SitesBLAST
Comparing PP_4934 FitnessBrowser__Putida:PP_4934 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)
P76658 Bifunctional protein HldE; EC 2.7.1.167; EC 2.7.7.70 from Escherichia coli (strain K12) (see 2 papers)
57% identity, 100% coverage: 1:473/473 of query aligns to 1:474/477 of P76658
- K179 (= K178) modified: N6-acetyllysine
- N195 (= N194) mutation to D: Loss of activity.
- E198 (= E197) mutation to D: Loss of activity.
- D264 (= D263) mutation to E: Loss of activity.; mutation to N: Loss of activity.
4e84A Crystal structure of burkholderia cenocepacia hlda (see paper)
54% identity, 62% coverage: 13:307/473 of query aligns to 17:311/313 of 4e84A
- binding phosphoaminophosphonic acid-adenylate ester: N199 (= N194), T235 (= T230), S237 (≠ G232), G240 (= G235), V259 (= V255), V262 (= V258), A265 (= A261), G266 (= G262), A294 (= A290)
- binding 7-O-phosphono-D-glycero-beta-D-manno-heptopyranose: M24 (= M20), D26 (= D22), G56 (= G52), K110 (= K106), R112 (= R108), R122 (= R118), Y156 (= Y151), K158 (= K153), G264 (= G260), D267 (= D263), T303 (= T299)
- binding phosphate ion: R200 (≠ L195), W210 (≠ C205), R236 (= R231)
4e8zA Crystal structure of burkholderia cenocepacia hlda in complex with an atp-competitive inhibitor (see paper)
54% identity, 62% coverage: 13:307/473 of query aligns to 14:308/308 of 4e8zA
- binding {[2-({[5-(2,6-dichlorophenyl)-1,2,4-triazin-3-yl]amino}methyl)-1,3-benzothiazol-5-yl]oxy}acetic acid: N196 (= N194), T232 (= T230), S234 (≠ G232), E235 (= E233), G237 (= G235), A262 (= A261), G263 (= G262), N288 (= N287), G292 (= G291)
4e84B Crystal structure of burkholderia cenocepacia hlda (see paper)
54% identity, 62% coverage: 13:307/473 of query aligns to 14:308/310 of 4e84B
- binding phosphoaminophosphonic acid-adenylate ester: N196 (= N194), T232 (= T230), R233 (= R231), S234 (≠ G232), A253 (= A252), V256 (= V255), V259 (= V258), G263 (= G262), A291 (= A290)
- binding 1,7-di-O-phosphono-D-glycero-beta-D-manno-heptopyranose: M21 (= M20), D23 (= D22), G53 (= G52), K107 (= K106), R109 (= R108), R119 (= R118), Y153 (= Y151), K155 (= K153), G261 (= G260), G263 (= G262), D264 (= D263), T300 (= T299)
- binding phosphate ion: R197 (≠ L195), R233 (= R231)
4e8wA Crystal structure of burkholderia cenocepacia hlda in complex with an atp-competitive inhibitor (see paper)
52% identity, 62% coverage: 13:307/473 of query aligns to 11:298/299 of 4e8wA
- binding {[2-({[5-(2,6-dimethoxyphenyl)-1,2,4-triazin-3-yl]amino}methyl)-1,3-benzothiazol-5-yl]oxy}acetic acid: N193 (= N194), T229 (= T230), S231 (≠ G232), G234 (= G235), A248 (= A250), V251 (= V258), A254 (= A261), G255 (= G262), N280 (= N287), V287 (= V294)
Q9ZVI9 Ethanolamine-phosphate cytidylyltransferase; CTP:phosphoethanolamine cytidylyltransferase; Phosphorylethanolamine cytidylyltransferase 1; EC 2.7.7.14 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 27% coverage: 342:470/473 of query aligns to 57:189/421 of Q9ZVI9
- P126 (= P412) mutation to S: In pect1-4; delayed embryo maturation and reduced fertility.
4xsvA Human ctp: phosphoethanolamine cytidylyltransferase in complex with ctp
37% identity, 19% coverage: 342:433/473 of query aligns to 7:97/306 of 4xsvA
Sites not aligning to the query:
- binding cytidine-5'-monophosphate: 174, 175, 176, 183, 186, 261, 262, 264, 290, 294
- binding cytidine-5'-triphosphate: 122, 123, 126, 127, 128
3glvB Crystal structure of the lipopolysaccharide core biosynthesis protein from thermoplasma volcanium gss1
36% identity, 24% coverage: 342:455/473 of query aligns to 5:116/122 of 3glvB
- active site: N45 (≠ K383), K47 (≠ P385)
- binding adenosine monophosphate: G9 (= G346), V10 (≠ C347), F11 (= F348), H15 (= H352), G17 (= G354), H18 (= H355), Y21 (= Y358), G92 (= G431), Y93 (≠ G432), D94 (= D433), Q95 (≠ Y434)
Sites not aligning to the query:
Q58579 FAD synthase; FMN adenylyltransferase; Flavin adenine dinucleotide synthase; EC 2.7.7.2 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see paper)
41% identity, 20% coverage: 339:433/473 of query aligns to 2:95/149 of Q58579
Sites not aligning to the query:
- 126 C→S: 2-fold increase in activity with Mg(2+) but loss of activity with Co(2+) as cofactor.
