SitesBLAST

P0A9J8 Bifunctional chorismate mutase/prephenate dehydratase; Chorismate mutase-prephenate dehydratase; P-protein; EC 5.4.99.5; EC 4.2.1.51 from Escherichia coli (strain K12)
27% identity, 99% coverage: 4:277/277 of query aligns to 103:381/386 of P0A9J8

query
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P0A9J8

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Sites not aligning to the query:

11 mutation R->A,K: Important decrease in catalytic efficiency and affinity.
28 mutation R->A,K: Important decrease in catalytic efficiency and affinity.
39 mutation K->A,Q,R: Important decrease in catalytic efficiency and affinity.
52 mutation E->A,D,Q: Important decrease in catalytic efficiency and affinity.
88 mutation Q->A,E,K: Important decrease in catalytic efficiency and affinity.

7am0B Gqqa- a novel type of quorum quenching acylases (see paper)
27% identity, 97% coverage: 7:274/277 of query aligns to 4:272/278 of 7am0B

query
sites
7am0B

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binding phenylalanine: N199 (≠ G202), N200 (≠ H203), Q201 (≠ K204), P202 (≠ A205), L205 (= L208), N218 (≠ S221), M219 (≠ L222), T220 (= T223), R221 (≠ K224), T234 (≠ Y237), F236 (= F239)

3mwbB The crystal structure of prephenate dehydratase in complex with l-phe from arthrobacter aurescens to 2.0a
27% identity, 96% coverage: 11:276/277 of query aligns to 7:276/303 of 3mwbB

query
sites
3mwbB

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active site: T176 (= T176), F178 (= F178)
binding magnesium ion: A155 (= A155), Q158 (≠ L158), L161 (= L161)
binding phenylalanine: D205 (vs. gap), H206 (≠ K204), L210 (= L208), N223 (≠ S221), L224 (= L222), S225 (≠ T223), R226 (≠ K224), I227 (= I225), Y236 (= Y237), F238 (= F239)

3mwbA The crystal structure of prephenate dehydratase in complex with l-phe from arthrobacter aurescens to 2.0a
26% identity, 96% coverage: 11:276/277 of query aligns to 7:279/306 of 3mwbA

query
sites
3mwbA

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active site: T176 (= T176), F178 (= F178)
binding phenylalanine: D205 (vs. gap), H206 (≠ K204), L210 (= L208), N223 (≠ S221), L224 (= L222), S225 (≠ T223), R226 (≠ K224), S229 (= S227), F241 (= F239)

3luyA Putative chorismate mutase from bifidobacterium adolescentis
20% identity, 96% coverage: 11:275/277 of query aligns to 10:287/326 of 3luyA

query
sites
3luyA

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active site: T177 (= T176)
binding 3-phenylpyruvic acid: G215 (≠ K204), L219 (= L208), Y248 (= Y237), F250 (= F239)

5fiiB Structure of a human aspartate kinase, chorismate mutase and tyra domain. (see paper)
42% identity, 19% coverage: 196:247/277 of query aligns to 3:54/78 of 5fiiB

query
sites
5fiiB

S

S

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L

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F

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x
E

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S

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binding phenylalanine: E10 (≠ H203), E11 (≠ K204), L15 (= L208), N28 (≠ S221), L29 (= L222), H31 (≠ K224), I32 (= I225), S34 (= S227), Y44 (= Y237), F46 (= F239)

P00439 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Homo sapiens (Human) (see 43 papers)
43% identity, 18% coverage: 196:244/277 of query aligns to 36:84/452 of P00439

query
sites
P00439

S

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F39 (= F199) to L: in HPA and PKU; haplotype 1; dbSNP:rs62642926; natural variant: Missing (in PKU; haplotypes 9,21)
L41 (≠ V201) to P: in PKU; mild; dbSNP:rs62642916
K42 (≠ G202) to I: in PKU; haplotype 21; dbSNP:rs62635346
G46 (= G206) to S: in PKU; haplotype 5; significantly reduces phenylalanine binding; dbSNP:rs74603784
A47 (≠ S207) to V: in non-PKU HPA; haplotype 4; significantly reduces phenylalanine binding; dbSNP:rs118203925
L48 (= L208) to S: in PKU; mild; haplotypes 3,4; dbSNP:rs5030841
F55 (= F215) to L: in HPA and PKU; does not affect oligomerization; results in loss of substrate activation; dbSNP:rs199475598
E56 (≠ A216) to D: in PKU; haplotype 10; dbSNP:rs199475567
TH 63:64 (≠ TK 223:224) natural variant: TH -> PN (in PKU; haplotype 1; abolishes phenylalanine binding)
I65 (= I225) to S: in PKU; results in disturbed oligomerization; results in loss of substrate activation; dbSNP:rs75193786; to T: in PKU; haplotypes 1,5,9,21,B; abolishes phenylalanine binding; dbSNP:rs75193786; to V: in HPA and PKU; dbSNP:rs199475643
S67 (= S227) to P: in PKU; haplotype 4; dbSNP:rs5030842
R68 (≠ M228) to S: in PKU; haplotype 1; dbSNP:rs76394784
E76 (= E236) to G: in non-PKU HPA; dbSNP:rs62507347
D84 (≠ E244) to Y: in PKU; haplotype 4; dbSNP:rs62514902

