SitesBLAST
Comparing PP_3970 FitnessBrowser__Putida:PP_3970 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)
4cpdA Alcohol dehydrogenase tadh from thermus sp. Atn1
39% identity, 97% coverage: 1:387/400 of query aligns to 1:344/346 of 4cpdA
- active site: C38 (= C38), G39 (= G39), S40 (= S40), H43 (= H43), H59 (= H60), E60 (= E61), C89 (= C90), C92 (= C93), C95 (= C96), C103 (= C104), G107 (≠ S113), D152 (= D170), T156 (= T174), K340 (= K383)
- binding nicotinamide-adenine-dinucleotide: G39 (= G39), S40 (= S40), T156 (= T174), G178 (= G196), P179 (= P197), V180 (= V198), D200 (= D218), R201 (≠ D219), R205 (= R223), A243 (= A264), V244 (= V265), V266 (≠ P307), V268 (= V309), L292 (≠ Q333), A293 (≠ T334), F333 (= F374)
- binding zinc ion: C38 (= C38), H59 (= H60), C89 (= C90), C92 (= C93), C95 (= C96), C103 (= C104), D152 (= D170)
4jlwA Crystal structure of formaldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
36% identity, 94% coverage: 2:375/400 of query aligns to 3:379/395 of 4jlwA
- binding nicotinamide-adenine-dinucleotide: C45 (= C38), G46 (= G39), S47 (= S40), H50 (= H43), D168 (= D170), T172 (= T174), G194 (= G196), P195 (= P197), V196 (= V198), D216 (= D218), R221 (= R223), V261 (= V265), R266 (≠ K270), H268 (≠ S272), V281 (≠ A290), P298 (= P307), L300 (≠ V309), Q336 (= Q333), T337 (= T334)
- binding zinc ion: C45 (= C38), H66 (= H60), C96 (= C90), C99 (= C93), C102 (= C96), C110 (= C104), D168 (= D170)
1kolA Crystal structure of formaldehyde dehydrogenase (see paper)
35% identity, 94% coverage: 2:375/400 of query aligns to 3:379/396 of 1kolA
- active site: C45 (= C38), G46 (= G39), S47 (= S40), H50 (= H43), H66 (= H60), E67 (= E61), C96 (= C90), C99 (= C93), C102 (= C96), C110 (= C104), N114 (= N108), D168 (= D170), T172 (= T174)
- binding nicotinamide-adenine-dinucleotide: C45 (= C38), G46 (= G39), S47 (= S40), H50 (= H43), F92 (= F86), D168 (= D170), T172 (= T174), G192 (= G194), G194 (= G196), P195 (= P197), V196 (= V198), D216 (= D218), L217 (≠ D219), R221 (= R223), A260 (= A264), V261 (= V265), R266 (≠ K270), H268 (≠ S272), V281 (≠ A290), P298 (= P307), L300 (≠ V309), Q336 (= Q333), T337 (= T334)
- binding zinc ion: C45 (= C38), H66 (= H60), C96 (= C90), C99 (= C93), C102 (= C96), C110 (= C104), D168 (= D170)
Sites not aligning to the query:
P46154 Glutathione-independent formaldehyde dehydrogenase; FALDH; FDH; Formaldehyde dismutase; EC 1.2.1.46; EC 1.2.98.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see paper)
35% identity, 94% coverage: 2:375/400 of query aligns to 5:381/399 of P46154
5ylnA Zinc dependent alcohol dehydrogenase 2 from streptococcus pneumonia - apo form
30% identity, 97% coverage: 1:386/400 of query aligns to 5:341/348 of 5ylnA
Q52078 Formaldehyde dismutase; EC 1.2.98.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see paper)
34% identity, 94% coverage: 2:376/400 of query aligns to 5:382/399 of Q52078
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2:399 modified: mature protein, Formaldehyde dismutase
2dphA Crystal structure of formaldehyde dismutase
