SitesBLAST
Comparing 14452 FitnessBrowser__Keio:14452 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
35% identity, 75% coverage: 33:541/677 of query aligns to 78:594/595 of P54582
- W101 (= W56) 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 (= E90) mutation to A: Strongly decreased betaine transport.
- G149 (= G104) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (≠ I105) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (= G106) mutation to A: Nearly abolishes betaine transport.
- I152 (= I107) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (≠ ID 107:108) binding
- G153 (≠ D108) 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 (= F111) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (≠ Y146) mutation to C: Mildly decreased betaine transport.
- W194 (= W151) mutation to L: Strongly decreased betaine transport.
- Y197 (= Y154) mutation to L: Nearly abolishes betaine transport.
- R210 (= R167) mutation to A: Nearly abolishes betaine transport.
- S253 (≠ T209) binding
- G301 (= G256) mutation to L: Strongly decreased betaine transport.
- N309 (= N264) mutation to A: Decreases affinity for sodium ions.
- T351 (≠ S306) 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 (= W315) mutation to C: Strongly decreased betaine transport.
- W366 (= W319) mutation to C: No effect on betaine transport.
- F369 (= F322) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
- W371 (= W324) mutation to L: No effect on betaine transport.
- W373 (= W326) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
- WWISW 373:377 (≠ WWVAW 326:330) binding
- W374 (= W327) 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 (= W330) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (= F333) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- F384 (= F337) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- R387 (= R340) mutation to A: Mildly decreased betaine transport.
- R392 (= R345) mutation to K: Moderately decreased betaine transport.
4llhA Substrate bound outward-open state of the symporter betp (see paper)
36% identity, 70% coverage: 33:508/677 of query aligns to 22:497/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (≠ I105), G95 (= G106), D97 (= D108), W133 (≠ Y146), W314 (= W326), W315 (= W327), W318 (= W330)
- binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: N42 (≠ T53), W45 (= W56), R495 (= R506)
- binding sodium ion: A91 (= A102), M94 (≠ I105), G95 (= G106), F405 (= F420), T408 (= T423), S409 (= S424)
Sites not aligning to the query:
3p03C Crystal structure of betp-g153d with choline bound (see paper)
36% identity, 70% coverage: 33:508/677 of query aligns to 22:496/508 of 3p03C
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
27% identity, 74% coverage: 5:503/677 of query aligns to 5:506/508 of 2wswA
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
27% identity, 74% coverage: 4:503/677 of query aligns to 1:501/514 of B4EY22
- E111 (= E116) mutation to A: Abolishes transport activity.
- R262 (≠ N264) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W319) mutation to A: 2.5-fold decrease in Vmax.
- M331 (≠ V334) mutation to V: 10-fold decrease in Vmax.
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
27% identity, 73% coverage: 13:503/677 of query aligns to 2:493/495 of 4m8jA
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
26% identity, 74% coverage: 4:501/677 of query aligns to 1:499/504 of P31553
- Y114 (≠ T119) binding ; mutation to L: Small decrease in transport activity.
- W142 (≠ Y146) binding
- D288 (≠ L290) 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 (vs. gap) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (= R298) 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 (= T303) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- GW 315:316 (≠ NW 318:319) binding
- W316 (= W319) mutation to L: Decrease in transport activity.
- W323 (= W326) binding ; mutation to L: Abolishes transport activity.
- WW 323:324 (= WW 326:327) binding
- W324 (= W327) mutation to L: Abolishes transport activity.
- Y327 (≠ W330) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ WSPF 330:333) binding
- Q330 (≠ F333) mutation to L: Decrease in transport activity.
- M331 (≠ V334) binding
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
26% identity, 72% coverage: 13:501/677 of query aligns to 3:492/496 of 2wsxA
- binding 3-carboxy-n,n,n-trimethylpropan-1-aminium: W135 (≠ Y146), W140 (= W151), G304 (≠ D310), F305 (≠ R311), G308 (≠ N318), W309 (= W319), W316 (= W326), Y320 (≠ W330), M324 (≠ V334), Q466 (= Q475)
3hfxA Crystal structure of carnitine transporter (see paper)
26% identity, 72% coverage: 15:501/677 of query aligns to 1:488/493 of 3hfxA
- binding carnitine: E74 (= E90), F75 (= F91), S90 (≠ G106), W96 (≠ F112), Y103 (≠ T119), W131 (≠ Y146), W136 (= W151), G300 (≠ D310), F301 (≠ R311), W305 (= W319), W312 (= W326), W313 (= W327), Y316 (≠ W330), Y316 (≠ W330), Q319 (≠ F333), M320 (≠ V334), F323 (= F337), I327 (= I341)
Query Sequence
>14452 FitnessBrowser__Keio:14452
MTDLSHSREKDKINPVVFYTSAGLILLFSLTTILFRDFSALWIGRTLDWVSKTFGWYYLL
AATLYIVFVVCIACSRFGSVKLGPEQSKPEFSLLSWAAMLFAAGIGIDLMFFSVAEPVTQ
YMQPPEGAGQTIEAARQAMVWTLFHYGLTGWSMYALMGMALGYFSYRYNLPLTIRSALYP
IFGKRINGPIGHSVDIAAVIGTIFGIATTLGIGVVQLNYGLSVLFDIPDSMAAKAALIAL
SVIIATISVTSGVDKGIRVLSELNVALALGLILFVLFMGDTSFLLNALVLNVGDYVNRFM
GMTLNSFAFDRPVEWMNNWTLFFWAWWVAWSPFVGLFLARISRGRTIRQFVLGTLIIPFT
FTLLWLSVFGNSALYEIIHGGAAFAEEAMVHPERGFYSLLAQYPAFTFSASVATITGLLF
YVTSADSGALVLGNFTSQLKDINSDAPGWLRVFWSVAIGLLTLGMLMTNGISALQNTTVI
MGLPFSFVIFFVMAGLYKSLKVEDYRRESANRDTAPRPLGLQDRLSWKKRLSRLMNYPGT
RYTKQMMETVCYPAMEEVAQELRLRGAYVELKSLPPEEGQQLGHLDLLVHMGEEQNFVYQ
IWPQQYSVPGFTYRARSGKSTYYRLETFLLEGSQGNDLMDYSKEQVITDILDQYERHLNF
IHLHREAPGHSVMFPDA
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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