SitesBLAST
Comparing Pf6N2E2_1312 4-hydroxyphenylacetate symporter, major facilitator superfamily (MFS) 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)
P53322 High-affinity nicotinic acid transporter; Nicotinic acid permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
25% identity, 71% coverage: 26:331/434 of query aligns to 92:399/534 of P53322
- K283 (≠ P219) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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, 45% coverage: 118:314/434 of query aligns to 166:355/495 of Q5Q0U0
- R168 (= R120) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ L123) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G124) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E127) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ A128) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (= F131) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P132) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ L135) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ L138) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ EQLSL 227:231) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P293) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
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.
- 136 K→E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- 371 G→V: Remains in the endoplasmic reticulum.
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, 45% coverage: 118:314/434 of query aligns to 166:355/495 of Q8BN82
- H183 (≠ L135) 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.
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)
22% identity, 65% coverage: 50:329/434 of query aligns to 96:372/495 of Q9NRA2
- K136 (≠ R90) 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 (≠ L135) 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 (≠ VT 150:151) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ LR 225:226) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ EQLSL 227:231) 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 (= G287) 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 (= P293) 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 (= G328) 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
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
26% identity, 84% coverage: 24:386/434 of query aligns to 28:402/448 of Q51955
- D41 (= D40) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (≠ N43) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (≠ N81) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (= D85) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G88) 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 (= R120) mutation to A: Abolishes 4-HBA transport.
- E144 (≠ R140) mutation to A: Strong decrease in 4-HBA transport.
- H183 (≠ Q186) mutation to A: Decrease in 4-HBA transport and chemotaxis.
- D323 (= D309) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- H328 (≠ R314) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to R: Decrease in 4-HBA transport and loss of chemotaxis.
- R386 (≠ Q373) mutation to A: Strong decrease in 4-HBA transport.
- R398 (≠ S382) mutation to A: Abolishes 4-HBA transport.
Sites not aligning to the query:
- 444 H→A: No change in 4-HBA transport and chemotaxis.
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
21% identity, 80% coverage: 85:433/434 of query aligns to 82:437/452 of Q5EXK5
- D82 (= D85) mutation to A: Loss of activity.
- V311 (≠ R306) mutation to W: Loss of activity.
- D314 (= D309) mutation to A: Loss of activity.
6zguA Crystal structure of a mfs transporter with bound 3-(2-methylphenyl) propanoic acid at 2.41 angstroem resolution
24% identity, 82% coverage: 73:427/434 of query aligns to 54:389/404 of 6zguA
6zgtA Crystal structure of a mfs transporter with bound 2-naphthoic acid at 2.39 angstroem resolution
24% identity, 82% coverage: 73:427/434 of query aligns to 54:389/404 of 6zgtA
Sites not aligning to the query:
6zgsA Crystal structure of a mfs transporter with bound 3-phenylpropanoic acid at 2.39 angstroem resolution
24% identity, 82% coverage: 73:427/434 of query aligns to 54:389/404 of 6zgsA
6g9xA Crystal structure of a mfs transporter at 2.54 angstroem resolution (see paper)
24% identity, 82% coverage: 73:427/434 of query aligns to 51:381/396 of 6g9xA
A0LNN5 L-lactate transporter; SfMCT from Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB) (see paper)
23% identity, 82% coverage: 73:427/434 of query aligns to 60:405/412 of A0LNN5
- Y119 (≠ F137) binding ; mutation Y->A,F: Loss of transport activity.
- L145 (≠ V158) mutation to A: Strong decrease in transport activity.
- H250 (= H276) mutation to A: Strong decrease in transport activity.; mutation to F: Loss of transport activity.
- R256 (≠ S282) mutation to A: No change in transport activity.; mutation to D: Increases transport activity.
- D257 (= D283) mutation to A: Loss of transport activity.
- N276 (vs. gap) mutation to A: Loss of transport activity.
- R280 (≠ M301) binding ; mutation to A: Abolishes L-lactate binding and L-lactate transport.
- Y331 (≠ A353) mutation to A: Loss of transport activity.; mutation to F: No change in transport activity.