34% identity, 94% coverage: 2:376/400 of query aligns to 4:381/398 of 2dphA
- active site: C45 (= C38), G46 (= G39), S47 (= S40), H50 (= H43), H66 (= H60), E67 (= E61), C96 (= C90), C99 (= C93), C102 (= C96), C110 (= C104), L114 (≠ I114), S168 (= S169), D169 (= D170), P172 (= P173)
- binding nicotinamide-adenine-dinucleotide: C45 (= C38), G46 (= G39), S47 (= S40), H50 (= H43), F92 (= F86), D169 (= D170), T173 (= T174), A192 (≠ Y193), G193 (= G194), G195 (= G196), P196 (= P197), V197 (= V198), G216 (≠ V217), D217 (= D218), Q218 (≠ D219), R222 (= R223), L236 (≠ F238), V262 (= V265), H267 (≠ K270), P298 (= P307), G299 (= G308), I300 (≠ V309), A337 (≠ T334)
- binding zinc ion: C45 (= C38), H66 (= H60), C96 (= C90), C99 (= C93), C102 (= C96), C110 (= C104), D169 (= D170)
Sites not aligning to the query:
O58389 L-threonine 3-dehydrogenase; L-ThrDH; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see 2 papers)
29% identity, 95% coverage: 1:379/400 of query aligns to 9:330/348 of O58389
- C42 (= C38) binding
- T44 (≠ S40) mutation to A: Total loss of enzymatic activity.
- H67 (= H60) binding
- E68 (= E61) binding
- C97 (= C90) binding
- C100 (= C93) binding
- C103 (= C96) binding
- C111 (= C104) binding
- E152 (≠ D170) mutation E->A,Q: Almost complete loss of enzymatic activity.; mutation to C: 120-fold decrease in catalytic efficiency.; mutation to D: Shows 3-fold higher turnover rate and reduced affinities toward L-threonine and NAD(+), compared to wild-type.; mutation to K: Total loss of enzymatic activity.
- L179 (≠ V198) binding
- E199 (≠ D218) binding ; mutation to A: Large decrease in affinity for NAD(+).
- R204 (= R223) binding ; mutation to A: Large decrease in affinity for NAD(+).
- LGL 266:268 (≠ PGV 307:309) binding
- IT 291:292 (≠ MG 331:332) binding
- R294 (≠ T334) mutation to A: 4000-fold decrease in catalytic efficiency.
2dfvA Hyperthermophilic threonine dehydrogenase from pyrococcus horikoshii (see paper)
29% identity, 95% coverage: 1:379/400 of query aligns to 7:328/346 of 2dfvA
- active site: C40 (= C38), G41 (= G39), T42 (≠ S40), H45 (= H43), H65 (= H60), E66 (= E61), C95 (= C90), C98 (= C93), C101 (= C96), C109 (= C104), K113 (≠ N108), P151 (≠ I171), A155 (= A175)
- binding nicotinamide-adenine-dinucleotide: G175 (= G196), P176 (= P197), L177 (≠ V198), E197 (≠ D218), P198 (≠ D219), R202 (= R223), F241 (≠ A264), S242 (≠ V265), A244 (≠ S287), L264 (≠ P307), G265 (= G308), L266 (≠ V309), I289 (≠ M331), T290 (≠ G332)
- binding zinc ion: C95 (= C90), C101 (= C96), C109 (= C104)
Sites not aligning to the query:
Q5JI69 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) (see paper)
28% identity, 95% coverage: 1:379/400 of query aligns to 9:330/350 of Q5JI69
3gfbA L-threonine dehydrogenase (tktdh) from the hyperthermophilic archaeon thermococcus kodakaraensis (see paper)
28% identity, 95% coverage: 1:379/400 of query aligns to 7:328/347 of 3gfbA
- active site: C40 (= C38), G41 (= G39), T42 (≠ S40), H45 (= H43), H65 (= H60), E66 (= E61), C95 (= C90), C98 (= C93), C101 (= C96), C109 (= C104), K113 (≠ N108), P151 (≠ I171), A155 (= A175)
