SitesBLAST
Comparing WP_057508987.1 NCBI__GCF_001431535.1:WP_057508987.1 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 20 (the maximum) hits to proteins with known functional sites (download)
1ltvA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure with bound oxidized fe(iii) (see paper)
68% identity, 87% coverage: 27:283/297 of query aligns to 21:275/275 of 1ltvA
3tcyA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum (cpah) bound to phenylalanine in a site distal to the active site (see paper)
68% identity, 87% coverage: 27:283/297 of query aligns to 23:277/277 of 3tcyA
- active site: H132 (= H136), H137 (= H141), E178 (= E184), S197 (= S203)
- binding cobalt (ii) ion: H132 (= H136), H137 (= H141), E178 (= E184)
- binding phenylalanine: A152 (= A156), Y153 (= Y157), K159 (= K163), L169 (= L175), T248 (= T254), P250 (= P256), D251 (= D257), F252 (= F258)
4etlA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum f258a mutation (see paper)
67% identity, 87% coverage: 27:283/297 of query aligns to 23:277/277 of 4etlA
1ltzA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure has bound iron (iii) and oxidized cofactor 7, 8-dihydrobiopterin (see paper)
67% identity, 87% coverage: 27:283/297 of query aligns to 23:274/274 of 1ltzA
2v27B Structure of the cold active phenylalanine hydroxylase from colwellia psychrerythraea 34h (see paper)
39% identity, 75% coverage: 28:250/297 of query aligns to 11:230/272 of 2v27B
5jk8A Phenylalanine hydroxylase from dictyostelium - bh2, norleucine complex
38% identity, 75% coverage: 28:249/297 of query aligns to 138:359/390 of 5jk8A
- active site: H250 (= H136), H255 (= H141), E295 (= E184), S314 (= S203)
- binding fe (iii) ion: H250 (= H136), H255 (= H141), E295 (= E184)
- binding 7,8-dihydrobiopterin: L214 (= L100), A216 (≠ E102), F219 (= F105), S287 (≠ T176), Y290 (= Y179)
- binding norleucine: Y242 (= Y128), T243 (≠ I129), H250 (= H136), S314 (= S203), S315 (= S204)
- binding piperazine-n,n'-bis(2-ethanesulfonic acid): T203 (= T89), R226 (= R112), D266 (= D152)
Sites not aligning to the query:
5jk5A Phenylalanine hydroxylase from dictyostelium - bh2 complex
38% identity, 75% coverage: 28:249/297 of query aligns to 147:368/400 of 5jk5A
- active site: H259 (= H136), H264 (= H141), E304 (= E184), S323 (= S203)
- binding fe (iii) ion: H259 (= H136), H264 (= H141), E304 (= E184)
- binding 7,8-dihydrobiopterin: G221 (= G98), L222 (= L99), L223 (= L100), F228 (= F105), L229 (≠ F106), S296 (≠ T176), Y299 (= Y179)
- binding piperazine-n,n'-bis(2-ethanesulfonic acid): T212 (= T89), P271 (= P148), D275 (= D152)
Sites not aligning to the query:
P00439 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Homo sapiens (Human) (see 43 papers)
37% identity, 73% coverage: 30:247/297 of query aligns to 175:392/452 of P00439
- R176 (≠ W31) to L: in non-PKU HPA and PKU; dbSNP:rs74486803