- F335 (≠ L357) mutation to A: Increases transport activity.
- F359 (≠ S381) mutation to A: Loss of transport activity.
- C362 (≠ G384) mutation to A: Decrease in transport activity.
- K377 (≠ R399) mutation K->A,D: No change in transport activity.
- D378 (= D400) mutation to A: Loss of transport activity.
- Y383 (≠ A405) mutation to A: Loss of transport activity.; mutation to F: Strong decrease in transport activity.
Sites not aligning to the query:
- 28 L→A: Loss of transport activity.
6zgrA Crystal structure of a mfs transporter with bound 1- hydroxynaphthalene-2-carboxylic acid at 2.67 angstroem resolution
23% identity, 86% coverage: 54:427/434 of query aligns to 33:384/399 of 6zgrA
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
22% identity, 62% coverage: 29:296/434 of query aligns to 9:269/409 of 6e9nA
Sites not aligning to the query:
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
22% identity, 70% coverage: 118:422/434 of query aligns to 141:456/493 of Q03567
Sites not aligning to the query:
- 69 modified: carbohydrate, N-linked (GlcNAc...) asparagine
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
22% identity, 62% coverage: 29:296/434 of query aligns to 20:288/430 of P0AA76
- Y29 (≠ H38) binding
- D31 (= D40) mutation to N: Loss of galactonate transport activity.
- R32 (= R41) binding
- Y64 (= Y73) binding
- E118 (= E127) mutation to Q: Loss of galactonate transport activity.
Sites not aligning to the query:
6zgrB Crystal structure of a mfs transporter with bound 1- hydroxynaphthalene-2-carboxylic acid at 2.67 angstroem resolution
24% identity, 82% coverage: 73:427/434 of query aligns to 48:362/364 of 6zgrB
6zguB Crystal structure of a mfs transporter with bound 3-(2-methylphenyl) propanoic acid at 2.41 angstroem resolution
24% identity, 82% coverage: 73:427/434 of query aligns to 48:363/364 of 6zguB
6zgtB Crystal structure of a mfs transporter with bound 2-naphthoic acid at 2.39 angstroem resolution
24% identity, 82% coverage: 73:427/434 of query aligns to 48:363/364 of 6zgtB
Sites not aligning to the query:
6zgsB Crystal structure of a mfs transporter with bound 3-phenylpropanoic acid at 2.39 angstroem resolution
24% identity, 82% coverage: 73:427/434 of query aligns to 48:363/364 of 6zgsB
Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
19% identity, 64% coverage: 2:279/434 of query aligns to 15:283/444 of Q8NLB7
- D54 (= D40) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- D57 (≠ N43) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- R103 (= R86) mutation to A: Loss of transport activity.
Sites not aligning to the query:
- 309 W→V: Loss of transport activity.
- 312 D→A: Loss of transport activity.
- 313 R→A: Loss of transport activity.
- 317 mutation I->H,Y: Loss of transport activity.
- 386 R→A: Loss of transport activity.
Query Sequence
>Pf6N2E2_1312 4-hydroxyphenylacetate symporter, major facilitator superfamily (MFS)
MSTAHTANTAGTVAHDRTHATITWRLMPLLLVCYLFAHLDRINIGFAKMQMSADLQFSDT
VYGFGAGLFFIAYALFGVPSNMALDRVGPRRWIATLMVVWGALSSGMFLIDSAAGFYVLR
FLLGVAEAGFFPGILVFLNRWYPARRRAQVTALFAIAVPMAGVIGGPLSGGILEHFHDVG
GLRGWQWMFVIEGLPVILLGLVVLKCLPDDFETVKWLTPHAKQQLREQLSLEEQRKSITS
FSAILNNPQVWLLVAVYFAVMLAVNTLAFWMPTLIHGAGIGSDGKVGLLSAVPYLAGCFF
MIGCGRSSDRHRERRWHLCVPLLMAALGIAVTGLSPGNPILVLSGLIVAGMGASAALPMF
WQLPPAFLSNGTQAAGIALISSFGSIASFFAPYLIGWMRDTTQSASLALYALALLIALGG
LLVLRTHAAIVNPQ
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