SitesBLAST
Comparing WP_013088541.1 NCBI__GCF_000092885.1:WP_013088541.1 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
86% identity, 99% coverage: 3:430/432 of query aligns to 1:428/430 of 5ti1H
- active site: D139 (= D141), H146 (= H148), E212 (= E214), E214 (= E216), D246 (= D248), R250 (= R252), Q253 (= Q255), K266 (= K268), T270 (= T272), E377 (= E379)
- binding magnesium ion: D139 (= D141), E212 (= E214), E214 (= E216), D246 (= D248)
P16930 Fumarylacetoacetase; FAA; Beta-diketonase; Fumarylacetoacetate hydrolase; EC 3.7.1.2 from Homo sapiens (Human) (see 14 papers)
59% identity, 93% coverage: 28:430/432 of query aligns to 11:415/419 of P16930
- N16 (= N33) to I: in TYRSN1; loss of activity; dbSNP:rs121965073
- A35 (= A52) to T: in TYRSN1; atypical mild phenotype
- F62 (= F77) to C: in TYRSN1; loss of activity
- A134 (= A149) to D: in TYRSN1; loss of activity; dbSNP:rs121965074
- C193 (= C208) to R: in TYRSN1; loss of activity
- D233 (= D248) to V: in TYRSN1; loss of activity; dbSNP:rs80338897
- W234 (= W249) to G: in TYRSN1; loss of activity; dbSNP:rs1555441595
- Q279 (= Q294) 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 (= R356) to W: does not cause a clinically relevant phenotype; results in lower enzyme activity; dbSNP:rs11555096
- P342 (≠ V357) to L: in TYRSN1; loss of activity; dbSNP:rs779040832
- R381 (= R396) to G: in TYRSN1; loss of activity; dbSNP:rs121965077
- F405 (= F420) 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)
59% identity, 93% coverage: 28:430/432 of query aligns to 11:415/419 of P35505
- D126 (= D141) binding Ca(2+)
- E199 (= E214) binding Ca(2+)
- E201 (= E216) binding Ca(2+); mutation to G: Decrease in activity.
- D233 (= D248) binding Ca(2+); binding Mg(2+)
- K253 (= K268) binding Mg(2+)
- T257 (= T272) binding Mg(2+)
1hyoB Crystal structure of fumarylacetoacetate hydrolase complexed with 4- (hydroxymethylphosphinoyl)-3-oxo-butanoic acid (see paper)
59% identity, 93% coverage: 28:430/432 of query aligns to 13:417/419 of 1hyoB
- active site: D128 (= D141), H135 (= H148), E201 (= E214), E203 (= E216), D235 (= D248), R239 (= R252), Q242 (= Q255), K255 (= K268), T259 (= T272), E366 (= E379)
- binding acetate ion: Y130 (= Y143), V139 (= V152), R144 (= R157)
- binding calcium ion: D128 (= D141), E201 (= E214), E203 (= E216), D235 (= D248)
- binding 4-[hydroxy-[methyl-phosphinoyl]]-3-oxo-butanoic acid: D128 (= D141), F129 (= F142), Y130 (= Y143), H135 (= H148), Y161 (= Y174), K255 (= K268), G351 (= G364), T352 (= T365)
- binding magnesium ion: D235 (= D248), W236 (= W249), K255 (= K268), G258 (≠ A271), T259 (= T272)
2hzyA Mouse fumarylacetoacetate hydrolase complexes with a transition-state mimic of the complete substrate (see paper)
59% identity, 93% coverage: 28:430/432 of query aligns to 11:415/416 of 2hzyA
- active site: D126 (= D141), H133 (= H148), E199 (= E214), E201 (= E216), D233 (= D248), R237 (= R252), Q240 (= Q255), K253 (= K268), T257 (= T272), E364 (= E379)
- binding calcium ion: G122 (≠ P137), D123 (≠ G138)
- binding manganese (ii) ion: D126 (= D141), E199 (= E214), E201 (= E216), D233 (= D248)
1qcoA Crystal structure of fumarylacetoacetate hydrolase complexed with fumarate and acetoacetate (see paper)
59% identity, 93% coverage: 28:430/432 of query aligns to 11:415/416 of 1qcoA
- active site: K253 (= K268)
- binding acetoacetic acid: D126 (= D141), F127 (= F142), Y128 (= Y143), H133 (= H148), Y159 (= Y174), E199 (= E214), K253 (= K268), G349 (= G364), T350 (= T365)
- binding calcium ion: D126 (= D141), E199 (= E214), E201 (= E216), D233 (= D248)
- binding fumaric acid: Y128 (= Y143), V137 (= V152), R142 (= R157), Q240 (= Q255), Y244 (= Y259)
Query Sequence
>WP_013088541.1 NCBI__GCF_000092885.1:WP_013088541.1
MNAVNDLQATLDASRKSWIESANEPACDFPIQNLPFGIFSDRGNDARRVGVAIGDQIVDL
AALQEANLLNAPAQNVFARDALNDFIALGRDAWRGVRIQLSQLLARDTATLRDDAALRAK
VLVRAADARLHLPVQIPGYTDFYSSKEHATNVGAMFRDPKNALLPNWSEMPIGYNGRASS
VVVSGTPVRRPNGQLKLPDQERPVFGACRKLDIELETGFIIGGGNALGEPIACEDAEAHI
FGMVLLNDWSARDIQQWEYVPLGPFNAKTFATTISPWVVTLDALEPFRVAQPVQEPEPLA
YLRHQGKHAFDIHLEVSLRAPHARQASTIARTNFKYMYWTMAQQLAHHTVAGCNTRVGDL
MGSGTISGPTEDSYGSLLELTWNGKKPLELQEGGTRTFIEDGDELTLVGWCQGDGYRVGF
GTCAGEILPARE
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