SitesBLAST
Comparing WP_017751184.1 NCBI__GCF_000816635.1:WP_017751184.1 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)
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, 96% coverage: 8:247/251 of query aligns to 7:212/216 of Q9X1K8
1vm6B Crystal structure of dihydrodipicolinate reductase (tm1520) from thermotoga maritima at 2.27 a resolution
38% identity, 96% coverage: 8:247/251 of query aligns to 12:217/218 of 1vm6B
- active site: H132 (= H141), K136 (= K145)
- binding nicotinamide-adenine-dinucleotide: G12 (= G8), S14 (≠ N10), G15 (= G11), R16 (= R12), M17 (= M13), D37 (= D34), V38 (≠ R35), F53 (= F61), S54 (= S62), S55 (≠ R63), E57 (≠ D65), A58 (= A66), G76 (≠ C84), T78 (= T86), Y101 (≠ A109), N102 (= N110), F103 (≠ M111), F192 (= F222)
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
36% identity, 98% coverage: 1:247/251 of query aligns to 1:264/269 of 5tejB
- active site: H155 (= H141), K159 (= K145)
- binding 2,5 Furan Dicarboxylic Acid: T100 (= T86), H156 (= H142), K159 (= K145), S164 (= S150), G165 (= G151), T166 (= T152)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G11 (= G11), R12 (= R12), M13 (= M13), E34 (≠ D34), R35 (= R35), F75 (= F61), T76 (≠ S62), S80 (≠ D65), G98 (≠ C84), T100 (= T86), P123 (≠ A109), N124 (= N110), Y125 (≠ M111), F239 (= F222)
5tejA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
36% identity, 98% coverage: 1:247/251 of query aligns to 1:264/269 of 5tejA
- active site: H155 (= H141), K159 (= K145)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G11 (= G11), R12 (= R12), M13 (= M13), E34 (≠ D34), R35 (= R35), F75 (= F61), T76 (≠ S62), S80 (≠ D65), G98 (≠ C84), T100 (= T86), P123 (≠ A109)
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
36% identity, 98% coverage: 1:247/251 of query aligns to 1:264/266 of 5temA
- active site: H155 (= H141), K159 (= K145)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G11 (= G11), R12 (= R12), M13 (= M13), E34 (≠ D34), R35 (= R35), F75 (= F61), T76 (≠ S62), S80 (≠ D65), G98 (≠ C84), T100 (= T86), P123 (≠ A109), N124 (= N110), Y125 (≠ M111), F239 (= F222)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T86), P123 (≠ A109), H156 (= H142), K159 (= K145), S164 (= S150), G165 (= G151), T166 (= T152)
4ywjA Crystal structure of 4-hydroxy-tetrahydrodipicolinate reductase (htpa reductase) from pseudomonas aeruginosa
32% identity, 99% coverage: 1:248/251 of query aligns to 1:266/268 of 4ywjA
- active site: H156 (= H141), K160 (= K145)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), R12 (= R12), M13 (= M13), D35 (= D34), R36 (= R35), F76 (= F61), T77 (≠ S62), V81 (≠ A66), G99 (≠ C84), T101 (= T86), A124 (= A109), N125 (= N110), F126 (≠ M111), R237 (= R219), F240 (= F222)
3ijpA Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
36% identity, 98% coverage: 2:247/251 of query aligns to 2:264/266 of 3ijpA
- active site: H155 (= H141), K159 (= K145)
- binding sodium ion: I21 (≠ A21), Q22 (≠ N22), R24 (≠ I24), V27 (= V27)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G8), N10 (= N10), G11 (= G11), R12 (= R12), M13 (= M13), R35 (= R35), F75 (= F61), S76 (= S62), Q77 (≠ R63), A80 (= A66), G98 (≠ C84), T100 (= T86), G123 (≠ A109), N124 (= N110), M125 (= M111), F239 (= F222)
3ijpB Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
36% identity, 98% coverage: 2:247/251 of query aligns to 2:264/267 of 3ijpB
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
31% identity, 100% coverage: 2:251/251 of query aligns to 6:272/273 of P04036
- G12 (= G8) binding NADP(+)
- GRM 15:17 (= GRM 11:13) binding NAD(+)
- RM 16:17 (= RM 12:13) binding NADP(+)
- E38 (≠ D34) binding NAD(+)
- R39 (= R35) binding NADP(+)
- TR 80:81 (≠ SR 62:63) binding NAD(+)
- GTT 102:104 (≠ CTT 84:86) binding NAD(+); binding NADP(+)
- AANF 126:129 (≠ SANM 108:111) binding NAD(+)
- F129 (≠ M111) binding NADP(+)
- H159 (= H141) mutation H->A,Q: 135 to 200-fold reduction in catalytic activity.
- K163 (= K145) binding NAD(+); mutation K->A,C,Q: 625 to 830-fold reduction in catalytic activity.
