SitesBLAST
Comparing H281DRAFT_04742 FitnessBrowser__Burk376:H281DRAFT_04742 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 6 hits to proteins with known functional sites (download)
5ti1H Crystal structure of fumarylacetoacetate hydrolase from burkholderia xenovorans lb400
88% identity, 99% coverage: 3:431/433 of query aligns to 1:428/430 of 5ti1H
- active site: D139 (= D142), H146 (= H149), E212 (= E215), E214 (= E217), D246 (= D249), R250 (= R253), Q253 (= Q256), K266 (= K269), T270 (= T273), E377 (= E380)
- binding magnesium ion: D139 (= D142), E212 (= E215), E214 (= E217), D246 (= D249)
P16930 Fumarylacetoacetase; FAA; Beta-diketonase; Fumarylacetoacetate hydrolase; EC 3.7.1.2 from Homo sapiens (Human) (see 14 papers)
59% identity, 94% coverage: 27:431/433 of query aligns to 10:415/419 of P16930
- N16 (= N33) to I: in TYRSN1; loss of activity; dbSNP:rs121965073
- A35 (= A52) to T: in TYRSN1; atypical mild phenotype
- F62 (= F78) to C: in TYRSN1; loss of activity
- A134 (= A150) to D: in TYRSN1; loss of activity; dbSNP:rs121965074
- C193 (= C209) to R: in TYRSN1; loss of activity
- D233 (= D249) to V: in TYRSN1; loss of activity; dbSNP:rs80338897
- W234 (= W250) to G: in TYRSN1; loss of activity; dbSNP:rs1555441595
- Q279 (= Q295) to R: in TYRSN1; may affect splicing resulting in skipping of exon 8 alone or together with exon 9; lower activity as compared to wild type; dbSNP:rs121965078
- R341 (= R357) to W: does not cause a clinically relevant phenotype; results in lower enzyme activity; dbSNP:rs11555096
- P342 (≠ V358) to L: in TYRSN1; loss of activity; dbSNP:rs779040832
- R381 (= R397) to G: in TYRSN1; loss of activity; dbSNP:rs121965077
- F405 (= F421) to H: in TYRSN1; requires 2 nucleotide substitutions
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
P35505 Fumarylacetoacetase; FAA; Beta-diketonase; Fumarylacetoacetate hydrolase; EC 3.7.1.2 from Mus musculus (Mouse) (see 3 papers)
58% identity, 94% coverage: 27:431/433 of query aligns to 10:415/419 of P35505
- D126 (= D142) binding
- E199 (= E215) binding
- E201 (= E217) binding ; mutation to G: Decrease in activity.
- D233 (= D249) binding ; binding
- K253 (= K269) binding
- T257 (= T273) binding
2hzyA Mouse fumarylacetoacetate hydrolase complexes with a transition-state mimic of the complete substrate (see paper)
58% identity, 94% coverage: 27:431/433 of query aligns to 10:415/416 of 2hzyA
- active site: D126 (= D142), H133 (= H149), E199 (= E215), E201 (= E217), D233 (= D249), R237 (= R253), Q240 (= Q256), K253 (= K269), T257 (= T273), E364 (= E380)
- binding calcium ion: G122 (≠ P138), D123 (≠ G139)
- binding manganese (ii) ion: D126 (= D142), E199 (= E215), E201 (= E217), D233 (= D249)
1qcoA Crystal structure of fumarylacetoacetate hydrolase complexed with fumarate and acetoacetate (see paper)
58% identity, 94% coverage: 27:431/433 of query aligns to 10:415/416 of 1qcoA
- active site: K253 (= K269)
- binding acetoacetic acid: D126 (= D142), F127 (= F143), Y128 (= Y144), H133 (= H149), Y159 (= Y175), E199 (= E215), K253 (= K269), G349 (= G365), T350 (= T366)
- binding calcium ion: D126 (= D142), E199 (= E215), E201 (= E217), D233 (= D249)
- binding fumaric acid: Y128 (= Y144), V137 (= V153), R142 (= R158), Q240 (= Q256), Y244 (= Y260)
1hyoB Crystal structure of fumarylacetoacetate hydrolase complexed with 4- (hydroxymethylphosphinoyl)-3-oxo-butanoic acid (see paper)
58% identity, 94% coverage: 27:431/433 of query aligns to 12:417/419 of 1hyoB
- active site: D128 (= D142), H135 (= H149), E201 (= E215), E203 (= E217), D235 (= D249), R239 (= R253), Q242 (= Q256), K255 (= K269), T259 (= T273), E366 (= E380)
- binding acetate ion: Y130 (= Y144), V139 (= V153), R144 (= R158)
- binding calcium ion: D128 (= D142), E201 (= E215), E203 (= E217), D235 (= D249)
- binding 4-[hydroxy-[methyl-phosphinoyl]]-3-oxo-butanoic acid: D128 (= D142), F129 (= F143), Y130 (= Y144), H135 (= H149), Y161 (= Y175), K255 (= K269), G351 (= G365), T352 (= T366)
- binding magnesium ion: D235 (= D249), W236 (= W250), K255 (= K269), G258 (≠ T272), T259 (= T273)
Query Sequence
>H281DRAFT_04742 FitnessBrowser__Burk376:H281DRAFT_04742
MSALSDLQATLDPSRKSWVQSANEPSNDFSIQNLPFGIFSDSKDDTPRVGVAIGDEIVDL
AALEAAGLLTVPSNAGVFARDTLNEFIALGRDAWRSVRIQLSNLLSRDTATLRDDAALRA
KALVRQADARLHLPVQIPGYTDFYSSKEHATNVGSMFRNPKDALLPNWSEMPIGYNGRAS
SVVVSGTPVRRPNGQLKLPDQERPVFGACRKLDIELETGFVIGGGNALGEPIACTDAEAH
IFGMVLLNDWSARDIQQWEYVPLGPFNSKSFTTTISPWIVTLDALEPFRVAQPVQEPQPL
AYLRHDGEHAFDIALEVTLRPQGAKQATTIARTNFKYMYWTMAQQLAHHTVGGCNTRVGD
LMGSGTISGPTEDSYGSLLELTLNGKKPLELNEGGTRSFIEDGDELTLSGWCQADGYRVG
FGTCVGEILPAKA
Or try a new SitesBLAST search
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