SitesBLAST
Comparing PP_1229 FitnessBrowser__Putida:PP_1229 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
62% identity, 97% coverage: 9:444/450 of query aligns to 14:449/461 of P76037
- Y110 (= Y105) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
27% identity, 83% coverage: 13:385/450 of query aligns to 13:399/489 of P25737
- Y102 (≠ S101) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y105) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (≠ Q162) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F211) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ D217) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E225) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ H266) 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 (≠ E269) 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.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
25% identity, 74% coverage: 69:400/450 of query aligns to 75:411/458 of P24207
- F87 (≠ A81) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y84) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ Q86) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ A88) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ I89) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ H92) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F95) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W99) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ S101) mutation to L: No effect on phenylalanine transport activity.
- W108 (≠ L102) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ Y105) 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 (≠ N112) mutation E->G,L,V,N: Loss of activity.
- K168 (≠ Q162) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (≠ D217) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (vs. gap) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P335) 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.
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
25% identity, 83% coverage: 4:377/450 of query aligns to 14:392/458 of 6f34A
- binding arginine: I40 (≠ L30), G42 (≠ P32), T43 (≠ M33), G44 (≠ T34), E115 (≠ D104), Y116 (= Y105), A119 (≠ L108), F228 (= F211), A229 (≠ S212), I231 (≠ L214), V314 (≠ G300)
- binding cholesterol: W201 (≠ R175), Y202 (≠ G176)
- binding : G28 (≠ R18), F30 (≠ W20), D31 (≠ H21), M34 (≠ I24), A178 (= A152), R179 (≠ H153), A186 (≠ G160), I187 (≠ V161), A190 (= A164), L194 (≠ V168), Q296 (≠ K282), V299 (≠ Q285)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
24% identity, 83% coverage: 4:377/450 of query aligns to 12:390/456 of 5oqtA
- binding alanine: I38 (≠ L30), G40 (≠ P32), T41 (≠ M33), G42 (≠ T34), F226 (= F211), A227 (≠ S212), I229 (≠ L214)
- binding : E24 (≠ T16), G26 (≠ R18), F28 (≠ W20), D29 (≠ H21), M32 (≠ I24), A176 (= A152), R177 (≠ H153), A184 (≠ G160), A188 (= A164), L192 (≠ V168), Q294 (≠ K282), V297 (≠ Q285)
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: 12:384/450 of query aligns to 27:435/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
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, 72% coverage: 62:383/450 of query aligns to 91:411/501 of Q9UPY5
- R135 (≠ L108) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ A122) 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 (≠ N155) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ V161) 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 (≠ Q162) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ F211) binding
- F254 (≠ C221) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ F238) 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 (≠ V293) 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 (≠ A302) 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.
- R396 (≠ A368) mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.; mutation to N: Loss of 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.
- 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.
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
25% identity, 72% coverage: 62:383/450 of query aligns to 47:367/453 of 7epzB
Sites not aligning to the query:
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
25% identity, 72% coverage: 62:383/450 of query aligns to 47:367/455 of 7p9uB
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
23% identity, 77% coverage: 51:395/450 of query aligns to 35:379/458 of 6li9B
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)
23% identity, 77% coverage: 51:395/450 of query aligns to 64:408/487 of P82251
- A70 (= A57) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y84) to H: in CSNU; uncertain significance
- G105 (≠ N90) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W99) to R: in CSNU; uncertain significance
- I120 (vs. gap) to L: in CSNU; uncertain significance
- T123 (vs. gap) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ L120) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ A122) modified: Interchain (with C-114 in SLC3A1)
- V170 (= V148) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ G160) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (≠ C173) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (= L209) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ C210) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (vs. gap) to D: in CSNU; decreased amino acid transport activity
- W230 (vs. gap) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ L214) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F216) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ A218) mutation to A: Reduces amino acid transport activity.
