SitesBLAST
Comparing Ac3H11_3353 FitnessBrowser__acidovorax_3H11:Ac3H11_3353 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 4 hits to proteins with known functional sites (download)
5b57A Inward-facing conformation of abc heme importer bhuuv from burkholderia cenocepacia (see paper)
37% identity, 79% coverage: 76:361/364 of query aligns to 45:328/330 of 5b57A
P15030 Fe(3+) dicitrate transport system permease protein FecC; Iron(III) dicitrate transport system permease protein FecC from Escherichia coli (strain K12) (see paper)
33% identity, 82% coverage: 63:360/364 of query aligns to 37:331/332 of P15030
- R60 (= R87) mutation to C: Retains 33% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 29% of wild-type citrate-mediated Fe(3+) transport.
- R63 (≠ Y90) mutation to C: Retains 74% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 30% of wild-type citrate-mediated Fe(3+) transport.
- R302 (≠ K331) mutation to C: Retains 24% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 28% of wild-type citrate-mediated Fe(3+) transport.
P15029 Fe(3+) dicitrate transport system permease protein FecD; Iron(III) dicitrate transport system permease protein FecD from Escherichia coli (strain K12) (see paper)
34% identity, 81% coverage: 67:361/364 of query aligns to 31:318/318 of P15029
- R51 (= R87) mutation to C: Retains 32% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 14% of wild-type citrate-mediated Fe(3+) transport.
- R54 (≠ Y90) mutation to C: Retains 19% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 24% of wild-type citrate-mediated Fe(3+) transport.
- R288 (≠ K331) mutation to C: Retains 65% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 35% of wild-type citrate-mediated Fe(3+) transport.
P06972 Iron(3+)-hydroxamate import system permease protein FhuB; Ferric hydroxamate uptake protein B; Ferrichrome transport system permease protein FhuB; Ferrichrome uptake protein FhuB; Iron(III)-hydroxamate import system permease protein FhuB from Escherichia coli (strain K12) (see paper)
33% identity, 76% coverage: 87:362/364 of query aligns to 390:660/660 of P06972
- R390 (= R87) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
- M484 (≠ I185) mutation to A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-175; A-492 and A-495.; mutation to L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-175; L-492 and L-495.
- M492 (≠ A193) mutation to A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-175; A-484 and A-495.; mutation to L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-175; L-484 and L-495.
- M495 (≠ W196) mutation to A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-175; A-484 and A-492.; mutation to L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-175; L-484 and L-492.
- Q507 (= Q209) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-510.
- T510 (≠ F212) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-507.
- S515 (= S217) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-517.
- Y517 (≠ S219) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-515.
- Q636 (≠ V338) mutation to A: Decreased binding to ferrichrome-FhuD.
Sites not aligning to the query:
- 57 S→A: Decreased binding to ferrichrome-FhuD.
- 170 D→A: Loss of binding to ferrichrome-FhuD; when associated with A-171.
- 171 Q→A: Loss of binding to ferrichrome-FhuD; when associated with A-170.
- 175 M→A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-484; A-492 and A-495.; M→L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-484; L-492 and L-495.
- 182 Interaction with FhuD; T→A: Loss of binding to ferrichrome-FhuD; when associated with A-184.
- 184 Interaction with FhuD; T→A: Loss of binding to ferrichrome-FhuD; when associated with A-182.
- 304 Interaction with FhuD; E→A: Decreased binding to ferrichrome-FhuD.
Query Sequence
>Ac3H11_3353 FitnessBrowser__acidovorax_3H11:Ac3H11_3353
VPDSATALASAATSPTPPPAGALAQRYRHFVRRRLLLLAALLAVLCASVVADIALGPSTF
AFADVLRGLFTPGALPQAQQVILWEVRLPYAVMAVLVGASLGLAGAEMQTALNNPLASPF
TLGVSAAAAVGASAAVVSGFTLLAWGENLAVPLCAFVGAACATALIQLLAWRQGATVDTV
VLFGIALLLSFEALLWLLQFIADSNALQQIVFWTMGSLSRATWTKIGIVGTVLSLCLLWS
ARQAWALTALRAGEDQARSFGIAVERLRLVTLLRVSLLAATALSFVGTIGFVGLVGPHIA
RMLLGEDHRYYLPGSALAGALMLSLASILSKALVPGVVLPIGIITALVGVPLFMTLVLRQ
RRVA
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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