- 143 C→S: Nearly no change in activity with Mg(2+) but loss of activity with Co(2+) as cofactor.
6a8cA Ribokinase from leishmania donovani with adp (see paper)
25% identity, 62% coverage: 9:299/473 of query aligns to 11:312/327 of 6a8cA
- binding adenosine-5'-diphosphate: G245 (= G232), A246 (≠ E233), T271 (≠ V258), A274 (= A261), G275 (= G262), N300 (= N287), A303 (= A290)
- binding glycerol: D25 (= D22), S42 (≠ K42), S44 (≠ D44), G50 (≠ P50), G51 (= G51), N55 (= N55)
6a8bA Ribokinase from leishmania donovani with amppcp (see paper)
25% identity, 62% coverage: 9:299/473 of query aligns to 11:312/327 of 6a8bA
- binding phosphomethylphosphonic acid adenylate ester: G245 (= G232), A246 (≠ E233), T271 (≠ V258), A274 (= A261), G275 (= G262), N300 (= N287), A303 (= A290), V307 (= V294)
- binding glycerol: D25 (= D22), G50 (≠ P50), G51 (= G51), N55 (= N55), N157 (≠ D150), I159 (≠ G154), E190 (vs. gap)
6a8aA Ribokinase from leishmania donovani with atp (see paper)
25% identity, 62% coverage: 9:299/473 of query aligns to 11:312/327 of 6a8aA
- binding adenosine-5'-triphosphate: N207 (= N194), T243 (= T230), G245 (= G232), A246 (≠ E233), G248 (= G235), T271 (≠ V258), G273 (= G260), A274 (= A261), G275 (= G262), N300 (= N287), A303 (= A290), V307 (= V294)
- binding glycerol: D25 (= D22), G50 (≠ P50), G51 (= G51), N55 (= N55)
1n1dA Glycerol-3-phosphate cytidylyltransferase complexed with cdp-glycerol (see paper)
34% identity, 28% coverage: 340:470/473 of query aligns to 2:126/126 of 1n1dA
- active site: K44 (≠ G384), K46 (≠ G386)
- binding [cytidine-5'-phosphate] glycerylphosphoric acid ester: G8 (= G346), T9 (≠ C347), F10 (= F348), K44 (≠ G384), K46 (≠ G386), E71 (= E417), G92 (≠ A442), W95 (≠ V445), R113 (≠ L457), T114 (≠ V458), I117 (≠ S461)
- binding sulfate ion: H14 (= H352), H17 (= H355), S118 (= S462), T119 (= T463)
1cozA Ctp:glycerol-3-phosphate cytidylyltransferase from bacillus subtilis (see paper)
34% identity, 28% coverage: 340:470/473 of query aligns to 2:126/126 of 1cozA
- active site: K44 (≠ G384), K46 (≠ G386)
- binding cytidine-5'-triphosphate: T9 (≠ C347), H14 (= H352), H17 (= H355), K46 (≠ G386), G92 (≠ A442), R113 (≠ L457), T114 (≠ V458), I117 (≠ S461), S118 (= S462), T119 (= T463), T120 (= T464)
P27623 Glycerol-3-phosphate cytidylyltransferase; GCT; GCTase; Gro-PCT; CDP-glycerol pyrophosphorylase; Teichoic acid biosynthesis protein D; EC 2.7.7.39 from Bacillus subtilis (strain 168) (see 3 papers)
34% identity, 28% coverage: 340:470/473 of query aligns to 2:126/129 of P27623
- TF 9:10 (≠ CF 347:348) binding
- D11 (= D349) mutation D->A,E: 0.1% of wild-type activity.
- H14 (= H352) mutation to A: Complete loss of activity.
- HWGH 14:17 (≠ HAGH 352:355) binding
- H17 (= H355) mutation to A: Complete loss of activity.
- D38 (= D376) mutation to A: 8% of wild-type activity, but 7-fold decrease in substrate affinity.
- K44 (≠ G384) binding ; mutation to A: Reduces affinity for glycerol 3-phosphate about 100-fold.
