SitesBLAST
Comparing RR42_RS29530 FitnessBrowser__Cup4G11:RR42_RS29530 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 7 hits to proteins with known functional sites (download)
P94363 Citrate/malate-proton symporter; CimHbs; Citrate/malate transporter from Bacillus subtilis (strain 168) (see paper)
59% identity, 97% coverage: 12:447/451 of query aligns to 9:446/450 of P94363
- R143 (= R145) mutation to C: No change in citrate uptake activity.
- C231 (≠ T233) mutation to S: Retains 75% of specific activity for citrate transport. Retains 52% of specific activity for citrate transport; when associated with S-402.
- C402 (= C403) mutation to S: Retains 55% of specific activity for citrate transport. Retains 52% of specific activity for citrate transport; when associated with S-231.
- R420 (= R421) mutation to C: No change in citrate uptake activity.
- Q428 (= Q429) mutation to C: No change in citrate uptake activity.
- R432 (= R433) mutation to C: Loss of citrate uptake activity.; mutation to K: Retains 5% of citrate uptake activity. 30-fold increase in KM for citrate, but Vmax is not significantly altered.
P31602 Citrate/sodium symporter; Citrate transporter CitS; Na(+)-dependent citrate carrier; Sodium-dependent citrate transport system from Klebsiella pneumoniae (see 3 papers)
29% identity, 99% coverage: 4:450/451 of query aligns to 2:445/446 of P31602
- I181 (= I192) binding Na(+)
- G183 (≠ A194) binding Na(+)
- N186 (≠ V197) binding citrate; mutation to V: 9-fold increase in KM for citrate, but no change in Vmax. The effect of Na(+) on the transport kinetics are comparable to the wild-type.
- G187 (= G198) binding citrate
- E195 (≠ I206) mutation to Q: Almost no effect on the kinetics of Na(+) or citrate transport.
- C278 (≠ L291) mutation to S: Retains 79% of specific activity, response to various thiol reagents is not affected; when associated with S-317 and S-347.
- C317 (vs. gap) mutation to S: Retains 79% of specific activity, response to various thiol reagents is not affected; when associated with S-278 and S-347.
- C347 (≠ A353) mutation to S: Retains 79% of specific activity, response to various thiol reagents is not affected; when associated with S-278 and S-317.
- C398 (= C403) mutation to S: Retains 56% of specific activity and is quite insensitive to NEM, MTSET and MTSES; when associated with S-414.
- M399 (≠ H404) binding Na(+)
- N401 (≠ G406) binding Na(+)
- R402 (≠ Q407) binding citrate
- G404 (= G409) binding citrate
- S405 (≠ T410) binding citrate
- C414 (≠ A419) mutation to S: Retains 56% of specific activity and is quite insensitive to NEM, MTSET and MTSES; when associated with S-398.
- R428 (= R433) binding citrate
5a1sD Crystal structure of the sodium-dependent citrate symporter secits form salmonella enterica. (see paper)
29% identity, 94% coverage: 29:450/451 of query aligns to 3:431/434 of 5a1sD
- binding citrate anion: L323 (≠ T343), G389 (= G408), G390 (= G409), S391 (≠ T410)
- binding sodium ion: I167 (= I192), M168 (= M193), G169 (≠ A194), C384 (= C403), M385 (≠ H404), M385 (≠ H404), A386 (≠ S405), N387 (≠ G406), N387 (≠ G406), G389 (= G408), D393 (= D412), S413 (≠ T432)
5x9rA Structural insights into the elevator-like mechanism of the sodium/citrate symporter cits (see paper)
30% identity, 93% coverage: 33:450/451 of query aligns to 1:416/416 of 5x9rA
- binding beta-D-glucopyranose: A108 (≠ S139), V112 (≠ M143), E225 (≠ R256), N389 (≠ T423), Y393 (≠ F427)
- binding citrate anion: G165 (= G196), N166 (≠ V197), Y319 (≠ M354), R373 (≠ Q407), G375 (= G409), S376 (≠ T410), R399 (= R433)
5xarD Structural insights into the elevator-like mechanism of the sodium/citrate symporter cits (see paper)
28% identity, 94% coverage: 25:450/451 of query aligns to 1:410/411 of 5xarD
5xasB Structural insights into the elevator-like mechanism of the sodium/citrate symporter cits (see paper)
28% identity, 94% coverage: 29:450/451 of query aligns to 2:406/407 of 5xasB
Q48769 Citrate transporter CitP; Citrate carrier; Citrate/lactate antiporter from Leuconostoc mesenteroides subsp. mesenteroides (see paper)
29% identity, 95% coverage: 24:450/451 of query aligns to 16:442/443 of Q48769
- R425 (= R433) mutation to C: Exchange is severely affected with (S)-malate as substrate. Affinity for divalent (S)-malate is strongly decreased. 20-fold increase in affinity for monovalent 2-hydroxyisobutyrate. Chemical modification of the mutant with the sulfhydryl reagent 2-aminoethyl methanethiosulfonate, which restores the positive charge at position 425, can largely restore exchange activity.; mutation to K: 10-fold decrease in affinity for divalent (S)-malate. 4-fold increase in affinity for monovalent 2-hydroxyisobutyrate.
Query Sequence
>RR42_RS29530 FitnessBrowser__Cup4G11:RR42_RS29530
MQTTSHTLPPAEAQQTAIKPRFWPEGWWKLMEFRIGIIPLPVYVILLALIAGFAVTGKVP
GEISMAIAVLAFFGFTCAEIGKRLPIIRNIGAAAIFATFIPSALTYYHLLPKPILSLTTE
FTKSTNFLYLFIASIIVGSILSMDRRVLIQGFIKIFIPLAVGSIAAGIVGTAVGTALGLG
AHHTFFYIVVPIMAGGVGEGAIPLSIGYSEILHLPQGDLFAQVLPPVMLGSLTAIILSGV
LDKVGKRFPHLTGEGRLQVGEEDEMDPVQEEIRGHIDVTHIAAAGITAITLYLLGLMCRN
LFGLPAPVAMLFLAVLVKITRAVSPPLQEGAFVVYKFFSTAVTYPLLFAIGVAMTPWDKL
IAAFTLANIVTIVATVTTLMGTGFVVARMLKMHPIDTAIVNACHSGQGGTGDVAILTAAN
RMTLMPFAQIATRIGGAIVVTLTLIVLAHMG
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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