SitesBLAST
Comparing PP_2586 FitnessBrowser__Putida:PP_2586 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)
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
40% identity, 95% coverage: 17:454/460 of query aligns to 11:449/461 of P76037
- Y110 (= Y118) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
26% identity, 92% coverage: 17:441/460 of query aligns to 14:446/458 of 6f34A
- binding arginine: I40 (≠ M43), G42 (≠ P45), T43 (≠ L46), G44 (≠ A47), E115 (≠ D117), Y116 (= Y118), A119 (vs. gap), F228 (≠ L222), A229 (≠ S223), I231 (≠ L225), V314 (≠ S310)
- binding cholesterol: W201 (≠ L188), Y202 (≠ K189)
- binding : G28 (≠ S31), F30 (≠ T33), D31 (≠ A34), M34 (≠ L37), A178 (≠ T165), R179 (= R166), A186 (≠ V173), I187 (≠ V174), A190 (≠ V177), L194 (≠ V181), Q296 (≠ R289), V299 (= V290)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
25% identity, 92% coverage: 17:441/460 of query aligns to 12:444/456 of 5oqtA
- binding alanine: I38 (≠ M43), G40 (≠ P45), T41 (≠ L46), G42 (≠ A47), F226 (≠ L222), A227 (≠ S223), I229 (≠ L225)
- binding : E24 (≠ S29), G26 (≠ S31), F28 (≠ T33), D29 (≠ A34), M32 (≠ L37), A176 (≠ T165), R177 (= R166), A184 (≠ V173), A188 (≠ V177), L192 (≠ V181), Q294 (≠ R289), V297 (= V290)
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)
24% identity, 70% coverage: 82:401/460 of query aligns to 67:389/457 of P15993
- Y103 (= Y118) 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)
24% identity, 65% coverage: 82:378/460 of query aligns to 75:372/458 of P24207
- F87 (≠ V94) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y97) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ R99) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ A101) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ F102) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ H105) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F108) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W112) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ L114) mutation to L: No effect on phenylalanine transport activity.
- W108 (≠ L115) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ Y118) 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 (≠ S125) mutation E->G,L,V,N: Loss of activity.
- K168 (≠ Q175) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (≠ D228) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (≠ G255) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P345) 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.
Sites not aligning to the query:
- 26 mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- 54 P→A: 50% of wild-type phenylalanine transport activity.; P→G: No change in phenylalanine transport activity.; P→L: 26% of wild-type phenylalanine transport activity.
- 442 P→A: 46% of wild-type phenylalanine transport activity.; P→G: 52% of wild-type phenylalanine transport activity.; P→L: 43% of wild-type phenylalanine 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)
26% identity, 80% coverage: 25:394/460 of query aligns to 27:436/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
24% identity, 75% coverage: 22:367/460 of query aligns to 4:356/469 of P46349
- G33 (≠ T51) mutation to D: Lack of activity.
- G42 (≠ K60) mutation to S: Lack of activity.
- G301 (≠ A311) mutation to V: Lack of activity.
- G338 (≠ V352) mutation to E: Lack of activity.
- F341 (≠ L355) mutation to S: Lack of activity.
Sites not aligning to the query:
- 414 G→R: Lack of activity.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
22% identity, 72% coverage: 27:356/460 of query aligns to 14:356/489 of P25737
- Y102 (≠ L114) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y118) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (≠ Q175) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (≠ L222) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ D228) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E236) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (= D285) 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 (≠ E293) 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.
Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
23% identity, 93% coverage: 10:435/460 of query aligns to 68:502/587 of Q9URZ4
Sites not aligning to the query:
- 29 modified: Phosphoserine
- 30 modified: Phosphoserine
- 37 modified: Phosphoserine
3l1lA Structure of arg-bound escherichia coli adic (see paper)
22% identity, 64% coverage: 66:358/460 of query aligns to 39:319/423 of 3l1lA
Sites not aligning to the query:
8b70A Kima from b. Subtilis with nucleotide second-messenger c-di-amp bound (see paper)
27% identity, 56% coverage: 80:335/460 of query aligns to 59:305/572 of 8b70A
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 445, 446, 447, 472, 545, 546, 548
- binding potassium ion: 15, 19, 22, 343
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
25% identity, 65% coverage: 75:374/460 of query aligns to 47:351/453 of 7epzB
Sites not aligning to the query:
Q9UPY5 Cystine/glutamate transporter; Amino acid transport system xc-; Calcium channel blocker resistance protein CCBR1; Solute carrier family 7 member 11; xCT from Homo sapiens (Human) (see 4 papers)
25% identity, 65% coverage: 75:373/460 of query aligns to 91:394/501 of Q9UPY5
- R135 (vs. gap) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ E135) modified: Interchain (with C-210 in SLC3A2); mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- Q191 (≠ N168) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ V174) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435.
