SitesBLAST
Comparing AO356_15120 AO356_15120 amino acid transporter 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)
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
41% identity, 97% coverage: 3:465/476 of query aligns to 2:479/489 of P25737
- Y102 (= Y103) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (= W107) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K164) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F218) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E224) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E232) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (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-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.
- E438 (≠ D432) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D443 (vs. gap) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (vs. gap) mutation to A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
37% identity, 98% coverage: 8:472/476 of query aligns to 2:459/469 of P46349
- G33 (≠ T39) mutation to D: Lack of activity.
- G42 (= G48) mutation to S: Lack of activity.
- G301 (= G309) mutation to V: Lack of activity.
- G338 (≠ S346) mutation to E: Lack of activity.
- F341 (≠ G349) mutation to S: Lack of activity.
- G414 (≠ L424) mutation to R: Lack of activity.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
35% identity, 88% coverage: 5:423/476 of query aligns to 10:419/458 of P24207
- R26 (= R21) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P49) 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 (= F83) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y86) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ T88) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ F90) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ L91) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ G94) mutation to L: No effect on phenylalanine transport activity.
- F101 (≠ Y97) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W101) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y103) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W104) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ W107) 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 (= E114) mutation E->G,L,V,N: Loss of activity.
- K168 (= K164) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E224) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R250) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P339) 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:
- 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.
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)
34% identity, 87% coverage: 6:421/476 of query aligns to 5:409/457 of P15993
- Y103 (≠ W107) 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%.
P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
32% identity, 84% coverage: 15:412/476 of query aligns to 85:496/590 of P04817
- P113 (≠ T43) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P78) 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 (≠ E79) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S82) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y103) 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 (= G231) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P236) 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 (≠ A367) 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 (≠ V377) 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)
32% identity, 83% coverage: 12:406/476 of query aligns to 78:481/587 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)
33% identity, 83% coverage: 11:407/476 of query aligns to 83:491/602 of P19145
- A297 (≠ S221) 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)
28% identity, 85% coverage: 5:407/476 of query aligns to 136:550/663 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)
23% identity, 95% coverage: 15:465/476 of query aligns to 278:814/852 of Q03770
- T382 (≠ G119) 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)
26% identity, 56% coverage: 1:267/476 of query aligns to 7:265/461 of P76037
- Y110 (≠ W107) 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)
25% identity, 86% coverage: 15:422/476 of query aligns to 24:421/458 of 6f34A
- binding arginine: I40 (≠ V31), G42 (= G33), T43 (= T34), G44 (= G35), E115 (≠ T106), Y116 (≠ W107), A119 (= A110), F228 (= F218), A229 (= A219), I231 (≠ S221), V314 (≠ A305)
- binding cholesterol: W201 (≠ S194), Y202 (≠ N195)
- binding : G28 (≠ Q19), F30 (≠ R21), D31 (≠ H22), M34 (= M25), A178 (≠ G181), R179 (≠ L182), A186 (≠ H189), I187 (vs. gap), A190 (vs. gap), L194 (vs. gap), Q296 (≠ I287), V299 (≠ S290)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
25% identity, 86% coverage: 15:422/476 of query aligns to 22:419/456 of 5oqtA
- binding alanine: I38 (≠ V31), G40 (= G33), T41 (= T34), G42 (= G35), F226 (= F218), A227 (= A219), I229 (≠ S221)
- binding : E24 (= E17), G26 (≠ Q19), F28 (≠ R21), D29 (≠ H22), M32 (= M25), A176 (≠ G181), R177 (≠ L182), A184 (≠ H189), A188 (vs. gap), L192 (vs. gap), Q294 (≠ I287), V297 (≠ S290)
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
26% identity, 68% coverage: 23:345/476 of query aligns to 11:325/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
26% identity, 68% coverage: 23:345/476 of query aligns to 15:329/445 of P60061
- I23 (≠ V31) binding ; binding
- S26 (≠ T34) binding
- Y93 (= Y103) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (vs. gap) binding ; binding
- C97 (≠ T106) binding
- N101 (≠ A110) 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 (≠ S113) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F218) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A219) binding
- I205 (≠ S221) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ G309) 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)
26% identity, 68% coverage: 23:345/476 of query aligns to 15:329/445 of P60063
- N22 (≠ G30) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ V31) binding
- GSG 25:27 (≠ GTG 33:35) Helix-breaking GSG motif TM1
- S26 (≠ T34) binding ; mutation to K: 5% Agm antiport.
- G27 (= G35) binding
- Y74 (≠ S84) 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 (= Y97) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y103) 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 (vs. gap) binding
- C97 (≠ T106) binding
- N101 (≠ A110) binding
- W202 (≠ F218) Periplasmic (proximal) gate; binding
- I205 (≠ S221) binding
- GVESA 206:210 (≠ GTELI 222:226) Helix-breaking GVESA motif TM6
- E208 (= E224) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ G309) 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.
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)
22% identity, 81% coverage: 8:393/476 of query aligns to 22:433/629 of P30825
- N226 (≠ H189) modified: carbohydrate, N-linked (GlcNAc...) asparagine
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
23% identity, 66% coverage: 12:327/476 of query aligns to 6:313/438 of O34739
- C94 (≠ V99) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ G140) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ T167) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A305) 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.
3l1lA Structure of arg-bound escherichia coli adic (see paper)
26% identity, 68% coverage: 23:345/476 of query aligns to 9:312/423 of 3l1lA
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)
22% identity, 69% coverage: 15:344/476 of query aligns to 36:368/531 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 (≠ W107) 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 (= F218) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
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)
22% identity, 69% coverage: 15:344/476 of query aligns to 37:369/535 of Q9UHI5
- I53 (≠ V31) binding
- Y93 (≠ L70) 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 (≠ W107) 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 (≠ R124) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ L144) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F218) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ S221) 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 (≠ F278) 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
Query Sequence
>AO356_15120 AO356_15120 amino acid transporter
MSITEQQTNTRTGFKQEMQTRHIVMLALGGVIGTGLFLTSGYTVNQAGPMGAVIAYIIGA
LMVYMVMMCLGELAVQMPETGSFSTYATRFLGPGTGYTVAWLYWLTWTVAIGSEFTAAGI
LMSRWFPDTPVWIWSALFAGVVFLTNVVSVRLFAETEFWLSLIKVLTVVVFLLIGGGAIL
GLLNIDQAHSIGLSNFTREGLFPTGFMPIAMTLLAVSFAFSGTELIGIAAGETKDPQRNV
PRAIRTTVLRLAVFFVGTIFVLATLLPREQAGLVESPFVTVFTYIGIPYSADIMNFVIIS
ALLSAANSGLYAASRMLWTLSDQGHLPKQFSALTRMGTPLNAIIVSMAGGAASLLSSVFA
ADTIYLALVSISGLAVVVVWMSIAASQIAFRRHYVANGGDIRDLKFRVRGYPWVPLGALV
CCSLACVGIAFDPEQRVALYFGLPFIAWCYFVYYITRKSRERRLSVALVAQPSDAF
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