SitesBLAST
Comparing 17750 b3691 D-galactonate transport (VIMSS) to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 14 hits to proteins with known functional sites (download)
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
100% identity, 100% coverage: 1:430/430 of query aligns to 1:430/430 of P0AA76
- Y29 (= Y29) binding
- D31 (= D31) mutation to N: Loss of galactonate transport activity.
- R32 (= R32) binding
- Y64 (= Y64) binding
- E118 (= E118) mutation to Q: Loss of galactonate transport activity.
- W358 (= W358) binding
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
98% identity, 97% coverage: 12:428/430 of query aligns to 1:409/409 of 6e9nA
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
93% identity, 98% coverage: 9:428/430 of query aligns to 1:393/393 of 6e9oA
Q9NRA2 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Membrane glycoprotein HP59; Solute carrier family 17 member 5; Vesicular excitatory amino acid transporter; VEAT from Homo sapiens (Human) (see 8 papers)
25% identity, 93% coverage: 28:428/430 of query aligns to 83:484/495 of Q9NRA2
- K136 (≠ R81) to E: in SD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transporter activity, but retains appreciable H(+)-coupled sialic acid transporter activity; dbSNP:rs80338795
- H183 (≠ N126) to R: in ISSD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; abolishes H(+)-coupled sialic acid transporter activity; has normal L-aspartate and L-glutamate transporter activity; dbSNP:rs119491109
- LL 198:199 (≠ AV 141:142) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ IR 208:209) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ KEARQ 223:227) natural variant: Missing (in ISSD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; abolishes H(+)-coupled sialic acid transporter activity; has normal L-aspartate and L-glutamate transporter activity)
- G328 (= G279) to E: in ISSD; some patients may manifest a milder phenotype consistent with Salla disease; markedly decreases H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs386833996
- P334 (= P285) to R: in ISSD; does not affect intracellular localization, targeted to lysosomes; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs119491110
- G371 (= G321) to V: in ISSD; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs777862172
Sites not aligning to the query:
- 22:23 Dileucine internalization motif; LL→AA: Targeted to plasma membrane.; LL→GG: Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH.
- 39 R → C: in SD; frequent variant in Finland; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transport activity, but retains appreciable H(+)-coupled sialic acid and nitrate transporter activity; dbSNP:rs80338794
Q8BN82 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Solute carrier family 17 member 5; Vesicular excitatory amino acid transporter; VEAT from Mus musculus (Mouse) (see paper)
25% identity, 86% coverage: 28:395/430 of query aligns to 83:447/495 of Q8BN82
- H183 (≠ N126) mutation to R: Abolishes sialic acid transporter activity. Does not affect L-aspartate and L-glutamate transporter activity.
Sites not aligning to the query:
- 39 R→C: Completely abolishes L-aspartate and L-glutamate transporter activity. Retains appreciable H(+)-coupled sialic acid transporter activity.
Q5Q0U0 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Solute carrier family 17 (Anion/sugar transporter), member 5; Vesicular excitatory amino acid transporter; VEAT from Rattus norvegicus (Rat) (see 2 papers)
25% identity, 86% coverage: 28:395/430 of query aligns to 83:447/495 of Q5Q0U0
- K136 (≠ R81) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- R168 (= R111) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ T114) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G115) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E118) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ A119) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (= F122) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P123) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ N126) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ V129) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SS---------LKN 268:272 (≠ DGGGLVDGDAPVKK 210:223) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P285) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- G371 (= G321) mutation to V: Remains in the endoplasmic reticulum.
Sites not aligning to the query:
- 22:23 Dileucine internalization motif; LL→AA: Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH.
- 39 R→C: Markedly decreases H(+)-coupled sialic acid transporter activity.
Q9JI12 Vesicular glutamate transporter 2; VGluT2; Differentiation-associated BNPI; Differentiation-associated Na(+)-dependent inorganic phosphate cotransporter; Solute carrier family 17 member 6 from Rattus norvegicus (Rat) (see 2 papers)
24% identity, 90% coverage: 13:398/430 of query aligns to 69:470/582 of Q9JI12
- R88 (= R32) mutation to A: Impairs synaptic transmission. Abolishes the chloride ion conductance.
- H128 (≠ F57) mutation to A: Greatly lowers L-glutamate transport.
- R184 (= R111) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E118) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ V252) mutation to A: Loss of L-glutamate release. Abolishes the chloride ion conductance.
