SitesBLAST
Comparing 14712 b0576 phenylalanine transporter (NCBI) 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)
100% identity, 100% coverage: 1:458/458 of query aligns to 1:458/458 of P24207
- R26 (= R26) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P54) 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 (= F87) mutation to L: No effect on phenylalanine transport activity.
- F90 (= F90) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (= Y92) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y94) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (= W95) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (= F98) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F101) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W105) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y107) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W108) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (= F111) 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 (= E118) mutation E->G,L,V,N: Loss of activity.
- K168 (= K168) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E226) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R252) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P341) 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 (= P442) 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)
65% identity, 94% coverage: 19:448/458 of query aligns to 11:440/457 of P15993
- Y103 (≠ F111) 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, 97% coverage: 14:458/458 of query aligns to 2:449/469 of P46349
- G33 (= G44) mutation to D: Lack of activity.
- G42 (= G53) mutation to S: Lack of activity.
- G301 (= G311) mutation to V: Lack of activity.
- G338 (≠ S348) mutation to E: Lack of activity.
- F341 (≠ I351) mutation to S: Lack of activity.
- G414 (≠ M423) 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)
38% identity, 88% coverage: 9:413/458 of query aligns to 3:420/489 of P25737
- Y102 (= Y107) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ F111) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K168) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F220) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E226) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E234) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ E272) 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 (≠ S275) 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)
36% identity, 92% coverage: 8:428/458 of query aligns to 73:513/590 of P04817
- P113 (≠ A48) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P82) 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 (= V83) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S86) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y107) 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 (≠ A233) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P238) 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 (≠ L369) 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 (≠ L379) 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)
33% identity, 93% coverage: 2:428/458 of query aligns to 68:502/587 of Q9URZ4
Sites not aligning to the query:
- 29 modified: Phosphoserine
- 30 modified: Phosphoserine
- 37 modified: Phosphoserine
P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
36% identity, 88% coverage: 15:415/458 of query aligns to 83:500/602 of P19145
- A297 (≠ G223) 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)
P48813 High-affinity glutamine permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 92% coverage: 8:428/458 of query aligns to 134:570/663 of P48813
Sites not aligning to the query:
- 132 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)
28% identity, 87% coverage: 19:418/458 of query aligns to 277:757/852 of Q03770
- T382 (≠ G123) 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.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
29% identity, 38% coverage: 75:246/458 of query aligns to 74:242/461 of P76037
- Y110 (≠ F111) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
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)
23% identity, 83% coverage: 12:393/458 of query aligns to 21:433/629 of P30825
- N226 (≠ H187) modified: carbohydrate, N-linked (GlcNAc...) asparagine
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
21% identity, 79% coverage: 28:390/458 of query aligns to 15:373/445 of P60061
- I23 (≠ A36) binding ; binding
- S26 (≠ T39) binding
- Y93 (= Y107) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ M110) binding ; binding
- C97 (≠ F111) binding
- N101 (≠ G115) 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 (≠ E118) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F220) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (= S221) binding
- I205 (≠ G223) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ G311) 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.
- S357 (≠ V374) binding ; mutation to A: 20% decreased affinity for Arg, 40% decrease affinity for Agm.
P60063 Arginine/agmatine antiporter from Escherichia coli O157:H7 (see 3 papers)
21% identity, 79% coverage: 28:390/458 of query aligns to 15:373/445 of P60063
- N22 (≠ G35) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ A36) binding
- GSG 25:27 (≠ GTG 38:40) Helix-breaking GSG motif TM1
- S26 (≠ T39) binding ; mutation to K: 5% Agm antiport.
- G27 (= G40) binding
- Y74 (≠ A88) 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 (≠ F101) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y107) 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 (≠ M110) binding
- C97 (≠ F111) binding
- N101 (≠ G115) binding
- W202 (≠ F220) Periplasmic (proximal) gate; binding
- I205 (≠ G223) binding
- GVESA 206:210 (≠ GLELI 224:228) Helix-breaking GVESA motif TM6
- E208 (= E226) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ G311) binding
- F337 (≠ V355) mutation to A: Severely decreased antiport.