- R240 (= R219) binding NADP(+)
- F243 (= F222) binding NAD(+)
1arzB Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
31% identity, 100% coverage: 2:251/251 of query aligns to 2:268/269 of 1arzB
- active site: H155 (= H141), K159 (= K145)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G8), G10 (≠ N10), G11 (= G11), R12 (= R12), M13 (= M13), E34 (≠ D34), F75 (= F61), T76 (≠ S62), R77 (= R63), G80 (≠ A66), H84 (≠ L70), G98 (≠ C84), T100 (= T86), A123 (= A109), N124 (= N110), F125 (≠ M111), F239 (= F222)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T86), H156 (= H142), K159 (= K145), S164 (= S150), G165 (= G151), T166 (= T152), F239 (= F222)
1drwA Escherichia coli dhpr/nhdh complex (see paper)
31% identity, 100% coverage: 2:251/251 of query aligns to 5:271/272 of 1drwA
- active site: H158 (= H141), K162 (= K145)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (= G8), G14 (= G11), R15 (= R12), M16 (= M13), E37 (≠ D34), R38 (= R35), F78 (= F61), T79 (≠ S62), R80 (= R63), G101 (≠ C84), T102 (= T85), T103 (= T86), A126 (= A109), N127 (= N110), F128 (≠ M111), F242 (= F222)
1drvA Escherichia coli dhpr/acnadh complex (see paper)
31% identity, 100% coverage: 2:251/251 of query aligns to 3:269/270 of 1drvA
- active site: H156 (= H141), K160 (= K145)
- binding 3-acetylpyridine adenine dinucleotide: G9 (= G8), G12 (= G11), R13 (= R12), M14 (= M13), E35 (≠ D34), F76 (= F61), T77 (≠ S62), R78 (= R63), G81 (≠ A66), G99 (≠ C84), A124 (= A109), F126 (≠ M111), R237 (= R219)
1druA Escherichia coli dhpr/nadh complex (see paper)
31% identity, 100% coverage: 2:251/251 of query aligns to 3:269/270 of 1druA
- active site: H156 (= H141), K160 (= K145)
- binding nicotinamide-adenine-dinucleotide: G9 (= G8), G12 (= G11), R13 (= R12), M14 (= M13), E35 (≠ D34), R36 (= R35), F76 (= F61), T77 (≠ S62), R78 (= R63), G81 (≠ A66), G99 (≠ C84), T100 (= T85), T101 (= T86), A124 (= A109), N125 (= N110), F126 (≠ M111), F240 (= F222)
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
31% identity, 100% coverage: 2:251/251 of query aligns to 5:271/272 of 1dihA
- active site: H158 (= H141), K162 (= K145)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G8), G14 (= G11), R15 (= R12), M16 (= M13), R38 (= R35), F78 (= F61), T79 (≠ S62), R80 (= R63), G83 (≠ A66), G101 (≠ C84), T103 (= T86), N127 (= N110), F128 (≠ M111), R239 (= R219), F242 (= F222)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
31% identity, 100% coverage: 2:251/251 of query aligns to 3:269/270 of 1arzA
5z2fA NADPH/pda bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
27% identity, 98% coverage: 1:247/251 of query aligns to 2:265/265 of 5z2fA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R11 (≠ N10), G12 (= G11), K13 (≠ R12), M14 (= M13), D35 (= D34), H36 (≠ R35), K37 (≠ N36), L76 (≠ F61), T77 (≠ S62), G99 (≠ C84), T100 (= T85), T101 (= T86), P126 (≠ A109), N127 (= N110), F128 (≠ M111)
- binding pyridine-2,6-dicarboxylic acid: P126 (≠ A109), H155 (= H141), H156 (= H142), K159 (= K145), S164 (= S150), G165 (= G151), T166 (= T152), A215 (≠ G197)
5z2eA Dipicolinate bound dihydrodipicolinate reductase from paenisporosarcina sp. Tg-14 (see paper)
27% identity, 98% coverage: 1:247/251 of query aligns to 2:265/265 of 5z2eA
5wolA Crystal structure of dihydrodipicolinate reductase dapb from coxiella burnetii
29% identity, 98% coverage: 2:247/251 of query aligns to 2:230/230 of 5wolA
- active site: H133 (= H141), K137 (= K145)
- binding pyridine-2-carboxylic acid: P104 (≠ A109), T144 (= T152), K147 (≠ L155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N7 (≠ S7), G11 (= G11), K12 (≠ R12), M13 (= M13), G34 (≠ D34), R35 (= R35), F54 (= F61), T55 (≠ S62), T56 (≠ R63), S59 (≠ A66), G77 (= G80), T78 (= T85), T79 (= T86), P104 (≠ A109), N105 (= N110), F106 (≠ M111)
1yl5A Crystal structure of mycobacterium tuberculosis dihydrodipicolinate reductase (rv2773c) (crystal form a) (see paper)
26% identity, 94% coverage: 1:236/251 of query aligns to 2:233/247 of 1yl5A
P9WP23 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
26% identity, 94% coverage: 2:236/251 of query aligns to 1:231/245 of P9WP23
- K9 (≠ N10) 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 (≠ R12) 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 12:13) binding NAD(+); binding NADP(+)
- D33 (= D34) binding NAD(+)
- GTT 75:77 (≠ CTT 84:86) binding NAD(+); binding NADP(+)
- APNF 102:105 (≠ SANM 108:111) binding NAD(+); binding NADP(+)
- K136 (= K145) binding NAD(+); binding NADP(+)
Query Sequence
>WP_017751184.1 NCBI__GCF_000816635.1:WP_017751184.1
MVKIILSGCNGRMGKVISKLANTIEDVSIVAGIDRNTEKSNYPIFASISDCNISADVILD
FSRPDALDSLIEYGKENNIGIVFCTTGYSDEQIKKINDLSKILPIFRSANMSIGINVVNN
ILKNISSLLYKNFDIEIVEKHHNQKVDSPSGTAILLADTIKDTIPDNIEFVNGREGIKKR
VHNEIGIHSIRGGSIVGEHEILFAGQGETIEIKHTAISREVFAIGALKACEFMYKKNAGL
YNMDNVISNDN
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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