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, 97% coverage: 11:380/380 of query aligns to 10:375/386 of P0A9J8

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P0A9J8

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R11 (= R12) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
R28 (= R29) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
K39 (= K40) mutation K->A,Q,R: Important decrease in catalytic efficiency and affinity.
E52 (= E53) mutation E->A,D,Q: Important decrease in catalytic efficiency and affinity.
Q88 (= Q88) mutation Q->A,E,K: Important decrease in catalytic efficiency and affinity.

6vh5D Crystal structure of prephenate dehydratase from brucella melitensis biovar abortus 2308 in complex with phenylalanine
36% identity, 70% coverage: 116:380/380 of query aligns to 8:276/282 of 6vh5D

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6vh5D

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binding phenylalanine: N207 (≠ H311), V208 (≠ E312), L212 (= L316), N225 (= N329), M226 (≠ L330), T227 (≠ S331), K228 (≠ H332), S231 (= S335), T241 (≠ Y345), F243 (= F347)

7am0B Gqqa- a novel type of quorum quenching acylases (see paper)
31% identity, 69% coverage: 117:380/380 of query aligns to 4:269/278 of 7am0B

query
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7am0B

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binding phenylalanine: N199 (≠ L310), N200 (≠ H311), Q201 (≠ E312), P202 (≠ S313), L205 (= L316), N218 (= N329), M219 (≠ L330), T220 (≠ S331), R221 (≠ H332), T234 (≠ Y345), F236 (= F347)

3mwbA The crystal structure of prephenate dehydratase in complex with l-phe from arthrobacter aurescens to 2.0a
30% identity, 68% coverage: 121:380/380 of query aligns to 7:274/306 of 3mwbA

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3mwbA

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active site: T176 (= T285), F178 (= F287)
binding phenylalanine: D205 (≠ E312), H206 (vs. gap), L210 (= L316), N223 (= N329), L224 (= L330), S225 (= S331), R226 (≠ H332), S229 (= S335), F241 (= F347)

3mwbB The crystal structure of prephenate dehydratase in complex with l-phe from arthrobacter aurescens to 2.0a
30% identity, 68% coverage: 121:380/380 of query aligns to 7:271/303 of 3mwbB

query
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3mwbB

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active site: T176 (= T285), F178 (= F287)
binding magnesium ion: A155 (= A264), Q158 (≠ L267), L161 (= L270)
binding phenylalanine: D205 (≠ E312), H206 (vs. gap), L210 (= L316), N223 (= N329), L224 (= L330), S225 (= S331), R226 (≠ H332), I227 (= I333), Y236 (= Y345), F238 (= F347)

3luyA Putative chorismate mutase from bifidobacterium adolescentis
22% identity, 66% coverage: 116:364/380 of query aligns to 5:267/326 of 3luyA

query
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active site: T177 (= T285)
binding 3-phenylpyruvic acid: G215 (vs. gap), L219 (= L316), Y248 (= Y345), F250 (= F347)

5fiiB Structure of a human aspartate kinase, chorismate mutase and tyra domain. (see paper)
37% identity, 18% coverage: 303:372/380 of query aligns to 2:70/78 of 5fiiB

query
sites
5fiiB

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binding phenylalanine: E10 (≠ H311), E11 (= E312), L15 (= L316), N28 (= N329), L29 (= L330), H31 (= H332), I32 (= I333), S34 (= S335), Y44 (= Y345), F46 (= F347)

P00439 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Homo sapiens (Human) (see 43 papers)
36% identity, 20% coverage: 298:372/380 of query aligns to 27:103/452 of P00439

query
sites
P00439

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F39 (= F307) to L: in HPA and PKU; haplotype 1; dbSNP:rs62642926; natural variant: Missing (in PKU; haplotypes 9,21)
L41 (= L309) to P: in PKU; mild; dbSNP:rs62642916
K42 (≠ L310) to I: in PKU; haplotype 21; dbSNP:rs62635346
G46 (= G314) to S: in PKU; haplotype 5; significantly reduces phenylalanine binding; dbSNP:rs74603784
A47 (≠ T315) to V: in non-PKU HPA; haplotype 4; significantly reduces phenylalanine binding; dbSNP:rs118203925
L48 (= L316) to S: in PKU; mild; haplotypes 3,4; dbSNP:rs5030841
F55 (= F323) to L: in HPA and PKU; does not affect oligomerization; results in loss of substrate activation; dbSNP:rs199475598
E56 (≠ L324) to D: in PKU; haplotype 10; dbSNP:rs199475567
TH 63:64 (≠ SH 331:332) natural variant: TH -> PN (in PKU; haplotype 1; abolishes phenylalanine binding)
I65 (= I333) 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 (= S335) to P: in PKU; haplotype 4; dbSNP:rs5030842
R68 (≠ V336) to S: in PKU; haplotype 1; dbSNP:rs76394784
E76 (= E344) to G: in non-PKU HPA; dbSNP:rs62507347
D84 (≠ N352) to Y: in PKU; haplotype 4; dbSNP:rs62514902
S87 (≠ H356) to R: in non-PKU HPA; haplotype 1; dbSNP:rs62516151
I94 (≠ A363) natural variant: Missing (in PKU; mild; haplotype 2)
L98 (≠ V367) to S: in non-PKU HPA; dbSNP:rs62517167

Sites not aligning to the query:

16 modified: Phosphoserine; by PKA; S → P: in PKU; uncertain significance; dbSNP:rs62642946
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:rs76212747; 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

>WP_005346963.1 NCBI__GCF_000173975.1:WP_005346963.1
MDKEIRKVDDVRDDITKIDYEIAELFEKRMGFAAELALSKKQAGESIYNKNKEDEKLSDI
TKNRSNPFVIKGLEEVFIQMMSISRKYQYHMVHQRDRYIENYFTEVPELVMFPDTRIVYP
GVPGSFSEMACEKFFGADVDHYAVVNFKDVAMALNNGDADYGVLPIENSSAGDVTGVYDI
LLENDVCMVGEVFVKVEHCLLGCPGSKIEDLEVVLSHPQGLMQCAPYLENLDVKKVSVEN
TAIAAERVAREKIMTQGAIASRRAAELYGLDILDAGINFDKNNVTRFVILSKKRQYTENA
NKISISFSLLHESGTLYNILSHFLYNDLNLSHIESVPLPDQQWEYRFYIDINGNLHDPAV
KNALQGVRTEVADFKILGNY

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