SitesBLAST
Comparing Ac3H11_686 FitnessBrowser__acidovorax_3H11:Ac3H11_686 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)
1arzB Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
58% identity, 95% coverage: 16:279/279 of query aligns to 3:267/269 of 1arzB
- active site: H155 (= H167), K159 (= K171)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G21), G10 (≠ S23), G11 (= G24), R12 (= R25), M13 (= M26), E34 (≠ D47), F75 (= F87), T76 (= T88), R77 (= R89), G80 (= G92), H84 (= H96), G98 (= G110), T100 (= T112), A123 (≠ P135), N124 (= N136), F125 (≠ M137), F239 (≠ Y251)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T112), H156 (= H168), K159 (= K171), S164 (= S176), G165 (= G177), T166 (= T178), F239 (≠ Y251)
P04036 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Escherichia coli (strain K12) (see 3 papers)
58% identity, 95% coverage: 16:279/279 of query aligns to 7:271/273 of P04036
- G12 (= G21) binding
- GRM 15:17 (= GRM 24:26) binding
- RM 16:17 (= RM 25:26) binding
- E38 (≠ D47) binding
- R39 (≠ V48) binding
- TR 80:81 (= TR 88:89) binding
- GTT 102:104 (= GTT 110:112) binding ; binding
- AANF 126:129 (≠ SPNM 134:137) binding
- F129 (≠ M137) binding
- H159 (= H167) mutation H->A,Q: 135 to 200-fold reduction in catalytic activity.
- K163 (= K171) binding ; mutation K->A,C,Q: 625 to 830-fold reduction in catalytic activity.
- R240 (= R248) binding
- F243 (≠ Y251) binding
1drvA Escherichia coli dhpr/acnadh complex (see paper)
58% identity, 95% coverage: 16:279/279 of query aligns to 4:268/270 of 1drvA
- active site: H156 (= H167), K160 (= K171)
- binding 3-acetylpyridine adenine dinucleotide: G9 (= G21), G12 (= G24), R13 (= R25), M14 (= M26), E35 (≠ D47), F76 (= F87), T77 (= T88), R78 (= R89), G81 (= G92), G99 (= G110), A124 (≠ P135), F126 (≠ M137), R237 (= R248)
1druA Escherichia coli dhpr/nadh complex (see paper)
58% identity, 95% coverage: 16:279/279 of query aligns to 4:268/270 of 1druA
- active site: H156 (= H167), K160 (= K171)
- binding nicotinamide-adenine-dinucleotide: G9 (= G21), G12 (= G24), R13 (= R25), M14 (= M26), E35 (≠ D47), R36 (≠ V48), F76 (= F87), T77 (= T88), R78 (= R89), G81 (= G92), G99 (= G110), T100 (= T111), T101 (= T112), A124 (≠ P135), N125 (= N136), F126 (≠ M137), F240 (≠ Y251)
1arzA Escherichia coli dihydrodipicolinate reductase in complex with nadh and 2,6 pyridine dicarboxylate (see paper)
58% identity, 95% coverage: 16:279/279 of query aligns to 4:268/270 of 1arzA
1drwA Escherichia coli dhpr/nhdh complex (see paper)
58% identity, 95% coverage: 16:279/279 of query aligns to 6:270/272 of 1drwA
- active site: H158 (= H167), K162 (= K171)
- binding nicotinamide purin-6-ol-dinucleotide: G11 (= G21), G14 (= G24), R15 (= R25), M16 (= M26), E37 (≠ D47), R38 (≠ V48), F78 (= F87), T79 (= T88), R80 (= R89), G101 (= G110), T102 (= T111), T103 (= T112), A126 (≠ P135), N127 (= N136), F128 (≠ M137), F242 (≠ Y251)
1dihA Three-dimensional structure of e. Coli dihydrodipicolinate reductase (see paper)
58% identity, 95% coverage: 16:279/279 of query aligns to 6:270/272 of 1dihA
