SitesBLAST
Comparing WP_012501610.1 NCBI__GCF_000020505.1:WP_012501610.1 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)
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
38% identity, 81% coverage: 46:246/249 of query aligns to 70:269/269 of 5tejB
- active site: H155 (= H134), K159 (= K138)
- binding 2,5 Furan Dicarboxylic Acid: T100 (= T76), H156 (= H135), K159 (= K138), S164 (= S143), G165 (= G144), T166 (= T145)
- binding nicotinamide-adenine-dinucleotide: F75 (= F51), T76 (= T52), S80 (≠ A56), G98 (= G74), T100 (= T76), P123 (≠ A100), N124 (= N101), Y125 (≠ F102), F239 (= F215)
Sites not aligning to the query:
5tejA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
38% identity, 81% coverage: 46:246/249 of query aligns to 70:269/269 of 5tejA
Sites not aligning to the query:
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
37% identity, 80% coverage: 46:244/249 of query aligns to 70:265/266 of 5temA
- active site: H155 (= H134), K159 (= K138)
- binding nicotinamide-adenine-dinucleotide: F75 (= F51), T76 (= T52), S80 (≠ A56), G98 (= G74), T100 (= T76), P123 (≠ A100), N124 (= N101), Y125 (≠ F102), F239 (= F215)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T76), P123 (≠ A100), H156 (= H135), K159 (= K138), S164 (= S143), G165 (= G144), T166 (= T145)
Sites not aligning to the query:
4ywjA Crystal structure of 4-hydroxy-tetrahydrodipicolinate reductase (htpa reductase) from pseudomonas aeruginosa
34% identity, 82% coverage: 40:244/249 of query aligns to 65:266/268 of 4ywjA
- active site: H156 (= H134), K160 (= K138)
- binding nicotinamide-adenine-dinucleotide: F76 (= F51), T77 (= T52), V81 (≠ A56), G99 (= G74), T101 (= T76), A124 (= A100), N125 (= N101), F126 (= F102), R237 (= R212), F240 (= F215)
Sites not aligning to the query:
1drwA Escherichia coli dhpr/nhdh complex (see paper)
33% identity, 80% coverage: 46:244/249 of query aligns to 73:268/272 of 1drwA
- active site: H158 (= H134), K162 (= K138)
- binding nicotinamide purin-6-ol-dinucleotide: F78 (= F51), T79 (= T52), R80 (≠ V53), G101 (= G74), T102 (= T75), T103 (= T76), A126 (= A100), N127 (= N101), F128 (= F102), F242 (= F215)
Sites not aligning to the query:
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
33% identity, 80% coverage: 46:244/249 of query aligns to 73:268/272 of 1dihA
- active site: H158 (= H134), K162 (= K138)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: F78 (= F51), T79 (= T52), R80 (≠ V53), G83 (≠ A56), G101 (= G74), T103 (= T76), N127 (= N101), F128 (= F102), R239 (= R212), F242 (= F215)
Sites not aligning to the query:
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
33% identity, 80% coverage: 46:244/249 of query aligns to 74:269/273 of P04036
- TR 80:81 (≠ TV 52:53) binding
- GTT 102:104 (= GTT 74:76) binding ; binding
- AANF 126:129 (≠ SANF 99:102) binding
- F129 (= F102) binding
- H159 (= H134) mutation H->A,Q: 135 to 200-fold reduction in catalytic activity.
- K163 (= K138) binding ; mutation K->A,C,Q: 625 to 830-fold reduction in catalytic activity.
- R240 (= R212) binding
- F243 (= F215) binding
Sites not aligning to the query:
- 12 binding
- 15:17 binding
- 16:17 binding
- 38 binding
- 39 binding
1drvA Escherichia coli dhpr/acnadh complex (see paper)
33% identity, 80% coverage: 46:244/249 of query aligns to 71:266/270 of 1drvA
Sites not aligning to the query:
1druA Escherichia coli dhpr/nadh complex (see paper)
33% identity, 80% coverage: 46:244/249 of query aligns to 71:266/270 of 1druA
- active site: H156 (= H134), K160 (= K138)
- binding nicotinamide-adenine-dinucleotide: F76 (= F51), T77 (= T52), R78 (≠ V53), G81 (≠ A56), G99 (= G74), T100 (= T75), T101 (= T76), A124 (= A100), N125 (= N101), F126 (= F102), F240 (= F215)
Sites not aligning to the query:
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
33% identity, 80% coverage: 46:244/249 of query aligns to 71:266/270 of 1arzA
1arzB Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
33% identity, 80% coverage: 46:244/249 of query aligns to 70:265/269 of 1arzB
- active site: H155 (= H134), K159 (= K138)