- V177 (≠ D32) to L: in PKU; haplotype 6; dbSNP:rs199475602
- E178 (≠ S33) to G: in non-PKU HPA; dbSNP:rs77958223
- V190 (≠ L45) to A: in PKU; haplotype 3; dbSNP:rs62514919
- H201 (≠ R56) to Y: in non-PKU HPA; haplotype 1; dbSNP:rs62517205
- Y204 (≠ Q59) to C: in PKU; mild; haplotypes 3,4; dbSNP:rs62514927
- N207 (vs. gap) to S: in PKU; severe; haplotype 4; dbSNP:rs62508721
- P211 (≠ L62) to T: in PKU; haplotype 4; dbSNP:rs62514931
- L213 (≠ A64) to P: in PKU; severe; dbSNP:rs62516109
- G218 (= G69) to V: in PKU; haplotypes 1,2; dbSNP:rs62514933
- E221 (≠ A72) to G: in PKU; haplotype 4; dbSNP:rs62514934
- D222 (= D73) to V: in PKU; haplotypes 3,4; dbSNP:rs62507319
- I224 (= I75) to M: in PKU; haplotype 4; dbSNP:rs199475576
- P225 (= P76) to T: in PKU; haplotype 1; dbSNP:rs199475589
- V230 (≠ L81) to I: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62516152
- F233 (≠ A84) to L: in PKU; haplotypes 2,3; dbSNP:rs62517208
- T238 (= T89) to P: in PKU; haplotype 4; dbSNP:rs199475577
- R241 (≠ T92) to C: in non-PKU HPA and PKU; haplotype 34; dbSNP:rs76687508; to H: in PKU; haplotypes 1,5; dbSNP:rs62508730
- R243 (≠ V94) to Q: in non-PKU HPA and PKU; haplotypes 4,7,9; dbSNP:rs62508588
- P244 (≠ G95) to L: in PKU; haplotype 12; dbSNP:rs118203923
- V245 (= V96) to A: in PKU, HPA and non-PKU HPA; haplotypes 3,7; dbSNP:rs796052017; to E: in PKU; haplotype 11; dbSNP:rs76212747
- G247 (= G98) to V: in PKU; haplotype 4; dbSNP:rs199475579
- L249 (= L100) to F: in PKU; haplotype 1; dbSNP:rs74503222
- R252 (≠ L103) to G: in PKU; haplotype 7; dbSNP:rs5030847; to Q: in PKU; haplotype 1; dbSNP:rs62644503; to W: in PKU; haplotypes 1,6,7,8,42, 69; complete loss of activity; dbSNP:rs5030847
- L255 (≠ F106) to S: in PKU; haplotype 36; dbSNP:rs62642930; to V: in PKU; haplotypes 18,21; dbSNP:rs62642931
- A259 (= A110) to T: in PKU; haplotype 3; dbSNP:rs62642932; to V: in PKU; haplotypes 7,42; dbSNP:rs118203921
- R261 (= R112) to Q: in HPA and PKU; mild; haplotypes 1,2,4,22, 24,28; dbSNP:rs5030849
- I269 (= I120) to L: in non-PKU HPA; dbSNP:rs62508692
- R270 (= R121) to S: in PKU; haplotype 1; dbSNP:rs62514951
- S273 (≠ D124) to F: in PKU; haplotype 7; dbSNP:rs62514953
- P275 (≠ I126) to L: in PKU; reduced activity; increased affinity for the substrate; mildly reduced substrate activation; decreased cofactor affinity; dbSNP:rs62508715
- M276 (≠ D127) to V: in PKU; haplotype 4; dbSNP:rs62516149
- Y277 (= Y128) to D: in PKU; haplotype 2; dbSNP:rs78655458
- E280 (= E131) to K: in PKU; haplotypes 1,2,4,16,38; partial residual activity; dbSNP:rs62508698
- P281 (= P132) to L: in PKU; haplotypes 1,4; dbSNP:rs5030851
- D282 (= D133) to N: in PKU; haplotype 1; dbSNP:rs199475582
- I283 (≠ M134) to F: in PKU; haplotype 21; dbSNP:rs62517168; to N: in PKU; severe; dbSNP:rs62508693; mutation to C: Loss of positive cooperativity and reduction of fold-activation by L-Phe preincubation.