- K46 (≠ G386) binding ; mutation to A: Reduces affinity for glycerol 3-phosphate about 100-fold.
- R55 (= R395) mutation to A: 0.25% of wild-type activity.; mutation to K: 23% of wild-type activity.
- R63 (≠ G403) mutation to A: 14% of wild-type activity.
- D66 (= D406) mutation to A: Complete loss of activity, and widespread change in 3D-structure.; mutation to E: 16% of wild-type activity.
- W74 (≠ L420) mutation to A: 50% of wild-type activity, but 9-fold decrease in substrate affinity.
- K77 (≠ V423) binding
- H84 (≠ Y434) mutation to A: Complete loss of activity.
- D94 (≠ I444) mutation to A: 18% of wild-type activity, but 100-fold decrease in substrate affinity.
- R113 (≠ L457) mutation to A: 1.75% of wild-type activity.; mutation to K: Complete loss of activity.
- 113:120 (vs. 457:464, 50% identical) binding
- T114 (≠ V458) mutation to A: 9% of wild-type activity.
- S118 (= S462) mutation to A: 6% of wild-type activity.
- T119 (= T463) mutation to A: 8% of wild-type activity.
3ikhA Crystal structure of ribokinase in complex with atp and glycerol in the active site from klebsiella pneumoniae
25% identity, 55% coverage: 13:272/473 of query aligns to 4:242/286 of 3ikhA
Sites not aligning to the query:
3i3yD Crystal structure of ribokinase in complex with d-ribose from klebsiella pneumoniae
25% identity, 55% coverage: 13:272/473 of query aligns to 3:241/285 of 3i3yD
7qa7A Crystal structure of thE C-terminal catalytic domain of plasmodium falciparum ctp:phosphocholine cytidylyltransferase with cyclopropanemethylamine
31% identity, 28% coverage: 341:473/473 of query aligns to 5:132/136 of 7qa7A
3b1rA Structure of burkholderia thailandensis nucleoside kinase (bthnk) in complex with amp-mg-amp (see paper)
27% identity, 52% coverage: 51:298/473 of query aligns to 47:287/310 of 3b1rA
- active site: D246 (= D257), P247 (≠ V258), G249 (= G260), C250 (≠ A261)
- binding adenosine monophosphate: G47 (= G51), C48 (≠ G52), N110 (≠ E123), F116 (≠ L130), P142 (≠ D150), Q168 (≠ K180), T219 (= T230), G221 (= G232), E222 (= E233), G224 (= G235), G249 (= G260), C250 (≠ A261), D252 (= D263), F254 (≠ V265), S276 (≠ N287), G279 (≠ A290), I283 (≠ V294)
Sites not aligning to the query:
3b1nB Structure of burkholderia thailandensis nucleoside kinase (bthnk) in complex with adp-mizoribine (see paper)
27% identity, 52% coverage: 51:298/473 of query aligns to 47:287/320 of 3b1nB
- active site: G249 (= G260), C250 (≠ A261), G251 (= G262), D252 (= D263)
- binding adenosine-5'-diphosphate: N110 (≠ E123), T219 (= T230), G221 (= G232), E222 (= E233), G224 (= G235), C250 (≠ A261), G251 (= G262), S276 (≠ N287), G279 (≠ A290), I283 (≠ V294)
- binding 5-hydroxy-1-(beta-D-ribofuranosyl)-1H-imidazole-4-carboxamide: G47 (= G51), C48 (≠ G52), N51 (= N55), F116 (≠ L130), Q168 (≠ K180), D252 (= D263)
Sites not aligning to the query:
Query Sequence
>PP_4934 FitnessBrowser__Putida:PP_4934
MKLSMPRFDQAPVLVVGDVMLDRYWHGGTSRISPEAPVPVVKVDQIEDRPGGAANVALNI
AALGAPASLIGVTGQDEAADSLANSLQAAGVRSVFQRIAHQPTIVKLRVMSRHQQLLRID
FEEPFATDPLSLGAEVDSLLEGVKVLVLSDYGKGALKNHQNLIQAARAKGIPVLADPKGK
DFSIYRGASLITPNLSEFETIVGRCVDEAELVAKGLQLLQDLDLGALLVTRGEHGMTLLR
VGQPALHLPARAREVFDVTGAGDTVISTLAAAIAAGEDLPHAVALANLAAGIVVGKLGTA
AISAPELRRAIQREEGSERGVLGLEQLLLAIDDARAHNEKIVFTNGCFDILHAGHVTYLE
QARAQGDRLIVAVNDDASVSRLKGPGRPINSVDRRMAVLAGLGAVDWVISFPEGTPENLL
SQVKPDVLVKGGDYGIDQVVGADIVKGYGGTVKVLGLVENSSTTAIVEKIRKN
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