- G259 (= G245) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ V247) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ A270) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ Q304) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ V307) to E: in CSNU; uncertain significance
- V330 (= V313) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M314) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R316) 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 (≠ N338) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ A365) mutation to A: Markedly reduces amino acid transport activity.
- A382 (= A368) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ F369) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ V372) mutation to A: Loss of amino acid transport activity.
- K401 (= K388) to E: in CSNU; uncertain significance; dbSNP:rs760264924
Sites not aligning to the query:
- 40 V → M: in CSNU; uncertain significance
- 43:47 binding
- 44 I → T: in CSNU; type I; dbSNP:rs121908485
- 51 S → F: in CSNU; uncertain significance
- 52 P → L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- 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.
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, 50% coverage: 12:236/450 of query aligns to 10:237/457 of P15993
- Y103 (= Y105) 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)
24% identity, 52% coverage: 4:236/450 of query aligns to 2:235/469 of P46349
- G33 (≠ T38) mutation to D: Lack of activity.
- G42 (≠ A47) mutation to S: Lack of activity.
Sites not aligning to the query:
- 301 G→V: Lack of activity.
- 338 G→E: Lack of activity.
- 341 F→S: Lack of activity.
- 414 G→R: Lack of activity.
Q9FFL1 Polyamine transporter RMV1; Protein RESISTANT TO METHYL VIOLOGEN 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
26% identity, 75% coverage: 39:374/450 of query aligns to 71:408/490 of Q9FFL1
- I377 (≠ S346) mutation to F: Loss of sensitivity to paraquat.
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, 82% coverage: 46:413/450 of query aligns to 67:444/531 of Q9QXW9
- Y130 (vs. gap) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (vs. gap) 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 (= F211) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
24% identity, 78% coverage: 65:413/450 of query aligns to 50:405/458 of 7cmiB
Sites not aligning to the query:
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
24% identity, 78% coverage: 65:413/450 of query aligns to 50:405/458 of 7cmhB
Sites not aligning to the query:
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
24% identity, 78% coverage: 65:413/450 of query aligns to 50:405/457 of 7b00A
Sites not aligning to the query:
P39277 L-methionine/branched-chain amino acid exporter YjeH from Escherichia coli (strain K12) (see paper)
29% identity, 45% coverage: 190:391/450 of query aligns to 173:374/418 of P39277
- W195 (≠ F211) 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.
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)
23% identity, 78% coverage: 65:413/450 of query aligns to 90:445/535 of Q9UHI5
- Y93 (= Y68) 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 (vs. gap) 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 (≠ A122) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ L142) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F211) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ L214) 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 (≠ I275) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (≠ A368) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ F369) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ S375) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- R418 (≠ N392) to C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
Sites not aligning to the query:
- 53 binding
- 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
Query Sequence
>PP_1229 FitnessBrowser__Putida:PP_1229
MQPDHSASGNGQLRKTLRLWHVIIIGLAYLTPMTVFDTFGIVSGITAGHVPSAYILALAG
ILFTAVSYGTLVKRFPQSGSAYTYTQRAINPHVGFLVGWSSLLDYLLLPMVNALLAKLYL
SAMFPEVPEWMWVAGFVTLISLINMRSVNLVAHFNLLFVGVQVAIIAVFIYLCVRGLDQG
EGLGTTWSLIPFADSQTQFSALAAGATILCFSFLGFDAVTCLSEETRDPAKTIPRAIFLT
ALIGGVVFITVSYFIQAYFPTMARFHDQEAALPEIALYVGGKLFQSIFIACTVINTIASG
LASQTSVSRLLYVMGRDNVIPASVFARLHSRYKTPVLNIAVVGLISLSAIFFDLVTATSI
INFGALVAFSFVNLSVINHCYLREGNRKGLANQLKYLVLPTIGFCIIVSLWLDLNAHSLM
FGGIWAALGLVYLGWLTKAFRAAPPNYVAE
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