SitesBLAST
Comparing PP_5031 FitnessBrowser__Putida:PP_5031 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)
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
45% identity, 95% coverage: 2:445/467 of query aligns to 14:452/458 of P24207
- R26 (= R14) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P42) mutation to A: 50% of wild-type phenylalanine transport activity.; mutation to G: No change in phenylalanine transport activity.; mutation to L: 26% of wild-type phenylalanine transport activity.
- F87 (= F75) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y78) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ T80) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y82) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ L83) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ M86) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F89) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W93) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y95) mutation to L: No effect on phenylalanine transport activity.
- W108 (≠ A96) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ M99) mutation to L: 60% of wild-type phenylalanine transport activity.; mutation to Y: Enables the transport of tryptophan to almost the same steady-state level as that of phenylalanine.
- E118 (≠ D106) mutation E->G,L,V,N: Loss of activity.
- K168 (= K156) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E218) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R244) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P333) mutation to A: 5% of wild-type phenylalanine transport activity.; mutation P->G,Q,K,R: Loss of activity.; mutation to S: 3% of wild-type phenylalanine transport activity.; mutation to T: 17% of wild-type phenylalanine transport activity.
- P442 (≠ V435) mutation to A: 46% of wild-type phenylalanine transport activity.; mutation to G: 52% of wild-type phenylalanine transport activity.; mutation to L: 43% of wild-type phenylalanine transport activity.
P15993 Aromatic amino acid transport protein AroP; Aromatic amino acid:H(+) symporter AroP; General aromatic amino acid permease; General aromatic transport system from Escherichia coli (strain K12) (see paper)
45% identity, 96% coverage: 2:450/467 of query aligns to 6:449/457 of P15993
- Y103 (≠ M99) Key residue for tryptophan transport; mutation to F: Decreases tryptophan transport to less than 50% of wild-type levels and reduces the ability of tryptophan to inhibit phenylalanine transport from 95 to 62%.
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
36% identity, 99% coverage: 1:461/467 of query aligns to 1:462/469 of P46349
- G33 (= G32) mutation to D: Lack of activity.
- G42 (= G41) mutation to S: Lack of activity.
- G301 (≠ D303) mutation to V: Lack of activity.
- G338 (≠ M340) mutation to E: Lack of activity.
- F341 (≠ A343) mutation to S: Lack of activity.
- G414 (≠ F413) mutation to R: Lack of activity.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
36% identity, 89% coverage: 2:417/467 of query aligns to 8:431/489 of P25737
- Y102 (= Y95) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ M99) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K156) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F212) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E218) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E226) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ G269) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-278.
- D278 (vs. gap) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-275.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 443 D→A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 446 D→A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
31% identity, 85% coverage: 3:399/467 of query aligns to 80:489/590 of P04817
- P113 (≠ A36) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P70) mutation to L: In CAN1-337; confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate, alpha-aminoisobutyrate, 3-chloro-L-alanine, L-ethionine, L-allylglycine, and D-histidine, but not sensitivity to L-aspartic acid alpha-hydroxamate or p-fluoro-L-phenylalanine.
- V149 (= V71) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S74) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y95) mutation to D: In CAN1-306; confers citrulline transport activity in GAP1-deleted cells.; mutation to H: In CAN1-327; confers citrulline transport activity in GAP1-deleted cells.
- G308 (= G225) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P230) mutation to S: In CAN1-329; confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate, alpha-aminoisobutyrate, 3-chloro-L-alanine, L-ethionine, L-allylglycine, and D-histidine, L-aspartic acid alpha-hydroxamate and p-fluoro-L-phenylalanine.
- TS 354:355 (vs. gap) mutation Missing: In CAN1-318; confers citrulline transport activity in GAP1-deleted cells.
- Y356 (vs. gap) mutation to H: In CAN1-340; confers citrulline transport activity in GAP1-deleted cells.; mutation to N: In CAN1-339; confers citrulline transport activity in GAP1-deleted cells.
- W451 (≠ L361) mutation to C: In CAN1-328; confers citrulline transport activity in GAP1-deleted cells.; mutation to L: In CAN1-316; confers citrulline transport activity in GAP1-deleted cells.; mutation to S: In CAN1-335; confers citrulline transport activity in GAP1-deleted cells.
- F461 (≠ V371) mutation to S: In CAN1-307; confers citrulline transport activity in GAP1-deleted cells.
Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 89% coverage: 2:415/467 of query aligns to 75:498/587 of Q9URZ4
Sites not aligning to the query:
- 29 modified: Phosphoserine
- 30 modified: Phosphoserine
- 37 modified: Phosphoserine
P48813 High-affinity glutamine permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 83% coverage: 2:389/467 of query aligns to 140:538/663 of P48813
Sites not aligning to the query:
- 132 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
30% identity, 85% coverage: 7:401/467 of query aligns to 86:493/602 of P19145
- A297 (≠ G215) mutation to V: Impairs basic amino-acids transport and regulation by these amino-acids.
