SitesBLAST
Comparing PP_1743 FitnessBrowser__Putida:PP_1743 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 5 hits to proteins with known functional sites (download)
P07117 Sodium/proline symporter; Proline carrier; Proline permease; Propionate transporter from Escherichia coli (strain K12) (see 4 papers)
26% identity, 80% coverage: 42:484/554 of query aligns to 7:462/502 of P07117
- R257 (= R288) mutation to C: Sodium-independent binding affinity for proline.
- C281 (≠ T316) mutation to S: Does not affect proline uptake activity. Confers resistance to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
- C344 (≠ G378) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (≠ G383) mutation to S: Does not affect proline uptake activity. Sensitive to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
- R376 (≠ K411) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.
B4EZY7 Sodium/sialic acid symporter SiaT; Na(+)-coupled sialic acid symporter; Sialic acid transporter from Proteus mirabilis (strain HI4320) (see paper)
22% identity, 50% coverage: 58:336/554 of query aligns to 29:308/496 of B4EZY7
- A56 (≠ G85) binding
- T58 (≠ Y87) mutation to A: 2-fold increase in Neu5Ac transport.
- L59 (≠ M88) binding
- S60 (= S89) mutation to A: Abolishes Neu5Ac transport.
- T63 (≠ S92) mutation to A: Abolishes Neu5Ac transport.
- Q82 (≠ S111) mutation to D: Abolishes Neu5Ac transport.
- R135 (≠ L166) mutation to E: Abolishes Neu5Ac transport.
- D182 (≠ Q212) binding ; mutation to A: Abolishes Neu5Ac transport.
Sites not aligning to the query:
- 339 binding
- 342 binding ; binding ; S→A: Abolishes Neu5Ac transport.
- 343 binding ; S→A: Abolishes Neu5Ac transport.
- 345 binding ; S→A: Reduces Neu5Ac transport.
- 346 binding ; S→A: Slightly increases Neu5Ac transport.
5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
22% identity, 50% coverage: 58:336/554 of query aligns to 25:304/480 of 5nv9A
- binding sodium ion: A52 (≠ G85), T53 (≠ D86), L55 (≠ M88), S56 (= S89), V174 (≠ T208), D178 (≠ Q212)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ Y87), S56 (= S89), I58 (≠ A91), T59 (≠ S92), G77 (≠ Y110), Q78 (≠ S111), R131 (≠ L166), F239 (vs. gap)
Sites not aligning to the query:
Q92911 Sodium/iodide cotransporter; Na(+)/I(-) cotransporter; Natrium iodide transporter; Sodium-iodide symporter; Na(+)/I(-) symporter; Solute carrier family 5 member 5 from Homo sapiens (Human) (see 3 papers)
25% identity, 33% coverage: 42:222/554 of query aligns to 19:201/643 of Q92911
- A102 (≠ L122) natural variant: A -> P
Sites not aligning to the query:
- 226 mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
- 237 D→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
- 242 Required for homodimerization; Y→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471. Loss of iodide transport activity; when associated with F-535.
- 243 Required for homodimerization; T→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471.
- 471 Required for homodimerization; Q→A: No effect on localization to the cell membrane, iodide transport activity and homodimerization. Significant loss of homodimerization; when associated with A-242 or A243.
- 525 A→F: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Loss of iodide transport activity; when associated with A-242.
- 536 T → Q: requires 2 nucleotide substitutions
- 556 S → Q: requires 2 nucleotide substitutions
P11170 Sodium/glucose cotransporter 1; Na(+)/glucose cotransporter 1; High affinity sodium-glucose cotransporter; Solute carrier family 5 member 1 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
19% identity, 82% coverage: 29:482/554 of query aligns to 18:501/662 of P11170
- C255 (≠ L261) modified: Disulfide link with 608
- Q457 (≠ F441) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (≠ A444) mutation to W: Decreased affinity for glucose and phlorizin.
Sites not aligning to the query:
- 608 modified: Disulfide link with 255
Query Sequence
>PP_1743 FitnessBrowser__Putida:PP_1743
MIRQVKALAVLACGAFAPAVWAADALTGEVQKQPLNVSAIAMFVAFVAFTLGITYWASKR
NKSASDYYAAGGKITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSIGFLVGWPI
ILFLIAERLRNLGKYTFADVASYRLGQKEIRTLSASGSLVVVAFYLIAQMVGAGKLIELL
FGLDYHVAVILVGILMCLYVLFGGMLATTWVQIIKAVLLLSGASFMALMVMKHVGFDFNT
LFSEAIKVHAKGEAIMSPGGLVKDPISAFSLGLALMFGTAGLPHILMRFFTVSDAKEARK
SVLYATGFIGYFYILTFIIGFGAILLVSTNPEFKDAAGALLGGNNMAAVHLANAVGGSVF
LGFISAVAFATILAVVAGLTLAGASAVSHDLYASVWRKGKANDKDEIRVSKITTVALGVL
AIGLGILFEKQNIAFMVGLAFSIAASCNFPVLLLSMYWKKLTTRGAMIGGWLGLVSAVTL
MILGPTIWVQILGHEKPIYPYEYPALFSMAIAFVSIWFFSVTDKSKAAEDERALFFPQFV
RSQTGLGASGAVSH
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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