- S357 (≠ V374) binding
- Y365 (≠ W382) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
21% identity, 79% coverage: 28:390/458 of query aligns to 11:369/437 of 5j4nA
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
21% identity, 84% coverage: 48:431/458 of query aligns to 53:431/458 of 6f34A
- binding arginine: E115 (≠ M110), Y116 (≠ F111), A119 (≠ V114), F228 (= F220), A229 (≠ S221), I231 (≠ G223), V314 (= V307)
- binding cholesterol: W201 (≠ E190), Y202 (≠ K191)
- binding : A178 (≠ T160), R179 (≠ E161), A186 (≠ K168), I187 (≠ V169), A190 (≠ I172), L194 (= L183), Q296 (≠ S289), V299 (= V292)
Sites not aligning to the query:
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
21% identity, 84% coverage: 48:431/458 of query aligns to 51:429/456 of 5oqtA
Sites not aligning to the query:
3l1lA Structure of arg-bound escherichia coli adic (see paper)
21% identity, 79% coverage: 28:390/458 of query aligns to 9:356/423 of 3l1lA
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
22% identity, 90% coverage: 8:419/458 of query aligns to 3:398/438 of O34739
- C94 (≠ S103) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ I144) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ G174) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ V307) 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.
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
21% identity, 57% coverage: 198:458/458 of query aligns to 168:431/444 of P0AAE8
- Y174 (≠ F204) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (vs. gap) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ I218) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E226) mutation to Q: Strong decrease in both cadaverine excretion and cadaverine uptake. 22-fold increase in Km for cadaverine for cadaverine uptake and 6-fold increase in Km for cadaverine for cadaverine excretion.
- Y235 (= Y257) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 23-fold increase in Km for cadaverine for cadaverine uptake and 7-fold increase in Km for cadaverine for cadaverine excretion.
- Y246 (= Y268) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ S304) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ G321) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ Q325) mutation to N: Strong decrease in both cadaverine excretion and cadaverine uptake. 24-fold increase in Km for cadaverine for cadaverine uptake and 9-fold increase in Km for cadaverine for cadaverine excretion.
- Y310 (≠ L332) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y366 (≠ W382) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- Y368 (≠ M384) mutation to L: Strong decrease in cadaverine uptake.
- C370 (= C386) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
- E377 (≠ R393) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C389 (= C417) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C394 (≠ M423) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C397 (≠ L426) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E408 (≠ R435) mutation to Q: Moderate decrease in cadaverine uptake.
- Y423 (≠ M450) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
Sites not aligning to the query:
- 12 C→S: Does not affect cadaverine excretion and cadaverine uptake.
- 41 W→L: Moderate decrease in cadaverine uptake.
- 43 W→L: Strong decrease in cadaverine uptake.
- 55 Y→L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 57 Y→L: Strong decrease in cadaverine uptake.
- 73 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake. 9-fold increase in Km for cadaverine for cadaverine uptake and 10-fold increase in Km for cadaverine for cadaverine excretion.
- 76 E→Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 89 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake. 10-fold increase in Km for cadaverine for cadaverine uptake and 5-fold increase in Km for cadaverine for cadaverine excretion.
- 90 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- 107 Y→L: Strong decrease in cadaverine uptake.
- 125 C→S: Does not affect cadaverine excretion and cadaverine uptake.
P39277 L-methionine/branched-chain amino acid exporter YjeH from Escherichia coli (strain K12) (see paper)
28% identity, 30% coverage: 209:345/458 of query aligns to 184:319/418 of P39277
- W195 (≠ F220) mutation to A: Strong decrease in methionine efflux.
Sites not aligning to the query:
- 24 T→Y: Strong decrease in methionine efflux.
- 25 G→F: Strong decrease in methionine efflux.
Query Sequence
>14712 b0576 phenylalanine transporter (NCBI)
MKNASTVSEDTASNQEPTLHRGLHNRHIQLIALGGAIGTGLFLGIGPAIQMAGPAVLLGY
GVAGIIAFLIMRQLGEMVVEEPVSGSFAHFAYKYWGPFAGFLSGWNYWVMFVLVGMAELT
AAGIYMQYWFPDVPTWIWAAAFFIIINAVNLVNVRLYGETEFWFALIKVLAIIGMIGFGL
WLLFSGHGGEKASIDNLWRYGGFFATGWNGLILSLAVIMFSFGGLELIGITAAEARDPEK
SIPKAVNQVVYRILLFYIGSLVVLLALYPWVEVKSNSSPFVMIFHNLDSNVVASALNFVI
LVASLSVYNSGVYSNSRMLFGLSVQGNAPKFLTRVSRRGVPINSLMLSGAITSLVVLINY
LLPQKAFGLLMALVVATLLLNWIMICLAHLRFRAAMRRQGRETQFKALLYPFGNYLCIAF
LGMILLLMCTMDDMRLSAILLPVWIVFLFMAFKTLRRK
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