Sites not aligning to the query:
- 76 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Q03770 SPS-sensor component SSY1; Amino-acid permease homolog SSY1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
23% identity, 85% coverage: 7:405/467 of query aligns to 277:754/852 of Q03770
- T382 (≠ G111) mutation T->H,L: Constitutively active, up-regulates amino acid permease transcription in response to subthreshold concentrations of amino acids.; mutation to K: In SSY1-102; constitutively active, up-regulates amino acid permease transcription in the absence of amino-acids.; mutation to R: Constitutively active, up-regulates amino acid permease transcription in the absence of amino acids.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
22% identity, 90% coverage: 2:419/467 of query aligns to 3:405/438 of O34739
- C94 (≠ L91) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (= C140) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L165) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A299) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
Sites not aligning to the query:
- 415 C→S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
23% identity, 81% coverage: 35:413/467 of query aligns to 52:420/458 of 6f34A
- binding arginine: E115 (= E98), Y116 (≠ M99), A119 (≠ V102), F228 (= F212), A229 (= A213), I231 (≠ G215), V314 (≠ A299)
- binding cholesterol: W201 (vs. gap), Y202 (vs. gap)
- binding : A178 (≠ M148), R179 (≠ E149), A186 (≠ K156), I187 (≠ V157), A190 (≠ I160), L194 (≠ I164), Q296 (≠ I281), V299 (≠ A284)
Sites not aligning to the query:
P30825 High affinity cationic amino acid transporter 1; CAT-1; CAT1; Ecotropic retroviral leukemia receptor homolog; Ecotropic retrovirus receptor homolog; Solute carrier family 7 member 1; System Y+ basic amino acid transporter from Homo sapiens (Human) (see paper)
24% identity, 68% coverage: 2:318/467 of query aligns to 23:369/629 of P30825
- N226 (≠ H182) modified: carbohydrate, N-linked (GlcNAc...) asparagine
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
23% identity, 81% coverage: 35:413/467 of query aligns to 50:418/456 of 5oqtA
Sites not aligning to the query:
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
27% identity, 41% coverage: 47:238/467 of query aligns to 58:242/461 of P76037
- Y110 (≠ M99) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
24% identity, 94% coverage: 19:455/467 of query aligns to 12:433/433 of 6f2wA
P82251 b(0,+)-type amino acid transporter 1; b(0,+)AT1; Glycoprotein-associated amino acid transporter b0,+AT1; Solute carrier family 7 member 9 from Homo sapiens (Human) (see 11 papers)
20% identity, 100% coverage: 1:466/467 of query aligns to 26:472/487 of P82251
- V40 (≠ L21) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ AIGTG 24:28) binding
- I44 (= I25) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ G32) to F: in CSNU; uncertain significance
- P52 (≠ S33) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ Y48) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (≠ H77) to H: in CSNU; uncertain significance
- G105 (= G84) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W93) to R: in CSNU; uncertain significance
- I120 (vs. gap) to L: in CSNU; uncertain significance
- T123 (≠ Y95) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ M114) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ F116) modified: Interchain (with C-114 in SLC3A1)
- V170 (= V142) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ L154) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G167) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ A205) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ S206) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (≠ V209) to D: in CSNU; decreased amino acid transport activity
- W230 (≠ F212) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ G215) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ I217) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ I219) mutation to A: Reduces amino acid transport activity.
- G259 (≠ A240) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (= P242) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (= S267) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ I304) mutation to S: Does not affect amino acid transport activity.
- A324 (= A307) to E: in CSNU; uncertain significance
- V330 (≠ G313) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ L314) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (≠ Q316) to Q: in CSNU; decreased amino acid transport activity; dbSNP:rs769576205; to W: in CSNU; severe loss of amino acid transport activity; dbSNP:rs121908484
- A354 (≠ T336) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ T370) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ V373) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (= W374) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ I377) mutation to A: Loss of amino acid transport activity.
- K401 (≠ R390) to E: in CSNU; uncertain significance; dbSNP:rs760264924
- L426 (≠ Q428) to P: in CSNU; uncertain significance
Sites not aligning to the query:
- 482 P → L: in CSNU; severe loss of amino acid transport activity; no effect on localization to the apical membrane; dbSNP:rs146815072; mutation P->A,G,S,V: No effect on amino acid transport activity.; mutation P->F,I,M,W: Decreased amino acid transport activity.
Q7YQK4 Large neutral amino acids transporter small subunit 1; 4F2 light chain; 4F2 LC; 4F2LC; L-type amino acid transporter 1; LAT1; Solute carrier family 7 member 5 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
23% identity, 54% coverage: 174:424/467 of query aligns to 211:469/503 of Q7YQK4
- G219 (= G185) mutation to D: Decreased KM and Vmax for Trp. Increased KM and Vmax for Phe; when associated with L-234.