- active site: H158 (= H167), K162 (= K171)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G21), G14 (= G24), R15 (= R25), M16 (= M26), R38 (≠ V48), F78 (= F87), T79 (= T88), R80 (= R89), G83 (= G92), G101 (= G110), T103 (= T112), N127 (= N136), F128 (≠ M137), R239 (= R248), F242 (≠ Y251)
5tejB Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
52% identity, 95% coverage: 16:279/279 of query aligns to 3:267/269 of 5tejB
- active site: H155 (= H167), K159 (= K171)
- binding 2,5 Furan Dicarboxylic Acid: T100 (= T112), H156 (= H168), K159 (= K171), S164 (= S176), G165 (= G177), T166 (= T178)
- binding nicotinamide-adenine-dinucleotide: G8 (= G21), G11 (= G24), R12 (= R25), M13 (= M26), E34 (≠ D47), R35 (≠ V48), F75 (= F87), T76 (= T88), S80 (≠ G92), G98 (= G110), T100 (= T112), P123 (= P135), N124 (= N136), Y125 (≠ M137), F239 (≠ Y251)
5tejA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,5 furan dicarboxylic and nadh (see paper)
52% identity, 95% coverage: 16:279/279 of query aligns to 3:267/269 of 5tejA
- active site: H155 (= H167), K159 (= K171)
- binding nicotinamide-adenine-dinucleotide: G8 (= G21), G11 (= G24), R12 (= R25), M13 (= M26), E34 (≠ D47), R35 (≠ V48), F75 (= F87), T76 (= T88), S80 (≠ G92), G98 (= G110), T100 (= T112), P123 (= P135)
5temA Structure of 4-hydroxy-tetrahydrodipicolinate reductase from vibrio vulnificus with 2,6 pyridine dicarboxylic and nadh (see paper)
52% identity, 94% coverage: 16:278/279 of query aligns to 3:266/266 of 5temA
- active site: H155 (= H167), K159 (= K171)
- binding nicotinamide-adenine-dinucleotide: G8 (= G21), G11 (= G24), R12 (= R25), M13 (= M26), E34 (≠ D47), R35 (≠ V48), F75 (= F87), T76 (= T88), S80 (≠ G92), G98 (= G110), T100 (= T112), P123 (= P135), N124 (= N136), Y125 (≠ M137), F239 (≠ Y251)
- binding pyridine-2,6-dicarboxylic acid: T100 (= T112), P123 (= P135), H156 (= H168), K159 (= K171), S164 (= S176), G165 (= G177), T166 (= T178)
4ywjA Crystal structure of 4-hydroxy-tetrahydrodipicolinate reductase (htpa reductase) from pseudomonas aeruginosa
53% identity, 95% coverage: 16:279/279 of query aligns to 3:268/268 of 4ywjA
- active site: H156 (= H167), K160 (= K171)
- binding nicotinamide-adenine-dinucleotide: G11 (= G24), R12 (= R25), M13 (= M26), D35 (= D47), R36 (≠ V48), F76 (= F87), T77 (= T88), V81 (≠ G92), G99 (= G110), T101 (= T112), A124 (≠ P135), N125 (= N136), F126 (≠ M137), R237 (= R248), F240 (≠ Y251)
3ijpB Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
42% identity, 95% coverage: 16:279/279 of query aligns to 3:267/267 of 3ijpB
3ijpA Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0a resolution (see paper)
42% identity, 94% coverage: 16:278/279 of query aligns to 3:266/266 of 3ijpA
- active site: H155 (= H167), K159 (= K171)
- binding sodium ion: I21 (= I34), Q22 (≠ R35), R24 (≠ S37), V27 (≠ C40)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G21), N10 (≠ S23), G11 (= G24), R12 (= R25), M13 (= M26), R35 (≠ V48), F75 (= F87), S76 (≠ T88), Q77 (≠ R89), A80 (≠ G92), G98 (= G110), T100 (= T112), G123 (≠ P135), N124 (= N136), M125 (= M137), F239 (≠ Y251)
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, 77% coverage: 63:276/279 of query aligns to 24:212/216 of Q9X1K8
