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R11 (≠ A18), G12 (= G19), K13 (≠ R20), M14 (= M21), D35 (≠ E42), H36 (≠ R43), K37 (≠ V44), L76 (≠ F83), T77 (= T84), G99 (= G106), T100 (= T107), T101 (= T108), P126 (≠ G131), N127 (= N132), F128 (≠ M133)
- binding pyridine-2,6-dicarboxylic acid: P126 (≠ G131), H155 (= H164), H156 (= H165), K159 (= K168), S164 (= S173), G165 (= G174), T166 (= T175), A215 (≠ G223)
5z2eA Dipicolinate bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
27% identity, 87% coverage: 10:251/277 of query aligns to 3:243/265 of 5z2eA
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
29% identity, 95% coverage: 10:273/277 of query aligns to 1:241/245 of 1p9lA
- active site: H132 (= H164), K136 (= K168)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (= G16), G10 (= G19), K11 (≠ R20), V12 (≠ M21), D33 (≠ E42), A34 (≠ R43), F52 (= F83), T53 (= T84), V57 (≠ A88), G75 (= G106), T77 (= T108), P103 (≠ G131), N104 (= N132), F105 (≠ M133), F217 (= F248)
- binding pyridine-2,6-dicarboxylic acid: H133 (= H165), K136 (= K168), S141 (= S173), G142 (= G174), T143 (= T175), A192 (≠ G223)
Query Sequence
>WP_106714899.1 NCBI__GCF_003010935.1:WP_106714899.1
MSDVEQPTPMKLAVVGAAGRMGQTLIRIIHSTPGAMLSGAIERVGSPHIGSDAGVLAGVG
KLGVPISDDALAAFAGVEGVLDFTTPAASVEFAGLAAQTGIVHVVGTTGCDSTDDAKIAL
AARHAVVIKSGNMSLGVNLLAVLVKQAAKALGADDFDVEILEMHHKHKVDAPSGTALLLG
EAAAEGRNIGLGQHSVRVRDGHTGAREAGTIGFASLRGGSVVGDHSVILAGQGERITLSH
HAEDRSIFARGAVKAALWGRGRKPGLYTMLDVLGLDT
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