- W234 (vs. gap) mutation to L: Decreased KM and Vmax for Trp. Increased KM but decreased Vmax for Phe. Increased KM and Vmax for Phe; when associated with D-219.
- C331 (≠ A296) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ I346) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (≠ M376) mutation to S: No significant effect on inhibition by HgCl(2).
- C439 (vs. gap) mutation to S: Prevents insertion into the plasma membrane and possibly protein folding.
- C454 (≠ M409) mutation to S: No significant effect on inhibition by HgCl(2). Slightly increased KM but slightly decreased Vmax for Phe.
Sites not aligning to the query:
- 88 C→S: No significant effect on inhibition by HgCl(2). Decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-183.
- 98 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Slightly less decreased KM and Vmax for Phe; when associated with S-183.
- 160 C→S: No change to KM or Vmax for Phe.
- 172 C→S: No change to KM or Vmax for Phe.
- 174 C→S: No change to KM or Vmax for Phe.
- 183 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-88. Slightly less decreased KM and Vmax for Phe; when associated with S-98.
- 492 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
24% identity, 71% coverage: 16:346/467 of query aligns to 11:332/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
24% identity, 74% coverage: 2:346/467 of query aligns to 3:336/445 of P60061
- I23 (≠ A24) binding ; binding
- S26 (≠ T27) binding
- Y93 (= Y95) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ E98) binding ; binding
- C97 (≠ M99) binding
- N101 (≠ A103) binding ; mutation to A: Vmax for Arg-Agm exchange 1% of wild-type, KM increases 3-fold.; mutation to D: Nearly wild-type Arg-Agm exchange.
- M104 (≠ D106) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F212) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A213) binding
- I205 (≠ G215) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ D303) binding ; mutation W->C,H,L: Loss of Arg-Agm exchange.; mutation W->F,Y: Less than 20% Arg-Agm exchange activity. Vmax 15% of wild-type rate.
Sites not aligning to the query:
- 357 binding ; S→A: 20% decreased affinity for Arg, 40% decrease affinity for Agm.
P60063 Arginine/agmatine antiporter from Escherichia coli O157:H7 (see 3 papers)
24% identity, 74% coverage: 2:346/467 of query aligns to 3:336/445 of P60063
- N22 (≠ S23) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ A24) binding
- GSG 25:27 (≠ GTG 26:28) Helix-breaking GSG motif TM1
- S26 (≠ T27) binding ; mutation to K: 5% Agm antiport.
- G27 (= G28) binding
- Y74 (≠ G76) mutation to A: 50% antiport activity at pH 6.0, 10-fold higher than wild-type antiport activity at pH 7.5, i.e. loss of pH-dependence of substrate transport. No change in binding of Arg or Agm.; mutation Y->C,H,L,M,Q,S: Loss of pH-dependence of substrate transport.; mutation to F: Approximately wild-type antiport.
- Y87 (≠ F89) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y95) mutation to A: Reduced binding affinity for Arg, no binding to Agm. 25% Agm antiport.; mutation to K: Almost no binding to both Arg and Agm. 5% Agm antiport.
- A96 (≠ E98) binding
- C97 (≠ M99) binding
- N101 (≠ A103) binding
- W202 (≠ F212) Periplasmic (proximal) gate; binding
- I205 (≠ G215) binding
- GVESA 206:210 (≠ GIEII 216:220) Helix-breaking GVESA motif TM6
- E208 (= E218) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ D303) binding
Sites not aligning to the query:
- 337 F→A: Severely decreased antiport.
- 357 binding
- 365 Y→A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
Query Sequence
>PP_5031 FitnessBrowser__Putida:PP_5031
MQQAQGLKRGLSARHIRFMALGSAIGTGLFYGSASAIQMAGPAVLLAYLIGGAAVFMVMR
ALGEMAVHNPVAGSFGHYATTYLGPMAGFILGWTYAFEMVIVAIADVTAFGIYMGFWFPE
VARWIWVLGIVFLIGGLNLCNVKVFGEMEFWLSLLKVGAIVAMILAGLGIMAFGFSQVGT
GHAVGMSNLFDHGGFMPNGVGGLIASFAVVMFAFGGIEIIGVTAGEAKDPQRVIPKAINA
VPLRILLFYVLTLFVLMCLYPWPQIGSQGSPFVQIFSNLGIGSAAAVLNVVVISAAISAI
NSDIFGAGRMMYGLAQQGHAPRGFSKLSKHGVPWMTVVVMGAALLIGVLLNYLIPENVFL
LIASIATFATVWVWLMILLTQVAMRRSMSREQVAQLKFPVPFWPYGPAMAIAFMVFIFGV
LGYFPDTQAALIVGVIWVVFLVASYLLWCKPRAGQGQPVAEPAELHR
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