SitesBLAST
Comparing PP_4495 FitnessBrowser__Putida:PP_4495 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)
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)
66% identity, 97% coverage: 1:458/472 of query aligns to 2:449/457 of P15993
- Y103 (= Y103) 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%.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
57% identity, 95% coverage: 11:459/472 of query aligns to 19:458/458 of P24207
- R26 (= R18) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P46) 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 (= F79) mutation to L: No effect on phenylalanine transport activity.
- F90 (= F82) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ H84) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y86) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (= W87) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (= F90) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F93) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W97) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ C99) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W100) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ Y103) 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 (= E110) mutation E->G,L,V,N: Loss of activity.
- K168 (= K160) 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 (= P342) 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 (= P443) 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.
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
35% identity, 99% coverage: 5:472/472 of query aligns to 2:462/469 of P46349
- G33 (= G36) mutation to D: Lack of activity.
- G42 (= G45) mutation to S: Lack of activity.
- G301 (= G312) mutation to V: Lack of activity.
- G338 (≠ S349) mutation to E: Lack of activity.
- F341 (≠ V352) mutation to S: Lack of activity.
- G414 (≠ L424) 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)
35% identity, 82% coverage: 11:395/472 of query aligns to 13:398/489 of P25737
- Y102 (≠ C99) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y103) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K160) 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 (= D270) 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 (≠ G273) 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)
32% identity, 89% coverage: 5:426/472 of query aligns to 78:510/590 of P04817
- P113 (≠ V40) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P74) 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 (= V75) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S78) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (≠ C99) 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 (≠ A225) 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 (≠ GG 273:274) mutation Missing: In CAN1-318; confers citrulline transport activity in GAP1-deleted cells.
- Y356 (≠ S275) 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 (≠ L370) 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 (≠ V380) mutation to S: In CAN1-307; confers citrulline transport activity in GAP1-deleted cells.
P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
32% identity, 83% coverage: 11:402/472 of query aligns to 86:483/602 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)
P48813 High-affinity glutamine permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
30% identity, 85% coverage: 4:402/472 of query aligns to 138:542/663 of P48813
Sites not aligning to the query:
- 132 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
33% identity, 83% coverage: 11:402/472 of query aligns to 80:474/587 of Q9URZ4
Sites not aligning to the query:
- 29 modified: Phosphoserine
- 30 modified: Phosphoserine
- 37 modified: Phosphoserine
Q03770 SPS-sensor component SSY1; Amino-acid permease homolog SSY1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 86% coverage: 10:413/472 of query aligns to 276:754/852 of Q03770
- T382 (≠ G115) 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)
25% identity, 36% coverage: 67:238/472 of query aligns to 74:242/461 of P76037
- Y110 (= Y103) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
25% identity, 70% coverage: 23:353/472 of query aligns to 8:335/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
25% identity, 70% coverage: 23:353/472 of query aligns to 8:335/458 of 7cmhB
Sites not aligning to the query:
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
25% identity, 70% coverage: 23:353/472 of query aligns to 8:335/457 of 7b00A
Sites not aligning to the query:
Q9UHI5 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; hLAT2; Solute carrier family 7 member 8 from Homo sapiens (Human) (see 3 papers)
25% identity, 71% coverage: 23:355/472 of query aligns to 48:377/535 of Q9UHI5
- I53 (≠ A28) binding
- Y93 (≠ L66) mutation to A: Nearly complete reduction of glycine, L-alanine, and L-glutamine uptake. Minimal effect on the transport of L-isoleucine, L-histidine and L-tryptophan.
- N134 (≠ M108) Important for substrate specificity; binding ; mutation to Q: Reduces L-leucine uptake activity. Abolishes L-tryptophan uptake.; mutation to S: The substrate specificity changed dramatically reducing L-glutamine, glycine and L-alanine uptake activity thus mimicking the selectivity of SLC7A5.
- C154 (≠ W128) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ A140) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F212) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (= G215) Important for substrate specificity; binding ; mutation to S: Strong decrease in the uptake of large substrates L-tryptophan, L-glutamine, and L-histidine but increases the uptake of small neutral amino acids glycine and L-alanine.
- V302 (≠ S272) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
Sites not aligning to the query:
- 395 binding ; N→Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- 396 Y→A: Strongly reduces L-leucine uptake activity.