Sites not aligning to the query:

16 modified: Phosphoserine; by PKA; S → P: in PKU; uncertain significance; dbSNP:rs62642946
87 S → R: in non-PKU HPA; haplotype 1; dbSNP:rs62516151
94 natural variant: Missing (in PKU; mild; haplotype 2)
98 L → S: in non-PKU HPA; dbSNP:rs62517167
104 A → D: in PKU; mild; haplotype 1; dbSNP:rs62642929
124 T → I: in PKU; haplotype 28; dbSNP:rs199475571
143 D → G: in PKU; haplotype 11; dbSNP:rs199475572
148 G → S: in PKU; haplotypes 1,2,7; dbSNP:rs80297647
151 D → H: in PKU; haplotypes 1,8; dbSNP:rs199475597
157 R → N: in PKU; severe; 5% activity; requires 2 nucleotide substitutions; dbSNP:rs1565853495
158 R → Q: in PKU; haplotypes 1,2,4,7,16, 28; dbSNP:rs5030843
161 F → S: in PKU; haplotype 4; dbSNP:rs79635844
164 I → T: in PKU; haplotype 1; dbSNP:rs199475595
170 H → Q: in PKU; does not affect oligomerization; dbSNP:rs199475652
171 G → A: in PKU; haplotype 1; dbSNP:rs199475596
173 P → T: in PKU; haplotype 4; dbSNP:rs199475574
174 I → T: in PKU; haplotype 1; dbSNP:rs138809906
176 R → L: in non-PKU HPA and PKU; dbSNP:rs74486803
177 V → L: in PKU; haplotype 6; dbSNP:rs199475602
178 E → G: in non-PKU HPA; dbSNP:rs77958223
190 V → A: in PKU; haplotype 3; dbSNP:rs62514919
201 H → Y: in non-PKU HPA; haplotype 1; dbSNP:rs62517205
204 Y → C: in PKU; mild; haplotypes 3,4; dbSNP:rs62514927
207 N → S: in PKU; severe; haplotype 4; dbSNP:rs62508721
211 P → T: in PKU; haplotype 4; dbSNP:rs62514931
213 L → P: in PKU; severe; dbSNP:rs62516109
218 G → V: in PKU; haplotypes 1,2; dbSNP:rs62514933
221 E → G: in PKU; haplotype 4; dbSNP:rs62514934
222 D → V: in PKU; haplotypes 3,4; dbSNP:rs62507319
224 I → M: in PKU; haplotype 4; dbSNP:rs199475576
225 P → T: in PKU; haplotype 1; dbSNP:rs199475589
230 V → I: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62516152
233 F → L: in PKU; haplotypes 2,3; dbSNP:rs62517208
238 T → P: in PKU; haplotype 4; dbSNP:rs199475577
241 R → C: in non-PKU HPA and PKU; haplotype 34; dbSNP:rs76687508; R → H: in PKU; haplotypes 1,5; dbSNP:rs62508730
243 R → Q: in non-PKU HPA and PKU; haplotypes 4,7,9; dbSNP:rs62508588
244 P → L: in PKU; haplotype 12; dbSNP:rs118203923
245 V → A: in PKU, HPA and non-PKU HPA; haplotypes 3,7; dbSNP:rs796052017; V → E: in PKU; haplotype 11; dbSNP:rs76212747
247 G → V: in PKU; haplotype 4; dbSNP:rs199475579
249 L → F: in PKU; haplotype 1; dbSNP:rs74503222
252 R → G: in PKU; haplotype 7; dbSNP:rs5030847; R → Q: in PKU; haplotype 1; dbSNP:rs62644503; R → W: in PKU; haplotypes 1,6,7,8,42, 69; complete loss of activity; dbSNP:rs5030847
255 L → S: in PKU; haplotype 36; dbSNP:rs62642930; L → V: in PKU; haplotypes 18,21; dbSNP:rs62642931
259 A → T: in PKU; haplotype 3; dbSNP:rs62642932; A → V: in PKU; haplotypes 7,42; dbSNP:rs118203921
261 R → Q: in HPA and PKU; mild; haplotypes 1,2,4,22, 24,28; dbSNP:rs5030849
269 I → L: in non-PKU HPA; dbSNP:rs62508692
270 R → S: in PKU; haplotype 1; dbSNP:rs62514951
273 S → F: in PKU; haplotype 7; dbSNP:rs62514953
275 P → L: in PKU; reduced activity; increased affinity for the substrate; mildly reduced substrate activation; decreased cofactor affinity; dbSNP:rs62508715
276 M → V: in PKU; haplotype 4; dbSNP:rs62516149
