SitesBLAST
Comparing GFF990 FitnessBrowser__WCS417:GFF990 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)
5ti1H Crystal structure of fumarylacetoacetate hydrolase from burkholderia xenovorans lb400
51% identity, 98% coverage: 8:427/428 of query aligns to 14:428/430 of 5ti1H
- active site: D139 (= D128), H146 (= H135), E212 (= E200), E214 (= E202), D246 (= D234), R250 (= R238), Q253 (= Q241), K266 (= K254), T270 (= T258), E377 (= E375)
- binding magnesium ion: D139 (= D128), E212 (= E200), E214 (= E202), D246 (= D234)
P16930 Fumarylacetoacetase; FAA; Beta-diketonase; Fumarylacetoacetate hydrolase; EC 3.7.1.2 from Homo sapiens (Human) (see 14 papers)
47% identity, 96% coverage: 18:427/428 of query aligns to 10:415/419 of P16930
- N16 (= N24) to I: in TYRSN1; loss of activity; dbSNP:rs121965073
- A35 (= A42) to T: in TYRSN1; atypical mild phenotype
- F62 (≠ T68) to C: in TYRSN1; loss of activity
- A134 (= A136) to D: in TYRSN1; loss of activity; dbSNP:rs121965074
- C193 (= C194) to R: in TYRSN1; loss of activity
- D233 (= D234) to V: in TYRSN1; loss of activity; dbSNP:rs80338897
- W234 (= W235) to G: in TYRSN1; loss of activity; dbSNP:rs1555441595
- Q279 (≠ R280) 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 (≠ Q352) to W: does not cause a clinically relevant phenotype; results in lower enzyme activity; dbSNP:rs11555096
- P342 (≠ A353) to L: in TYRSN1; loss of activity; dbSNP:rs779040832
- R381 (= R392) to G: in TYRSN1; loss of activity; dbSNP:rs121965077
- F405 (= F417) 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)
46% identity, 96% coverage: 18:427/428 of query aligns to 10:415/419 of P35505
- D126 (= D128) binding Ca(2+)
- E199 (= E200) binding Ca(2+)
- E201 (= E202) binding Ca(2+); mutation to G: Decrease in activity.
- D233 (= D234) binding Ca(2+); binding Mg(2+)
- K253 (= K254) binding Mg(2+)
- T257 (= T258) binding Mg(2+)
1hyoB Crystal structure of fumarylacetoacetate hydrolase complexed with 4- (hydroxymethylphosphinoyl)-3-oxo-butanoic acid (see paper)
46% identity, 96% coverage: 18:427/428 of query aligns to 12:417/419 of 1hyoB
- active site: D128 (= D128), H135 (= H135), E201 (= E200), E203 (= E202), D235 (= D234), R239 (= R238), Q242 (= Q241), K255 (= K254), T259 (= T258), E366 (= E375)
- binding acetate ion: Y130 (= Y130), V139 (= V139), R144 (= R144)
- binding calcium ion: D128 (= D128), E201 (= E200), E203 (= E202), D235 (= D234)
- binding 4-[hydroxy-[methyl-phosphinoyl]]-3-oxo-butanoic acid: D128 (= D128), F129 (= F129), Y130 (= Y130), H135 (= H135), Y161 (= Y160), K255 (= K254), G351 (= G360), T352 (= T361)
- binding magnesium ion: D235 (= D234), W236 (= W235), K255 (= K254), G258 (≠ I257), T259 (= T258)
2hzyA Mouse fumarylacetoacetate hydrolase complexes with a transition-state mimic of the complete substrate (see paper)
46% identity, 96% coverage: 18:427/428 of query aligns to 10:415/416 of 2hzyA
- active site: D126 (= D128), H133 (= H135), E199 (= E200), E201 (= E202), D233 (= D234), R237 (= R238), Q240 (= Q241), K253 (= K254), T257 (= T258), E364 (= E375)
- binding calcium ion: G122 (≠ N124), D123 (= D125)
- binding manganese (ii) ion: D126 (= D128), E199 (= E200), E201 (= E202), D233 (= D234)
1qcoA Crystal structure of fumarylacetoacetate hydrolase complexed with fumarate and acetoacetate (see paper)
46% identity, 96% coverage: 18:427/428 of query aligns to 10:415/416 of 1qcoA
- active site: K253 (= K254)
- binding acetoacetic acid: D126 (= D128), F127 (= F129), Y128 (= Y130), H133 (= H135), Y159 (= Y160), E199 (= E200), K253 (= K254), G349 (= G360), T350 (= T361)
- binding calcium ion: D126 (= D128), E199 (= E200), E201 (= E202), D233 (= D234)
- binding fumaric acid: Y128 (= Y130), V137 (= V139), R142 (= R144), Q240 (= Q241), Y244 (= Y245)
8skyB Crystal structure of yisk from bacillus subtilis in complex with oxalate (see paper)
28% identity, 41% coverage: 194:368/428 of query aligns to 142:273/303 of 8skyB
Sites not aligning to the query:
8sutA Crystal structure of yisk from bacillus subtilis in complex with reaction product 4-hydroxy-2-oxoglutaric acid (see paper)
28% identity, 41% coverage: 194:368/428 of query aligns to 143:274/303 of 8sutA
Sites not aligning to the query:
O06724 Oxaloacetate tautomerase YisK; Oxaloacetate decarboxylase YisK; EC 5.3.2.2; EC 4.1.1.112 from Bacillus subtilis (strain 168) (see paper)
28% identity, 41% coverage: 194:368/428 of query aligns to 142:273/301 of O06724
- E148 (= E200) binding Mn(2+)
- EGE 148:150 (≠ ELE 200:202) mutation to AGA: Abolished enzyme activities.
- E150 (= E202) binding Mn(2+)
- D179 (= D234) binding Mn(2+)
- K196 (= K254) binding oxalate
- T266 (= T361) binding oxalate
Sites not aligning to the query:
- 30 E→A: Impaired subcellular localization without affecting the enzyme activity.
- 99 binding oxalate
Query Sequence
>GFF990 FitnessBrowser__WCS417:GFF990
MTQPTLTRSWVASANGHTDFPLQNLPLGVFSINGSAPRAGVAIGDSILDLQAAIDEFDGE
ARRAIEATAGGQLNAFFALGRGPRVALRERLLELLAEGSTLHTREAQVLHRAADCQMHVP
AQINDYTDFYVGIEHAQNVGKLFRPDNPLLPNYKYVPIGYHGRASTIRTSGTDVRRPKGQ
TLPAGQSEPTFGPCARLDYELELGIWIGQGNEMGDSIAIGDAADHIAGFCLLNDWSARDI
QAWEYQPLGPFLSKSFITTISPWVVTAEALEPFRKAQPARPEGDPQPLSYLLDKRDQAAG
ALDIELEVLLTTAAMREQNLPAHRLALSNSLHMYWTVAQLVAHHSVNGCQLQAGDLFGSG
TLSGPQAGQFGSLLEMTEGGKKPVELPSGEVRKFLEDGDEIILRARCNREGFASIGFGEC
RGTVIAAR
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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