SitesBLAST

Comparing WP_049988637.1 NCBI__GCF_000784335.1:WP_049988637.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 13 hits to proteins with known functional sites

7t9gA Structure of vcindy-na+ (see paper)
34% identity, 90% coverage: 43:527/541 of query aligns to 32:439/445 of 7t9gA

• binding sodium ion: S129 (= S141), S133 (= S145), N134 (= N146), G182 (= G225), T356 (= T436), A359 (≠ T439), S360 (= S440), N361 (= N441), A403 (= A491)

6wtxA Structure of vcindy in complex with terephthalate (see paper)
34% identity, 90% coverage: 43:527/541 of query aligns to 32:439/445 of 6wtxA

• binding sodium ion: S129 (= S141), S133 (= S145), N134 (= N146), G176 (= G219), G182 (= G225), T356 (= T436), A359 (≠ T439), S360 (= S440), N361 (= N441), A403 (= A491)
• binding terephthalic acid: N134 (= N146), S183 (≠ T226), S360 (= S440), N361 (= N441), T362 (≠ A442), T404 (= T492)

6okzB Structure of vcindy bound to fumarate
34% identity, 90% coverage: 43:527/541 of query aligns to 31:438/444 of 6okzB

• binding fumaric acid: N133 (= N146), S182 (≠ T226), P183 (= P227), S359 (= S440), N360 (= N441), T361 (≠ A442)

Q28615 Solute carrier family 13 member 2; Na(+)/dicarboxylate cotransporter 1; NaDC-1; Renal sodium/dicarboxylate cotransporter from Oryctolagus cuniculus (Rabbit) (see paper)
32% identity, 89% coverage: 41:519/541 of query aligns to 40:549/593 of Q28615

• L83 (≠ F87) mutation to C: Decreases cell membrane expression. Decreases succinate transport activity. Decreases Km value for succinate.
• T86 (≠ H90) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity.
• Y228 (= Y213) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity.
• Y432 (≠ I393) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity. Decreases Km value for succinate. More sensitive to inhibition by lithium.
• T474 (= T436) mutation to C: Does not affect cell membrane localization. Abolishes succinate transport activity.
• N525 (= N495) mutation to C: Decreases cell membrane expression. Decreases succinate transport activity.
• M539 (= M509) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity. Insensitive to inhibition by lithium.

Q86YT5 Na(+)/citrate cotransporter; NaCT; Sodium-coupled citrate transporter; Sodium-dependent citrate transporter; Solute carrier family 13 member 5 from Homo sapiens (Human) (see 5 papers)
34% identity, 87% coverage: 50:519/541 of query aligns to 46:535/568 of Q86YT5

• T142 (= T147) to M: in DEE25; no loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs761917087
• G219 (= G218) to E: loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs150024888; to R: in DEE25; loss of function in citrate transport; loss of localization to plasma membrane; dbSNP:rs144332569
• T227 (= T226) to M: in DEE25; loss of function in citrate transport; no effect on localization to plasma membrane; dbSNP:rs587777577
• D243 (= D241) to N: no effect on localization to plasma membrane; no effect on its function in citrate transport; dbSNP:rs142262032
• G409 (= G384) mutation to Q: No effect on its function in citrate transport.
• I410 (≠ T385) mutation I->A,F: Significant loss of function in citrate transport.; mutation to V: No effect on its function in citrate transport.
• L420 (= L395) to P: loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs150738356
• S427 (≠ T402) to L: in DEE25; loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs548065551
• L485 (= L465) to R: no effect on localization to plasma membrane; reduced function in citrate transport; increased Km and Vmax values compared with that of wild type with citrate as substrate; dbSNP:rs148049520
• L488 (= L472) to P: in DEE25; loss of function in citrate transport; loss of localization to plasma membrane; dbSNP:rs587777578
• D524 (≠ H508) to H: in DEE25; loss of function in citrate transport; no effect on localization to plasma membrane; dbSNP:rs863225448

Sites not aligning to the query:

• 341:568 natural variant: Missing (in DEE25; loss of localization to plasma membrane; loss of function in citrate transport)
• 562 modified: carbohydrate, N-linked (GlcNAc...) asparagine

7jsjA Structure of the nact-pf2 complex (see paper)
33% identity, 89% coverage: 37:519/541 of query aligns to 24:441/468 of 7jsjA

• binding sodium ion: S124 (= S141), I127 (≠ V144), S128 (= S145), N129 (= N146), G172 (= G225), T366 (= T436), T369 (= T439), S370 (= S440), N371 (= N441), A413 (= A491), T414 (= T492)
• binding (2R)-2-[2-(4-tert-butylphenyl)ethyl]-2-hydroxybutanedioic acid: N129 (= N146), T130 (= T147), T173 (= T226), G315 (= G384), I316 (≠ T385), N371 (= N441)

4f35B Crystal structure of a bacterial dicarboxylate/sodium symporter (see paper)
33% identity, 90% coverage: 43:527/541 of query aligns to 31:408/414 of 4f35B

• binding sodium ion: S122 (= S141), I125 (≠ V144), S126 (= S145), N127 (= N146), G164 (= G219), G170 (= G225), S171 (≠ T226)

8w6nA Nas1 with sulfate in in/out state (see paper)
31% identity, 89% coverage: 45:524/541 of query aligns to 37:470/494 of 8w6nA

• binding sodium ion: S132 (= S141), N137 (= N146), G181 (= G219), G187 (= G225), T188 (= T226)

8w6nB Nas1 with sulfate in in/out state (see paper)
31% identity, 89% coverage: 45:524/541 of query aligns to 33:458/481 of 8w6nB

• binding sulfate ion: N133 (= N146), T134 (= T147), T181 (= T226), S182 (≠ P227)

8w6hA Nas1 with sulfate - in/in state (see paper)
29% identity, 89% coverage: 45:524/541 of query aligns to 32:439/462 of 8w6hA