- R297 (≠ P148) to C: in PKU; haplotype 4; dbSNP:rs62642945
- F299 (= F150) to C: in PKU; haplotype 8; dbSNP:rs62642933
- A300 (= A151) to 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
- S303 (≠ M154) to P: in PKU; haplotype 5; dbSNP:rs199475608
- I306 (≠ Y157) to V: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642934
- A309 (≠ G160) to D: in PKU; haplotype 7; dbSNP:rs62642935
- S310 (≠ G161) to F: in PKU; haplotype 7; dbSNP:rs62642913; to Y: in HPA; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs62642913
- L311 (≠ V162) to P: in PKU; haplotypes 1,7,10; dbSNP:rs62642936
- P314 (= P169) to 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
- I318 (≠ L172) to T: in PKU; partial loss of activity; dbSNP:rs62642918
- A322 (≠ T176) to G: in PKU; haplotype 12; dbSNP:rs62514958; to T: in PKU; haplotype 1; dbSNP:rs62514957
- F331 (= F185) to L: in PKU; haplotype 1; dbSNP:rs62517179
- D338 (= D192) to Y: in PKU; haplotype 4; dbSNP:rs62516150
- A342 (≠ I196) to T: in PKU; haplotype 5; dbSNP:rs62507282
- A345 (= A199) to T: in PKU; haplotype 7; dbSNP:rs62516062
- L348 (≠ V202) to V: in PKU; mild haplotype 9; dbSNP:rs62516092
- S349 (= S203) to L: in PKU; severe; dbSNP:rs62507279; to P: in PKU; haplotypes 1,4; dbSNP:rs62508646
- S350 (= S204) to T: in PKU; haplotype 2; dbSNP:rs62517183
- L364 (≠ R219) natural variant: Missing (in PKU; haplotype 5; dbSNP:rs62516096)
- Y377 (= Y232) to C: in PKU; haplotype 4; dbSNP:rs62642942
- T380 (≠ D235) to M: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642937
- Y387 (≠ F242) to H: in PKU; haplotype 1; dbSNP:rs62517194
- V388 (= V243) to M: in PKU; haplotypes 1,4; dbSNP:rs62516101
- E390 (≠ D245) to G: in PKU and non-PKU HPA; haplotype 4; dbSNP:rs5030856
Sites not aligning to the query:
- 16 modified: Phosphoserine; by PKA; S → P: in PKU; uncertain significance; dbSNP:rs62642946
- 39 F → L: in HPA and PKU; haplotype 1; dbSNP:rs62642926; natural variant: Missing (in PKU; haplotypes 9,21)
- 41 L → P: in PKU; mild; dbSNP:rs62642916
- 42 K → I: in PKU; haplotype 21; dbSNP:rs62635346
- 46 G → S: in PKU; haplotype 5; significantly reduces phenylalanine binding; dbSNP:rs74603784
- 47 A → V: in non-PKU HPA; haplotype 4; significantly reduces phenylalanine binding; dbSNP:rs118203925
- 48 L → S: in PKU; mild; haplotypes 3,4; dbSNP:rs5030841
- 55 F → L: in HPA and PKU; does not affect oligomerization; results in loss of substrate activation; dbSNP:rs199475598
- 56 E → D: in PKU; haplotype 10; dbSNP:rs199475567
- 63:64 natural variant: TH -> PN (in PKU; haplotype 1; abolishes phenylalanine binding)
- 65 I → S: in PKU; results in disturbed oligomerization; results in loss of substrate activation; dbSNP:rs75193786; I → T: in PKU; haplotypes 1,5,9,21,B; abolishes phenylalanine binding; dbSNP:rs75193786; I → V: in HPA and PKU; dbSNP:rs199475643
- 67 S → P: in PKU; haplotype 4; dbSNP:rs5030842
- 68 R → S: in PKU; haplotype 1; dbSNP:rs76394784
- 76 E → G: in non-PKU HPA; dbSNP:rs62507347
- 84 D → Y: in PKU; haplotype 4; dbSNP:rs62514902
- 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
- 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
6pahA Human phenylalanine hydroxylase catalytic domain dimer with bound l- dopa (3,4-dihydroxyphenylalanine) inhibitor (see paper)
37% identity, 73% coverage: 30:247/297 of query aligns to 59:276/308 of 6pahA
5pahA Human phenylalanine hydroxylase catalytic domain dimer with bound dopamine inhibitor (see paper)
37% identity, 73% coverage: 30:247/297 of query aligns to 59:276/308 of 5pahA
4pahA Human phenylalanine hydroxylase catalytic domain dimer with bound nor- adrenaline inhibitor (see paper)
37% identity, 73% coverage: 30:247/297 of query aligns to 59:276/308 of 4pahA
3pahA Human phenylalanine hydroxylase catalytic domain dimer with bound adrenaline inhibitor (see paper)
37% identity, 73% coverage: 30:247/297 of query aligns to 59:276/308 of 3pahA