- binding nicotinamide-adenine-dinucleotide: G173 (= G194), G175 (= G196), P176 (= P197), L177 (≠ V198), S196 (≠ V217), E197 (≠ D218), P198 (≠ D219), R202 (= R223), F241 (≠ A264), S242 (≠ V265), A244 (≠ S287), L264 (≠ P307), G265 (= G308), L266 (≠ V309), I289 (≠ L327), T290 (= T328)
Sites not aligning to the query:
2ejvA Crystal structure of threonine 3-dehydrogenase complexed with NAD+
28% identity, 94% coverage: 17:390/400 of query aligns to 20:343/343 of 2ejvA
- active site: C38 (= C38), G39 (= G39), T40 (≠ S40), H43 (= H43), H63 (= H60), E64 (= E61), C93 (= C90), C96 (= C93), C99 (= C96), C107 (= C104), Q111 (≠ N108), P149 (≠ I171), A153 (= A175), K336 (= K383)
- binding nicotinamide-adenine-dinucleotide: G172 (= G194), G174 (= G196), P175 (= P197), I176 (≠ V198), S195 (≠ V217), D196 (= D218), P197 (≠ D219), R201 (= R223), F238 (≠ A264), S239 (≠ V265), N241 (≠ F267), A244 (= A290), L261 (≠ P307), G262 (= G308), I263 (≠ V309)
- binding zinc ion: C38 (= C38), H63 (= H60), E64 (= E61), C96 (= C93), C99 (= C96), C107 (= C104)
2dq4A Crystal structure of threonine 3-dehydrogenase
28% identity, 94% coverage: 17:390/400 of query aligns to 20:343/343 of 2dq4A
- active site: C38 (= C38), G39 (= G39), T40 (≠ S40), H43 (= H43), H63 (= H60), E64 (= E61), C93 (= C90), C96 (= C93), C99 (= C96), C107 (= C104), Q111 (≠ N108), P149 (≠ I171), A153 (= A175), K336 (= K383)
- binding zinc ion: C38 (= C38), H63 (= H60), E64 (= E61), C93 (= C90), C96 (= C93), C107 (= C104)
Q5SKS4 L-threonine 3-dehydrogenase; TDH; EC 1.1.1.103 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
28% identity, 94% coverage: 17:390/400 of query aligns to 20:343/343 of Q5SKS4
P07913 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Escherichia coli (strain K12) (see paper)
26% identity, 97% coverage: 1:386/400 of query aligns to 1:338/341 of P07913
- C38 (= C38) mutation to D: Shows only 1% of wild-type catalytic activity. This mutant can be stimulated to the wild-type activity level after incubation with Zn(+).; mutation to S: Loss of catalytic activity. This mutant cannot be stimulated to the wild-type activity level after incubation with Zn(+).
8conA Alcohol dehydrogenase class-P (see paper)
30% identity, 85% coverage: 27:366/400 of query aligns to 36:357/379 of 8conA
- binding 1,4-dihydronicotinamide adenine dinucleotide: H48 (≠ G39), T181 (= T174), G202 (= G194), G204 (= G196), V206 (= V198), D226 (= D218), F227 (≠ D219), C271 (≠ A264), T272 (≠ V265), V295 (= V304), G296 (≠ S305), V297 (= V306), F321 (= F329), F322 (≠ M331)
- binding zinc ion: C47 (= C38), H69 (= H60), E70 (= E61), C99 (= C90), C102 (= C93), C105 (= C96), C113 (= C104), C177 (≠ D170)
P06525 Alcohol dehydrogenase class-P; AtADH; EC 1.1.1.1 from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
30% identity, 85% coverage: 27:366/400 of query aligns to 36:357/379 of P06525
- C47 (= C38) binding
- T49 (≠ S40) binding ; binding ; binding
- H69 (= H60) binding
- C99 (= C90) binding
- C102 (= C93) binding
- C105 (= C96) binding ; mutation to Y: In R006; inactive enzyme.