- K198 (≠ Q175) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ L222) binding
- F254 (≠ T232) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (vs. gap) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- C327 (= C307) mutation to A: Does not affect L-glutamate transport activity. Does not affect location at cell membrane Does not affect expression level.; mutation to L: Loss of L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Loss of inhibitio nof L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid. Decrease L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to T: Does not affect L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.
- F336 (≠ A316) mutation to A: Decreases L-cystine transport activity about 50%. Increases sensitivity to erastin-induced ferroptosis. Significantly decreases the L-cystine transport activity.; mutation to Y: Does not affect L-cystine transport activity.
Sites not aligning to the query:
- 86 C→S: Does not affect L-cystine transport activity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- 396 R→A: Loss of L-cystine transport activity.; R→K: Loss of L-cystine transport activity.; R→N: Loss of L-cystine transport activity.
- 414 C→S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- 435 C→S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
25% identity, 65% coverage: 75:374/460 of query aligns to 47:351/455 of 7p9uB
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
22% identity, 64% coverage: 66:358/460 of query aligns to 41:332/437 of 5j4nA
Sites not aligning to the query:
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
22% identity, 64% coverage: 66:358/460 of query aligns to 45:336/445 of P60061
- Y93 (≠ L115) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ Y118) binding ; binding
- C97 (≠ I119) binding
- N101 (≠ L123) 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 (≠ Y126) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ L222) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (= S223) binding
- I205 (≠ L225) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ S314) 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:
- 23 binding ; binding
- 26 binding
- 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)
22% identity, 64% coverage: 66:358/460 of query aligns to 45:336/445 of P60063
- Y74 (= Y95) 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 (≠ F108) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (≠ L115) 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 (≠ Y118) binding
- C97 (≠ I119) binding
- N101 (≠ L123) binding
- W202 (≠ L222) Periplasmic (proximal) gate; binding
- I205 (≠ L225) binding
- GVESA 206:210 (≠ GFDAV 226:230) Helix-breaking GVESA motif TM6
- E208 (≠ D228) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ S314) binding
Sites not aligning to the query:
- 22 N→A: No change in antiport activity, 6-fold higher affinity for Arg.
- 23 binding
- 25:27 Helix-breaking GSG motif TM1
- 26 binding ; S→K: 5% Agm antiport.
- 27 binding
- 337 F→A: Severely decreased antiport.
- 357 binding
- 365 Y→A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
P96589 Potassium transporter KimA; K(+) importer A; Potassium-proton symporter KimA from Bacillus subtilis (strain 168) (see paper)
25% identity, 56% coverage: 80:335/460 of query aligns to 80:339/607 of P96589
- D117 (= D117) binding ; mutation D->A,N,E: No effect on growth.
- T121 (≠ L121) mutation to A: Decreases potassium uptake.
- S125 (= S125) binding ; mutation to A: Decreases potassium uptake.
- E233 (≠ D228) mutation E->A,Q: Abolishes potassium uptake.
Sites not aligning to the query:
- 36 binding ; binding ; mutation D->A,N: Abolishes potassium uptake.
- 43 binding ; Y→N: Abolishes potassium uptake.
- 377 Y→A: Decreases potassium uptake.
6s3kB Kima from bacillus subtilis in inward-facing, occluded state (see paper)
25% identity, 56% coverage: 80:335/460 of query aligns to 54:313/573 of 6s3kB
Sites not aligning to the query:
P39277 L-methionine/branched-chain amino acid exporter YjeH from Escherichia coli (strain K12) (see paper)
24% identity, 61% coverage: 86:367/460 of query aligns to 64:343/418 of P39277
- W195 (≠ L222) 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
>PP_2586 FitnessBrowser__Putida:PP_2586
MHTTTSTAHSPAPHAPSQPGTSTGRFRKSMSMTALVLFGLAYMVPLAVFTTYGLVTQMTK
GHLPTAYLLTLAAMLLTAYSYGRMVQAHPYSGSVYTYTRKAFGSHIGFITGWTLLLDYIF
LPLLSYLLIGIYMSEYFPTIHAWVWVAGSIALVTFLNLIGIESITRVNWILVVVQLVFII
VFVALSILKLSGQAEPVSLLAPLHHDGFSVPLIMTGAAVLCLSFLGFDAVSTMAEETSNP
TYRIPVAILAVSLIGGLLFLVVSYCAQMVFPDWGSFADPDSASVDVMRRVGGELLVTAFT
ATYVAGCFASAMVSQASVSRVLFAMGRDGALPRAFGQLVTKKRVPATAILVVSLLSLIAL
VITLDTVANMISFGALFAFSAVNLAVVKHYLVDQKLRGCRNCLLYGAIPGLGFLSTLWLW
SSLTSLSFTIGLCWMGLGLLVLLGLTRALRVKLPELQMAE
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