7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
23% identity, 90% coverage: 13:398/430 of query aligns to 11:412/452 of 7t3nA
- binding (1s,3r)-1-aminocyclopentane-1,3-dicarboxylic acid: Y77 (= Y64), Y137 (≠ F122), Y165 (≠ F150), R264 (≠ V252), F268 (≠ L256), Y269 (≠ W257)
- binding (2R)-2-(methoxymethyl)-4-{[(25R)-spirost-5-en-3beta-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside: R12 (= R14), Y13 (= Y15), E152 (= E137), G163 (= G148)
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
24% identity, 90% coverage: 10:395/430 of query aligns to 12:430/493 of Q03567
- N69 (≠ S39) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q9Y2C5 Probable small intestine urate exporter; Solute carrier family 17 member 4 from Homo sapiens (Human) (see 2 papers)
25% identity, 87% coverage: 53:427/430 of query aligns to 110:486/497 of Q9Y2C5
- A372 (≠ I319) to T: in dbSNP:rs11754288
Sites not aligning to the query:
- 66 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-75 and A-90.
- 75 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-66 and A-90.
- 90 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-75 and A-90.
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
24% identity, 41% coverage: 5:182/430 of query aligns to 11:188/452 of Q5EXK5
- D82 (= D76) mutation to A: Loss of activity.
Sites not aligning to the query:
- 311 V→W: Loss of activity.
- 314 D→A: Loss of activity.
Q9GQQ0 Protein spinster; Protein benchwarmer; Protein diphthong from Drosophila melanogaster (Fruit fly) (see paper)
20% identity, 92% coverage: 3:398/430 of query aligns to 102:488/605 of Q9GQQ0
- E217 (= E118) mutation to K: In bnch(N); leads to storage in yolk spheres during oogenesis and results in widespread accumulation of enlarged lysosomal and late endosomal inclusions.
P0AGC0 Hexose-6-phosphate:phosphate antiporter from Escherichia coli (strain K12) (see paper)
21% identity, 93% coverage: 1:398/430 of query aligns to 13:413/463 of P0AGC0
- C108 (≠ L96) mutation to S: No change in activity.
- C143 (≠ T124) mutation to S: 30% of wild-type sugar phosphate transport activity.
- C265 (≠ A251) mutation to S: No change in activity.
- C331 (= C320) mutation to S: No change in activity.
Sites not aligning to the query:
- 436 C→S: No change in activity.
- 438 C→S: No change in activity.
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
22% identity, 40% coverage: 5:177/430 of query aligns to 18:190/448 of Q51955
- D41 (≠ C28) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (= D31) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (= G72) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (= D76) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G79) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to C: No change in 4-HBA transport and chemotaxis.; mutation G->L,V: Abolishes 4-HBA transport and chemotaxis.; mutation to Q: Decrease in 4-HBA transport and strong decrease in chemotaxis.
- R124 (= R111) mutation to A: Abolishes 4-HBA transport.
- E144 (≠ S131) mutation to A: Strong decrease in 4-HBA transport.
- H183 (= H170) mutation to A: Decrease in 4-HBA transport and chemotaxis.
Sites not aligning to the query:
- 323 D→N: Abolishes 4-HBA transport and chemotaxis.
- 328 H→A: Decrease in 4-HBA transport and chemotaxis.; H→R: Decrease in 4-HBA transport and loss of chemotaxis.
- 386 R→A: Strong decrease in 4-HBA transport.
- 398 R→A: Abolishes 4-HBA transport.
- 444 H→A: No change in 4-HBA transport and chemotaxis.
Query Sequence
>17750 b3691 D-galactonate transport (VIMSS)
MDIPVNAAKPGRRRYLTLVMIFITVVICYVDRANLAVASAHIQEEFGITKAEMGYVFSAF
AWLYTLCQIPGGWFLDRVGSRVTYFIAIFGWSVATLFQGFATGLMSLIGLRAITGIFEAP
AFPTNNRMVTSWFPEHERASAVGFYTSGQFVGLAFLTPLLIWIQEMLSWHWVFIVTGGIG
IIWSLIWFKVYQPPRLTKGISKAELDYIRDGGGLVDGDAPVKKEARQPLTAKDWKLVFHR
KLIGVYLGQFAVASTLWFFLTWFPNYLTQEKGITALKAGFMTTVPFLAAFVGVLLSGWVA
DLLVRKGFSLGFARKTPIICGLLISTCIMGANYTNDPMMIMCLMALAFFGNGFASITWSL
VSSLAPMRLIGLTGGVFNFAGGLGGITVPLVVGYLAQGYGFAPALVYISAVALIGALSYI
LLVGDVKRVG
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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