Sites not aligning to the query:
1p9lA Structure of m. Tuberculosis dihydrodipicolinate reductase in complex with nadh and 2,6 pdc (see paper)
29% identity, 95% coverage: 15:279/279 of query aligns to 1:245/245 of 1p9lA
- active site: H132 (= H167), K136 (= K171)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G7 (= G21), G10 (= G24), K11 (≠ R25), V12 (≠ M26), D33 (= D47), A34 (≠ V48), F52 (= F87), T53 (= T88), V57 (≠ G92), G75 (= G110), T77 (= T112), P103 (= P135), N104 (= N136), F105 (≠ M137), F217 (≠ Y251)
- binding pyridine-2,6-dicarboxylic acid: H133 (= H168), K136 (= K171), S141 (= S176), G142 (= G177), T143 (= T178), A192 (≠ G226)
1c3vA Dihydrodipicolinate reductase from mycobacterium tuberculosis complexed with NADPH and pdc (see paper)
29% identity, 95% coverage: 15:279/279 of query aligns to 1:245/245 of 1c3vA
- active site: H132 (= H167), K136 (= K171)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K9 (≠ S23), G10 (= G24), K11 (≠ R25), V12 (≠ M26), D33 (= D47), A34 (≠ V48), F52 (= F87), T53 (= T88), V57 (≠ G92), G75 (= G110), T77 (= T112), P103 (= P135), N104 (= N136), F217 (≠ Y251)
- binding pyridine-2,6-dicarboxylic acid: T77 (= T112), N104 (= N136), K136 (= K171), S141 (= S176), G142 (= G177), T143 (= T178), A192 (≠ G226)
1yl5A Crystal structure of mycobacterium tuberculosis dihydrodipicolinate reductase (rv2773c) (crystal form a) (see paper)
29% identity, 95% coverage: 15:279/279 of query aligns to 3:247/247 of 1yl5A
P9WP23 4-hydroxy-tetrahydrodipicolinate reductase; HTPA reductase; EC 1.17.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
29% identity, 95% coverage: 15:279/279 of query aligns to 1:245/245 of P9WP23
- K9 (≠ S23) 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 (≠ R25) 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 25:26) binding ; binding
- D33 (= D47) binding
- GTT 75:77 (= GTT 110:112) binding ; binding
- APNF 102:105 (≠ SPNM 134:137) binding ; binding
- K136 (= K171) binding ; binding
1vm6B Crystal structure of dihydrodipicolinate reductase (tm1520) from thermotoga maritima at 2.27 a resolution
31% identity, 77% coverage: 63:276/279 of query aligns to 29:217/218 of 1vm6B
- active site: H132 (= H167), K136 (= K171)
- binding nicotinamide-adenine-dinucleotide: D37 (≠ T71), V38 (≠ A72), F53 (= F87), S54 (≠ T88), S55 (≠ R89), E57 (= E91), A58 (≠ G92), G76 (= G110), T78 (= T112), Y101 (≠ P135), N102 (= N136), F103 (≠ M137), F192 (≠ Y251)
Sites not aligning to the query:
5ugvA Dapb from mycobacterium tuberculosis (see paper)
29% identity, 89% coverage: 15:263/279 of query aligns to 2:230/245 of 5ugvA
Query Sequence
>Ac3H11_686 FitnessBrowser__acidovorax_3H11:Ac3H11_686
MTGTPTPAATVTTPCRVAVAGASGRMGRMLIEAIRASDDCVLAGALDVAASPAVGSDATA
FLGHASGVAITADIAAGLKNADVLIDFTRPEGTLAHLAVCSQLGVKAVIGTTGFTDAQKA
ELDACAQRTAIMFSPNMSVGVNVTLKLLQMAAKAMTTGYDIEIIEAHHRHKVDAPSGTAL
KMGEVIAEAMGRDLKECAVYAREGVTGERDPSSIGFAAIRGGDIVGDHTVLFAGIGERIE
VTHKSSSRATYAQGALRAVRFLAAHKTGMFDMFDVLGLH
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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