277 Y → D: in PKU; haplotype 2; dbSNP:rs78655458
280 E → K: in PKU; haplotypes 1,2,4,16,38; partial residual activity; dbSNP:rs62508698
281 P → L: in PKU; haplotypes 1,4; dbSNP:rs5030851
282 D → N: in PKU; haplotype 1; dbSNP:rs199475582
283 I → F: in PKU; haplotype 21; dbSNP:rs62517168; I → N: in PKU; severe; dbSNP:rs62508693; I→C: Loss of positive cooperativity and reduction of fold-activation by L-Phe preincubation.
297 R → C: in PKU; haplotype 4; dbSNP:rs62642945
299 F → C: in PKU; haplotype 8; dbSNP:rs62642933
300 A → S: in PKU and HPA; haplotype 1; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs5030853
303 S → P: in PKU; haplotype 5; dbSNP:rs199475608
306 I → V: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642934
309 A → D: in PKU; haplotype 7; dbSNP:rs62642935
310 S → F: in PKU; haplotype 7; dbSNP:rs62642913; S → Y: in HPA; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs62642913
311 L → P: in PKU; haplotypes 1,7,10; dbSNP:rs62642936
314 P → S: in HPA; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs199475650
318 I → T: in PKU; partial loss of activity; dbSNP:rs62642918
322 A → G: in PKU; haplotype 12; dbSNP:rs62514958; A → T: in PKU; haplotype 1; dbSNP:rs62514957
331 F → L: in PKU; haplotype 1; dbSNP:rs62517179
338 D → Y: in PKU; haplotype 4; dbSNP:rs62516150
342 A → T: in PKU; haplotype 5; dbSNP:rs62507282
345 A → T: in PKU; haplotype 7; dbSNP:rs62516062
348 L → V: in PKU; mild haplotype 9; dbSNP:rs62516092
349 S → L: in PKU; severe; dbSNP:rs62507279; S → P: in PKU; haplotypes 1,4; dbSNP:rs62508646
350 S → T: in PKU; haplotype 2; dbSNP:rs62517183
364 natural variant: Missing (in PKU; haplotype 5; dbSNP:rs62516096)
377 Y → C: in PKU; haplotype 4; dbSNP:rs62642942
380 T → M: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642937
387 Y → H: in PKU; haplotype 1; dbSNP:rs62517194
388 V → M: in PKU; haplotypes 1,4; dbSNP:rs62516101
390 E → G: in PKU and non-PKU HPA; haplotype 4; dbSNP:rs5030856
395 A → P: in PKU; haplotype 1; dbSNP:rs62516103
403 A → V: in non-PKU HPA and PKU; haplotype 43; dbSNP:rs5030857
408 R → Q: in PKU; haplotypes 4,12; dbSNP:rs5030859; R → W: in HPA and PKU; haplotypes 1,2,4,5,13,34,41,44; most common mutation; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs5030858
410 F → S: in PKU; mild; dbSNP:rs62644475
413 R → P: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs79931499; R → S: in PKU; haplotype 1; dbSNP:rs62644467
414 Y → C: in HPA and PKU; haplotype 4; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs5030860
415 D → N: in PKU, HPA and non-PKU HPA; haplotype 1; dbSNP:rs62644499
417 Y → H: in PKU; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs62644471
418 T → P: in PKU; haplotype 4; dbSNP:rs62644501

Query Sequence

>CA265_RS11630 FitnessBrowser__Pedo557:CA265_RS11630
METTKRVAIQGIKASFHEEAAYKFFGKDIETVECNSFKETCDKLEKNDADFVVMAIENSI
AGSLLPNYTLIRDFGFSVVGEVYLPIQLHLMALPGVKFEDIKVVTSHPIAIRQCIDFFYD
YPHIKIVESNDTAACAKRIQEEQLTDTMAIANSLAAELYSLNILERRVESNKKNYTRFLI
LKKDKTDEGKKINKASICFQVGHKAGSLATVLNIFAEQDVSLTKIQSMPVLGKRNEYYFY
VDLEWPSTEKYDKAIRKALKYTSNFNILGEYQKNDKV

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