SitesBLAST
Comparing PP_3940 FitnessBrowser__Putida:PP_3940 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)
P53322 High-affinity nicotinic acid transporter; Nicotinic acid permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
25% identity, 73% coverage: 18:335/437 of query aligns to 82:394/534 of P53322
- K283 (≠ A221) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
24% identity, 80% coverage: 87:436/437 of query aligns to 82:436/452 of Q5EXK5
- D82 (≠ Q87) mutation to A: Loss of activity.
- V311 (≠ A310) mutation to W: Loss of activity.
- D314 (= D313) mutation to A: Loss of 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)
21% identity, 61% coverage: 52:318/437 of query aligns to 96:355/495 of Q9NRA2
- K136 (= K92) 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 (≠ L137) 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 (≠ II 152:153) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ LA 227:228) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ ADLAA 229:233) 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 (= G291) 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 (= P297) 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
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
- 371 G → V: in ISSD; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs777862172
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
23% identity, 72% coverage: 40:353/437 of query aligns to 18:328/409 of 6e9nA
Sites not aligning to the query:
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
22% identity, 72% coverage: 40:353/437 of query aligns to 29:347/430 of P0AA76
- Y29 (= Y40) binding
- D31 (= D42) mutation to N: Loss of galactonate transport activity.
- R32 (= R43) binding
- Y64 (= Y75) binding
- E118 (= E129) mutation to Q: Loss of galactonate transport activity.
Sites not aligning to the query:
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)
23% identity, 57% coverage: 69:318/437 of query aligns to 113:355/495 of Q8BN82
- H183 (≠ L137) 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.
Q9C0U9 Uncharacterized transporter PB1C11.03 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
20% identity, 59% coverage: 11:267/437 of query aligns to 81:343/570 of Q9C0U9
Sites not aligning to the query:
- 14 modified: Phosphoserine
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)
22% identity, 65% coverage: 55:339/437 of query aligns to 99:378/495 of Q5Q0U0
- K136 (= K92) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- R168 (= R122) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ L125) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G126) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E129) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ A130) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (≠ L133) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P134) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ L137) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ L140) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ ADLAA 229:233) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P297) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- G371 (≠ A332) 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.
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
22% identity, 72% coverage: 40:353/437 of query aligns to 21:312/393 of 6e9oA
Sites not aligning to the query:
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
21% identity, 82% coverage: 22:380/437 of query aligns to 24:389/448 of Q51955
- D41 (= D42) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (≠ N45) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (≠ N83) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (≠ Q87) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G90) 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 (= R122) mutation to A: Abolishes 4-HBA transport.
- E144 (≠ M142) mutation to A: Strong decrease in 4-HBA transport.
- H183 (≠ Q188) mutation to A: Decrease in 4-HBA transport and chemotaxis.
- D323 (= D313) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- H328 (≠ R318) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to R: Decrease in 4-HBA transport and loss of chemotaxis.
- R386 (≠ A377) mutation to A: Strong decrease in 4-HBA transport.
Sites not aligning to the query:
- 398 R→A: Abolishes 4-HBA transport.
- 444 H→A: No change in 4-HBA transport and chemotaxis.
Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
23% identity, 64% coverage: 42:319/437 of query aligns to 57:318/444 of Q8NLB7
- D57 (= D42) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- R103 (= R88) mutation to A: Loss of transport activity.
- W309 (≠ A310) mutation to V: Loss of transport activity.
- D312 (= D313) mutation to A: Loss of transport activity.
- R313 (= R314) mutation to A: Loss of transport activity.
- I317 (≠ R318) mutation I->H,Y: Loss of transport activity.
Sites not aligning to the query:
- 54 D→A: Loss of transport activity.; D→E: Retains 50% of its transport activity.
- 386 R→A: Loss of transport 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)
21% identity, 59% coverage: 44:299/437 of query aligns to 104:357/582 of Q9JI12
- H128 (≠ A68) mutation to A: Greatly lowers L-glutamate transport.
- R184 (= R122) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E129) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ I264) mutation to A: Loss of L-glutamate release. Abolishes the chloride ion conductance.
Sites not aligning to the query:
- 88 R→A: Impairs synaptic transmission. Abolishes the chloride ion conductance.
7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
20% identity, 63% coverage: 43:319/437 of query aligns to 30:319/452 of 7t3nA
Sites not aligning to the query:
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
21% identity, 81% coverage: 71:426/437 of query aligns to 90:456/493 of Q03567
Sites not aligning to the query:
- 69 modified: carbohydrate, N-linked (GlcNAc...) asparagine
Query Sequence
>PP_3940 FitnessBrowser__Putida:PP_3940
MPIANATTVHSDIDHGTKALYSKITWRLIPFLCFCYLAAYLDRINVGFAKLQMLEDLQFS
TAAYGLGAGLFFVGYIIFEVPSNLILQRVGAKLWIARIMITWGLLSACTMFVTSTTQFYI
LRFLLGAAEAGFLPGVLYYLTMWYPTYRRGRIIALFMIGLPLSSVIGGPISGWIMGHFDQ
VQGLHGWQWLFLLEAIPSVLLGILTFWALPNHFQQAKWLSADDKAQLAADLAADDAEGKD
SKHSFRDGFFNLKVWMLGGIDFSILLSAYAMGFWMPTFIRDAGVSDTFHIGLLTAIPSLA
ALAGMLMIGASSDRHRERRWHIIVPFIIGAIAMASSTLFSQNLVMTVVLFAIASAAIIGA
VPVFFSLPATFLKGTAAATGFALACSVANIAGLVSNSLMGVVTDLTGTSHAALWVFAGCL
ILSCFLVIALPAKLVNR
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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