- binding 1,4-dihydronicotinamide adenine dinucleotide: F75 (= F51), T76 (= T52), R77 (≠ V53), G80 (≠ A56), H84 (≠ N60), G98 (= G74), T100 (= T76), A123 (= A100), N124 (= N101), F125 (= F102), F239 (= F215)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T76), H156 (= H135), K159 (= K138), S164 (= S143), G165 (= G144), T166 (= T145), F239 (= F215)
Sites not aligning to the query:
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, 98% coverage: 1:243/249 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, 98% coverage: 1:243/249 of query aligns to 6:217/218 of 1vm6B
- active site: H132 (= H134), K136 (= K138)
- binding nicotinamide-adenine-dinucleotide: G12 (= G7), S14 (≠ N8), G15 (= G9), R16 (= R10), M17 (= M11), D37 (= D32), V38 (= V33), F53 (= F51), S54 (≠ T52), S55 (≠ V53), E57 (≠ D55), A58 (= A56), G76 (= G74), T78 (= T76), Y101 (≠ A100), N102 (= N101), F103 (= F102), F192 (= F215)
3ijpB Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
32% identity, 98% coverage: 1:243/249 of query aligns to 2:264/267 of 3ijpB
3ijpA Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
32% identity, 98% coverage: 1:243/249 of query aligns to 2:264/266 of 3ijpA
- active site: H155 (= H134), K159 (= K138)
- binding sodium ion: I21 (≠ V19), Q22 (≠ N20), R24 (vs. gap), V27 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G7), N10 (= N8), G11 (= G9), R12 (= R10), M13 (= M11), R35 (vs. gap), F75 (= F51), S76 (≠ T52), Q77 (≠ V53), A80 (= A56), G98 (= G74), T100 (= T76), G123 (≠ A100), N124 (= N101), M125 (≠ F102), F239 (= F215)
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
29% identity, 99% coverage: 1:246/249 of query aligns to 1:244/245 of 1p9lA
- active site: H132 (= H134), K136 (= K138)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (= G7), G10 (= G9), K11 (≠ R10), V12 (≠ M11), D33 (= D32), A34 (≠ V33), F52 (= F51), T53 (= T52), V57 (≠ A56), G75 (= G74), T77 (= T76), P103 (≠ A100), N104 (= N101), F105 (= F102), F217 (= F215)
- binding pyridine-2,6-dicarboxylic acid: H133 (= H135), K136 (= K138), S141 (= S143), G142 (= G144), T143 (= T145), A192 (≠ G190)
1c3vA Dihydrodipicolinate reductase from mycobacterium tuberculosis complexed with NADPH and pdc (see paper)
29% identity, 99% coverage: 1:246/249 of query aligns to 1:244/245 of 1c3vA
- active site: H132 (= H134), K136 (= K138)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K9 (≠ N8), G10 (= G9), K11 (≠ R10), V12 (≠ M11), D33 (= D32), A34 (≠ V33), F52 (= F51), T53 (= T52), V57 (≠ A56), G75 (= G74), T77 (= T76), P103 (≠ A100), N104 (= N101), F217 (= F215)
- binding pyridine-2,6-dicarboxylic acid: T77 (= T76), N104 (= N101), K136 (= K138), S141 (= S143), G142 (= G144), T143 (= T145), A192 (≠ G190)
P9WP23 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
29% identity, 99% coverage: 1:246/249 of query aligns to 1:244/245 of P9WP23
- K9 (≠ N8) 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 (≠ R10) 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 10:11) binding ; binding
- D33 (= D32) binding
- GTT 75:77 (= GTT 74:76) binding ; binding
- APNF 102:105 (≠ SANF 99:102) binding ; binding
- K136 (= K138) binding ; binding
5ugvA Dapb from mycobacterium tuberculosis (see paper)
29% identity, 99% coverage: 1:246/249 of query aligns to 2:245/245 of 5ugvA
5tjzA Structure of 4-hydroxytetrahydrodipicolinate reductase from mycobacterium tuberculosis with NADPH and 2,6 pyridine dicarboxylic acid (see paper)
29% identity, 99% coverage: 1:246/249 of query aligns to 2:245/245 of 5tjzA
- active site: H133 (= H134), K137 (= K138)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G7), G11 (= G9), K12 (≠ R10), V13 (≠ M11), D34 (= D32), A35 (≠ V33), F53 (= F51), T54 (= T52), G76 (= G74), T77 (= T75), T78 (= T76), P104 (≠ A100), N105 (= N101), F106 (= F102), F218 (= F215)
- binding pyridine-2,6-dicarboxylic acid: T78 (= T76), P104 (≠ A100), H134 (= H135), K137 (= K138), S142 (= S143), G143 (= G144), T144 (= T145), A193 (≠ G190)
Query Sequence
>WP_012501610.1 NCBI__GCF_000020505.1:WP_012501610.1
MKVTLVGNGRMGQQIAGIVNASDANVIHKVLDVSDAVTPEVFEGSDAIIDFTVRDAFLAN
YKAMIASGVPVVVGTTGWDELMPQIAEEVNAAGSSMLYSANFSLGVNVFFRTLREAARLI
APFEQFDIALSEQHHTGKADFPSGTAIKAAQEVLNNNPRKRTIVRELEDGKKLQSDELQV
SSIRLGTVFGVHSAIIDSESDTIELTHTAKNRTGFASGAVRAAEWLAQQHAAKPGFYTMD
DFLNDLFSA
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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