- 402 T → M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- 418 R → C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
- 460 V → E: found in a patient with age-related hearing loss; strongly decreases L-alanine transport activity. Decreases L-tyrosine transport activity. Decreases cell membrane localization
Q9QXW9 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; mLAT2; Solute carrier family 7 member 8 from Mus musculus (Mouse) (see paper)
25% identity, 71% coverage: 23:355/472 of query aligns to 47:376/531 of Q9QXW9
- Y130 (≠ L105) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ M108) mutation to S: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake. Increases the export of both L-leucine and L-phenylalanine.
- F242 (= F212) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
22% identity, 82% coverage: 23:409/472 of query aligns to 12:387/433 of 6f2wA
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
21% identity, 89% coverage: 42:460/472 of query aligns to 55:454/458 of 6f34A
- binding arginine: E115 (≠ L102), Y116 (= Y103), A119 (vs. gap), F228 (= F212), A229 (≠ S213), I231 (≠ G215), V314 (= V308)
- binding cholesterol: W201 (≠ Y173), Y202 (≠ L174)
- binding : A178 (= A152), R179 (≠ E153), A186 (≠ K160), I187 (≠ V161), A190 (≠ I164), L194 (≠ I168), Q296 (≠ S290), V299 (≠ A293)
Sites not aligning to the query:
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)
24% identity, 50% coverage: 4:238/472 of query aligns to 14:256/487 of P82251
- V40 (≠ L25) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ AIGTG 28:32) binding
- I44 (= I29) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ G36) to F: in CSNU; uncertain significance
- P52 (≠ S37) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (= A53) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (≠ H81) to H: in CSNU; uncertain significance
- G105 (= G88) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W97) to R: in CSNU; uncertain significance
- I120 (≠ Y103) to L: in CSNU; uncertain significance
- T123 (vs. gap) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (= V118) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ Y120) modified: Interchain (with C-114 in SLC3A1)
- V170 (= V146) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ I158) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G171) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (= L207) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (= A208) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (vs. gap) 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 (≠ L217) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ M219) mutation to A: Reduces amino acid transport activity.
Sites not aligning to the query:
- 259 G → R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- 261 P → L: in CSNU; types I and III; dbSNP:rs121908486
- 286 S → F: in CSNU; uncertain significance; dbSNP:rs755135545
- 321 C→S: Does not affect amino acid transport activity.
- 324 A → E: in CSNU; uncertain significance
- 330 V → M: in CSNU; type III; dbSNP:rs201618022
- 331 A → V: in CSNU; non-classic type I; dbSNP:rs768466784
- 333 R → Q: in CSNU; decreased amino acid transport activity; dbSNP:rs769576205; R → W: in CSNU; severe loss of amino acid transport activity; dbSNP:rs121908484
- 354 A → T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- 379 S→A: Markedly reduces amino acid transport activity.
- 382 A → T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- 383 W→A: Complete loss of amino acid transport activity.
- 386 Y→A: Loss of amino acid transport activity.
- 401 K → E: in CSNU; uncertain significance; dbSNP:rs760264924
- 426 L → P: in CSNU; uncertain significance
- 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.
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)
27% identity, 39% coverage: 193:374/472 of query aligns to 245:414/629 of P30825
Sites not aligning to the query:
- 226 modified: carbohydrate, N-linked (GlcNAc...) asparagine
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
21% identity, 96% coverage: 6:459/472 of query aligns to 1:436/438 of O34739
- C94 (≠ S95) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (vs. gap) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ S166) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ V308) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- C415 (≠ V437) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
Query Sequence
>PP_4495 FitnessBrowser__Putida:PP_4495
MSGQNMHSGELKRGLKNRHIQLIALGGAIGTGLFLGSAGVMKSAGPSMILGYAICGFIAF
MIMRQLGEMIVEEPVAGSFSHFAHTYWGGFAGFLSGWNCWVLYILVGMSELSAVGKYVHY
WWPEIPTWVTAAAFFVLINAINLMNVKFFGEAEFWFAIIKVVAIVSMIGLGAYLLTSGSG
GPEATVANLWTHGGFFPNGVSGLVMALAFIMFSFGGLEMLGFTAAEADKPKTVIPKAINQ
VIYRILIFYVGALVVLLSLTPWDNLVASIDASGGSYGSSPFVQVFSLLGSDVAANLLNFV
VLTAALSVYNSGTYCNARMLLGMAEQGDAPASLAKVDKRGVPVRSILVSAAVTFVAVLLN
YLMPQNALELLMSLVVATLVINWAMISYSHLKFRQHLDRTGQKPLFKALWYPYGNYVVLA
FVVLILGIMLMIPGIQVSVYAIPVWLLAMLVVYMVKSRRQVNAGGAVETVAK
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