SitesBLAST
Comparing AZOBR_RS23220 FitnessBrowser__azobra:AZOBR_RS23220 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)
40% identity, 71% coverage: 18:490/662 of query aligns to 67:547/595 of P54582
- W101 (= W47) 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 (= E81) mutation to A: Strongly decreased betaine transport.
- G149 (= G95) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (= M96) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (= G97) mutation to A: Nearly abolishes betaine transport.
- I152 (= I98) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (= IG 98:99) binding
- G153 (= G99) 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 (= F102) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (= W137) mutation to C: Mildly decreased betaine transport.
- W194 (= W142) mutation to L: Strongly decreased betaine transport.
- Y197 (= Y145) mutation to L: Nearly abolishes betaine transport.
- R210 (= R158) mutation to A: Nearly abolishes betaine transport.
- S253 (= S200) binding
- G301 (= G247) mutation to L: Strongly decreased betaine transport.
- N309 (= N255) mutation to A: Decreases affinity for sodium ions.
- T351 (= T297) 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 (= W305) mutation to C: Strongly decreased betaine transport.
- W366 (= W309) mutation to C: No effect on betaine transport.
- F369 (= F312) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
- W371 (= W314) mutation to L: No effect on betaine transport.
- W373 (= W316) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
- WWISW 373:377 (= WWISW 316:320) binding
- W374 (= W317) 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 (= W320) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (= F323) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- F384 (= F327) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- R387 (= R330) mutation to A: Mildly decreased betaine transport.
- R392 (= R335) mutation to K: Moderately decreased betaine transport.
3p03C Crystal structure of betp-g153d with choline bound (see paper)
40% identity, 71% coverage: 18:490/662 of query aligns to 11:487/508 of 3p03C
4llhA Substrate bound outward-open state of the symporter betp (see paper)
41% identity, 71% coverage: 18:490/662 of query aligns to 11:488/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (= M96), G95 (= G97), D97 (≠ G99), W314 (= W316), W315 (= W317), W318 (= W320)
- binding sodium ion: A91 (≠ S93), M94 (= M96), G95 (= G97), F405 (= F410), T408 (= T413), S409 (= S414)
Sites not aligning to the query:
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
27% identity, 69% coverage: 34:492/662 of query aligns to 40:503/504 of P31553
- Y114 (≠ L110) binding ; mutation to L: Small decrease in transport activity.
- W142 (= W137) binding
- D288 (≠ E281) 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 (≠ W288) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (≠ Y292) 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 (= T297) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- GW 315:316 (≠ SW 308:309) binding
- W316 (= W309) mutation to L: Decrease in transport activity.
- W323 (= W316) binding ; mutation to L: Abolishes transport activity.
- WW 323:324 (= WW 316:317) binding
- W324 (= W317) mutation to L: Abolishes transport activity.
- Y327 (≠ W320) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ WAPF 320:323) binding
- Q330 (≠ F323) mutation to L: Decrease in transport activity.
- M331 (≠ V324) binding
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
27% identity, 70% coverage: 31:492/662 of query aligns to 42:508/508 of 2wswA
3hfxA Crystal structure of carnitine transporter (see paper)
27% identity, 69% coverage: 34:492/662 of query aligns to 29:492/493 of 3hfxA
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
27% identity, 69% coverage: 34:492/662 of query aligns to 33:496/496 of 2wsxA
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
27% identity, 70% coverage: 31:492/662 of query aligns to 29:495/495 of 4m8jA
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
27% identity, 70% coverage: 31:492/662 of query aligns to 37:503/514 of B4EY22
- E111 (= E107) mutation to A: Abolishes transport activity.
- R262 (≠ N255) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W309) mutation to A: 2.5-fold decrease in Vmax.
- M331 (≠ V324) mutation to V: 10-fold decrease in Vmax.
Query Sequence
>AZOBR_RS23220 FitnessBrowser__azobra:AZOBR_RS23220
MHGINKTVSFTAGGLIVLFVLLASVFTEPFGERISALQSAIVGNFGWFYILSVAGFLLFA
FWLFFSPYGSIKLGKDDDEPEFSYLTWFAMLFSAGMGIGLLFYGVAEPVLHLANPRVGEA
GTPDAAREAMNLAFLHWGLHAWGIYITVGLSLGYFAYRHDLPLTIRSALYPLLGDRLSGW
PGHLVDIVAIVGTLFGIATSLGLGVMQINAGLDYLGLVSVGTVQQMVLIAVITAIATASA
VSGVGRGIRRLSELNMLAGLLLLLFVFLLGPSVFLLSTLVESIGRYLWTLPYTSFRTLPY
TGAEWQASWTMFYWGWWISWAPFVGMFIARVSRGRTIREFIGGVLFAPVALTFVWFTVFG
ETAIHMEMFEGGGMAAAVQENVPTALFVMLDRLPLSVITSALATLIVVTFFVTSADSGAL
VIDIIGSGGNQDPPIATRIFWAVLCGVVAAVLLLVGGLQALQTAAVTTALPFAVVMVLMC
VGLVTSLRAERRAGPDRRVARVPTASEGGAPVQPVGDGDWRQQLAAVIGRKAAIAAAVPP
GGAGARREVARFIADTVEPAFRDIAAELERLGRRAVIEVGPFNAGLAVLRDGEEEFSYDI
RARAYHPLTFAFPDLKAADEQWQMRVEVILRGGLHKQLLPALAGREAIVRDFVQEYGKWR
GW
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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