SitesBLAST
Comparing GFF2851 FitnessBrowser__Marino:GFF2851 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 9 hits to proteins with known functional sites (download)
P54582 Glycine betaine transporter BetP; Glycine betaine permease from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see 6 papers)
37% identity, 97% coverage: 5:520/531 of query aligns to 40:547/595 of P54582
- W101 (= W70) mutation to A: Mainly monomeric, shows a decrease in activity and cannot be activated in response to increased osmolality; when associated with A-351.
- E135 (= E104) mutation to A: Strongly decreased betaine transport.
- G149 (= G118) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (= M119) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (= G120) mutation to A: Nearly abolishes betaine transport.
- I152 (≠ T121) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (≠ TG 121:122) binding
- G153 (= G122) mutation to A: Decreases betaine transport and alters activation at higher osmolality.; mutation to D: Changes substrate specificity, giving rise to proton-coupled choline transport. Decreases sodium-dependent betaine transport.
- F156 (= F125) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (= W164) mutation to C: Mildly decreased betaine transport.
- W194 (= W169) mutation to L: Strongly decreased betaine transport.
- Y197 (= Y172) mutation to L: Nearly abolishes betaine transport.
- R210 (≠ N185) mutation to A: Nearly abolishes betaine transport.
- S253 (= S227) binding
- G301 (= G274) mutation to L: Strongly decreased betaine transport.
- N309 (= N282) mutation to A: Decreases affinity for sodium ions.
- T351 (≠ F324) mutation to A: Mainly trimeric, but shows reduced activity at high osmolalities. Mainly monomeric, shows a decrease in activity and cannot be activated in response to increased osmolality; when associated with A-101.
- W362 (= W332) mutation to C: Strongly decreased betaine transport.
- W366 (= W336) mutation to C: No effect on betaine transport.
- F369 (= F339) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
- W371 (= W341) mutation to L: No effect on betaine transport.
- W373 (= W343) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
- WWISW 373:377 (= WWISW 343:347) binding
- W374 (= W344) mutation to A: Strongly decreases betaine transport, but has no major effect on affinity for glycine betaine.; mutation to L: No effect on betaine transport.
- W377 (= W347) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (= F350) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- F384 (= F354) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- R387 (= R357) mutation to A: Mildly decreased betaine transport.
- R392 (= R362) mutation to K: Moderately decreased betaine transport.
3p03C Crystal structure of betp-g153d with choline bound (see paper)
38% identity, 91% coverage: 37:520/531 of query aligns to 12:487/508 of 3p03C
4llhA Substrate bound outward-open state of the symporter betp (see paper)
38% identity, 91% coverage: 37:520/531 of query aligns to 12:488/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (= M119), G95 (= G120), D97 (≠ G122), W314 (= W343), W315 (= W344), W318 (= W347)
- binding sodium ion: A91 (= A116), M94 (= M119), G95 (= G120), F405 (= F437), T408 (= T440), S409 (= S441)
Sites not aligning to the query:
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
29% identity, 86% coverage: 57:515/531 of query aligns to 38:501/508 of 2wswA
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
29% identity, 86% coverage: 57:515/531 of query aligns to 25:488/495 of 4m8jA
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
29% identity, 86% coverage: 57:515/531 of query aligns to 33:496/514 of B4EY22
- E111 (= E130) mutation to A: Abolishes transport activity.
- R262 (≠ N282) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W336) mutation to A: 2.5-fold decrease in Vmax.
- M331 (≠ V351) mutation to V: 10-fold decrease in Vmax.
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
28% identity, 82% coverage: 86:522/531 of query aligns to 62:496/496 of 2wsxA
3hfxA Crystal structure of carnitine transporter (see paper)
28% identity, 82% coverage: 86:522/531 of query aligns to 58:492/493 of 3hfxA
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
28% identity, 82% coverage: 86:522/531 of query aligns to 69:503/504 of P31553
- Y114 (= Y134) binding ; mutation to L: Small decrease in transport activity.
- W142 (= W164) binding
- D288 (= D308) mutation to A: Retains 70% of transport activity. Forms mostly monomers.; mutation to R: Abolishes transport activity. Forms mostly monomers.; mutation to W: Retains 4% of transport activity. Forms mostly monomers.
- M295 (≠ S312) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (≠ N316) mutation to A: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers. Shows a high tendency to aggregate.
- T304 (≠ S321) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- GW 315:316 (= GW 335:336) binding
- W316 (= W336) mutation to L: Decrease in transport activity.
- W323 (= W343) binding ; mutation to L: Abolishes transport activity.
- WW 323:324 (= WW 343:344) binding
- W324 (= W344) mutation to L: Abolishes transport activity.
- Y327 (≠ W347) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ WSPF 347:350) binding
- Q330 (≠ F350) mutation to L: Decrease in transport activity.
- M331 (≠ V351) binding
Query Sequence
>GFF2851 FitnessBrowser__Marino:GFF2851
MGDVISDDYQTDYVAGQDNIEKFGFDIHNIVFPLTAILIVAFVVGTLIFPAGAKELLDSA
KNGAIAVFDWGFLLSANLFVVFCLALIFMPVGKIRIGGLDAKPEFSLLSWFAMLFAAGMG
TGLMFWSVAEPVAYYTDWYGTPLGVEPNTAEGARLAMGATMYHWGLHPWAIYAIVGLSLS
FFAFNKGLPLTIRSAFFPILGDKVWGWPGNVIDTVSVLATIFGLATSLGFGAQQAASGIS
YLFDIEGGLNIQVGVIAGVTAVATLSVIRGIHGGVRILSNANMIMAGLLLLFVIFAGPTL
AVFQWLWDTSVSYASNMFSLSNPFGREEDTTWFHGWTVFYWAWWISWSPFVGMFIARVSH
GRTVREFVTAVLIIPTIITLFWMSAFGGGALNQVQNEIGVLGSEGLTEVSLAMFQMLENI
SLSGITSFIGITLVLTFFVTSSDSGSLVIDSITSGGKTDAPKAQRIFWAVTEGTIAGVLL
FVGGEQALNALQAGALSVGLPFTLVLLVMTYSLFKGLHHERRLLIAEGKMV
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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