1mmtA Crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase (fe(ii)) complexed with tetrahydrobiopterin and norleucine (see paper)
37% identity, 73% coverage: 30:247/297 of query aligns to 59:276/308 of 1mmtA
- active site: H169 (= H136), H174 (= H141), E214 (= E184), S233 (= S203)
- binding fe (ii) ion: H169 (= H136), H174 (= H141), E214 (= E184)
- binding 5,6,7,8-tetrahydrobiopterin: G131 (= G98), L132 (= L99), L133 (= L100), S135 (≠ E102), F138 (= F105), L139 (≠ F106), H148 (≠ P115), E170 (≠ D137), Y209 (= Y179), E214 (= E184)
- binding norleucine: R154 (= R121), Y161 (= Y128), T162 (≠ I129), H169 (= H136), S233 (= S203), S234 (= S204)
1kw0A Catalytic domain of human phenylalanine hydroxylase (fe(ii)) in complex with tetrahydrobiopterin and thienylalanine (see paper)
37% identity, 73% coverage: 30:247/297 of query aligns to 58:275/307 of 1kw0A
- active site: H168 (= H136), H173 (= H141), E213 (= E184), S232 (= S203)
- binding fe (ii) ion: H168 (= H136), H173 (= H141), E213 (= E184)
- binding 5,6,7,8-tetrahydrobiopterin: L131 (= L99), L132 (= L100), S134 (≠ E102), F137 (= F105), H147 (≠ P115), E169 (≠ D137), E213 (= E184)
- binding beta(2-thienyl)alanine: R153 (= R121), Y160 (= Y128), T161 (≠ I129), E163 (= E131), P164 (= P132), H168 (= H136), F214 (= F185), S232 (= S203), S233 (= S204)
1j8uA Catalytic domain of human phenylalanine hydroxylase fe(ii) in complex with tetrahydrobiopterin (see paper)
37% identity, 73% coverage: 30:247/297 of query aligns to 58:275/307 of 1j8uA
- active site: H168 (= H136), H173 (= H141), E213 (= E184), S232 (= S203)
- binding fe (ii) ion: H168 (= H136), H173 (= H141), E213 (= E184)
- binding 5,6,7,8-tetrahydrobiopterin: L132 (= L100), S134 (≠ E102), F137 (= F105), L138 (≠ F106), A205 (≠ T176)
1j8tA Catalytic domain of human phenylalanine hydroxylase fe(ii) (see paper)
37% identity, 73% coverage: 30:247/297 of query aligns to 58:275/307 of 1j8tA
1dmwA Crystal structure of double truncated human phenylalanine hydroxylase with bound 7,8-dihydro-l-biopterin (see paper)
37% identity, 73% coverage: 30:247/297 of query aligns to 58:275/307 of 1dmwA
- active site: H168 (= H136), H173 (= H141), E213 (= E184), S232 (= S203)
- binding fe (iii) ion: H168 (= H136), H173 (= H141), E213 (= E184)
- binding 7,8-dihydrobiopterin: G130 (= G98), L132 (= L100), S134 (≠ E102), F137 (= F105), A205 (≠ T176), Y208 (= Y179)
4anpA Crystal structure of human phenylalanine hydroxylase in complex with a pharmacological chaperone (see paper)
37% identity, 73% coverage: 30:247/297 of query aligns to 59:276/309 of 4anpA
- active site: H169 (= H136), H174 (= H141), E214 (= E184), S233 (= S203)
- binding 5,6-dimethyl-3-(4-methyl-2-pyridinyl)-2-thioxo-2,3-dihydrothieno[2,3- d]pyrimidin-4(1h)-one: F138 (= F105), P163 (≠ A130), P165 (= P132), H169 (= H136), W210 (= W180), E214 (= E184)
- binding fe (iii) ion: H169 (= H136), H174 (= H141), E214 (= E184)
P16331 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Mus musculus (Mouse) (see paper)
36% identity, 73% coverage: 30:247/297 of query aligns to 175:392/453 of P16331
- F263 (= F114) mutation to S: Mutant mice have features of phenylketonuria.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 106 V→A: Mutant mice have mild features of phenylketonuria.
P04176 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Rattus norvegicus (Rat) (see 2 papers)
36% identity, 73% coverage: 30:247/297 of query aligns to 175:392/453 of P04176
- H285 (= H136) binding
- H290 (= H141) binding
- E330 (= E184) binding
Sites not aligning to the query:
- 16 modified: Phosphoserine; by PKA
Query Sequence
>WP_057508987.1 NCBI__GCF_001431535.1:WP_057508987.1
MDQTTPRRVEHQQTDKGYVPVYTTAVVEQPWDSYSADDHATWSTLFKRQRDLLNGRACQE
FLDAQDAMGMSADRIPRFEQLNEALAAATGWTLVGVEGLLPELDFFDHLANRRFPVTWWI
RRPDQIDYIAEPDMFHDLFGHVPLLMNPVFADYMEAYGRGGVKAHALGPDALQNLTRLYW
YTVEFGLINTADGLRIYGAGIVSSKGESLYSLESPAPNRIGFDLERIMRTRYRIDTFQKT
YFVIDSFEQLMQATAPDFTPIYASLADQPQLPAGEVQADDRVFQRGTGAGWATGGDV
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