- C113 (= C104) binding
- C177 (≠ D170) binding
- GLGAVG 202:207 (≠ GAGPVG 194:199) binding
- D226 (= D218) binding
- R231 (= R223) binding
- T272 (≠ V265) binding
- V295 (= V304) binding
- F322 (≠ M331) binding
Sites not aligning to the query:
4rquB Alcohol dehydrogenase crystal structure in complex with NAD (see paper)
30% identity, 85% coverage: 27:366/400 of query aligns to 32:353/375 of 4rquB
- active site: C43 (= C38), H44 (≠ G39), T45 (≠ S40), Y48 (≠ H43), H65 (= H60), E66 (= E61), C95 (= C90), C98 (= C93), C101 (= C96), C109 (= C104), R113 (≠ T106), C173 (≠ D170), T177 (= T174)
- binding nicotinamide-adenine-dinucleotide: C43 (= C38), H44 (≠ G39), T45 (≠ S40), F91 (= F86), C173 (≠ D170), T177 (= T174), G200 (= G196), V202 (= V198), D222 (= D218), F223 (≠ D219), R227 (= R223), C267 (≠ A264), T268 (≠ V265), V291 (= V304), F318 (≠ M331)
- binding zinc ion: C43 (= C38), H65 (= H60), C95 (= C90), C98 (= C93), C101 (= C96), C109 (= C104), C173 (≠ D170)
Sites not aligning to the query:
P19854 Alcohol dehydrogenase class-3; Alcohol dehydrogenase 5; Alcohol dehydrogenase class-III; Glutathione-dependent formaldehyde dehydrogenase; FALDH; FDH; GSH-FDH; S-(hydroxymethyl)glutathione dehydrogenase; EC 1.1.1.1; EC 1.1.1.-; EC 1.1.1.284 from Equus caballus (Horse) (see 2 papers)
30% identity, 66% coverage: 3:266/400 of query aligns to 11:270/374 of P19854
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
5kiaA Crystal structure of l-threonine 3-dehydrogenase from burkholderia thailandensis
30% identity, 54% coverage: 26:241/400 of query aligns to 25:216/339 of 5kiaA
- active site: C37 (= C38), G38 (= G39), T39 (≠ S40), H42 (= H43), H61 (= H60), E62 (= E61), C91 (= C90), C94 (= C93), C97 (= C96), C105 (= C104), V109 (≠ T109), P147 (≠ D170), A151 (≠ T174)
- binding calcium ion: D146 (≠ S169), N150 (≠ P173)
- binding zinc ion: C91 (= C90), C94 (= C93), C97 (= C96), C105 (= C104)
Sites not aligning to the query:
Query Sequence
>PP_3970 FitnessBrowser__Putida:PP_3970
MRAVSYHGANDVRVDSVPDPILQDADDIILRVTATAICGSDLHLYRGKIPETEQGDIFGH
EFMGIVEEVGRDVTTLQVGDRVVIPFVIACGSCFFCQQDLFAACETTNTGRGSIINKKGI
PPGAALFGYSHLYGGIPGGQADYVRVPKGNVGPFKVPTTLADDKVLFLSDILPTAWQAVI
NAEIGEGSSVAIYGAGPVGLLSAACARMLGAHTVFMVDDNDYRLAYAQEAYGVIPINFEK
DDDPADSIIRQTPGMRGVDAVIDAVGFEAKGSTTETVMTALKLEGSSGKALRQSIAAVRR
GGVVSVPGVYAGFIHGFMFGDAFDKGLTFKMGQTHVQKYLPELLEHIEAGRLQPELIVTH
RLALEEAAMGYKMFDQKQDNCRKVILVPGAAPGTLGPDHL
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