SitesBLAST
Comparing WP_012757074.1 NCBI__GCF_000023185.1:WP_012757074.1 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)
2v27B Structure of the cold active phenylalanine hydroxylase from colwellia psychrerythraea 34h (see paper)
44% identity, 98% coverage: 5:263/263 of query aligns to 2:263/272 of 2v27B
3tcyA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum (cpah) bound to phenylalanine in a site distal to the active site (see paper)
39% identity, 92% coverage: 14:256/263 of query aligns to 24:264/277 of 3tcyA
- active site: H132 (= H122), H137 (= H127), E178 (= E167), S197 (= S186)
- binding cobalt (ii) ion: H132 (= H122), H137 (= H127), E178 (= E167)
- binding phenylalanine: A152 (≠ H142), Y153 (≠ F143), K159 (≠ R149), L169 (= L158), T248 (≠ V237), P250 (≠ Q239), D251 (= D240), F252 (≠ I241)
4etlA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum f258a mutation (see paper)
39% identity, 92% coverage: 14:256/263 of query aligns to 24:264/277 of 4etlA
1ltvA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure with bound oxidized fe(iii) (see paper)
39% identity, 92% coverage: 14:256/263 of query aligns to 22:262/275 of 1ltvA
1ltzA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure has bound iron (iii) and oxidized cofactor 7, 8-dihydrobiopterin (see paper)
40% identity, 84% coverage: 14:233/263 of query aligns to 24:244/274 of 1ltzA
P04177 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Rattus norvegicus (Rat) (see 7 papers)
33% identity, 81% coverage: 19:232/263 of query aligns to 224:440/498 of P04177
- Q310 (≠ P101) mutation to H: Does not affect Vmax for phenylalanine. Increases KM for phenylalanine.
- H323 (≠ Y114) mutation to Y: Does not affect Vmax for phenylalaninet. Increases KM for phenylalanine.
- H331 (= H122) binding Fe cation
- H336 (= H127) binding Fe cation
- W372 (= W163) mutation to F: Does not affect substrate specificity.
- E376 (= E167) binding Fe cation
- D425 (≠ I217) Important for substrate specificity; mutation to V: Shifts substrate specificity from tyrosine to phenylalanine.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 19 modified: Phosphoserine; by CaMK2
- 31 modified: Phosphoserine
- 40 modified: Phosphoserine; by CaMK2 and PKA
1mlwA Crystal structure of human tryptophan hydroxylase with bound 7,8- dihydro-l-biopterin cofactor and fe(iii) (see paper)
34% identity, 81% coverage: 19:232/263 of query aligns to 62:278/290 of 1mlwA
- active site: H169 (= H122), H174 (= H127), E214 (= E167), S233 (= S186)
- binding fe (iii) ion: H169 (= H122), H174 (= H127), E214 (= E167)
- binding 7,8-dihydrobiopterin: Y132 (≠ L85), L133 (≠ I86), P135 (= P88), F138 (= F91), Y209 (≠ F162)
3hf6A Crystal structure of human tryptophan hydroxylase type 1 with bound lp-521834 and fe (see paper)
34% identity, 81% coverage: 19:232/263 of query aligns to 52:268/280 of 3hf6A
- active site: H159 (= H122), H164 (= H127), E204 (= E167), S223 (= S186)
- binding fe (iii) ion: H159 (= H122), H164 (= H127), E204 (= E167)
- binding 4-(4-amino-6-{[(1R)-1-naphthalen-2-ylethyl]amino}-1,3,5-triazin-2-yl)-L-phenylalanine: G121 (≠ A84), Y122 (≠ L85), R144 (= R107), Y151 (= Y114), T152 (≠ I115), P153 (≠ E116), E154 (= E117), P155 (= P118), H159 (= H122), F200 (≠ W163), E204 (= E167), S223 (= S186), S224 (= S187)
3hfbA Crystal structure of human tryoptophan hydroxylase type 1 with lp- 534193 (see paper)
34% identity, 81% coverage: 19:232/263 of query aligns to 46:262/274 of 3hfbA
- active site: H153 (= H122), H158 (= H127), E198 (= E167), S217 (= S186)
- binding fe (iii) ion: H153 (= H122), H158 (= H127), E198 (= E167)
- binding 4-(5-{[(2'-methylbiphenyl-2-yl)methyl]amino}pyrazin-2-yl)-L-phenylalanine: P119 (= P88), R138 (= R107), Y145 (= Y114), T146 (≠ I115), P147 (≠ E116), H153 (= H122), Q187 (≠ W156), A190 (≠ F159), F194 (≠ W163), E198 (= E167), S217 (= S186), S218 (= S187), C245 (≠ Y215)
3hf8A Crystal structure of human tryoptophan hydroxylase type 1 with bound lp-533401 and fe (see paper)
34% identity, 81% coverage: 19:232/263 of query aligns to 46:262/274 of 3hf8A
- active site: H153 (= H122), H158 (= H127), E198 (= E167), S217 (= S186)
- binding fe (iii) ion: H153 (= H122), H158 (= H127), E198 (= E167)
- binding 4-{2-amino-6-[(1R)-2,2,2-trifluoro-1-(3'-fluorobiphenyl-4-yl)ethoxy]pyrimidin-4-yl}-L-phenylalanine: Y116 (≠ L85), L117 (≠ I86), S118 (≠ P87), P119 (= P88), R138 (= R107), Y145 (= Y114), T146 (≠ I115), P147 (≠ E116), E148 (= E117), P149 (= P118), H153 (= H122), F194 (≠ W163), E198 (= E167), S217 (= S186), S218 (= S187), C245 (≠ Y215), I247 (= I217)
2tohA Tyrosine hydroxylase catalytic and tetramerization domains from rat (see paper)
32% identity, 88% coverage: 1:232/263 of query aligns to 44:278/336 of 2tohA
- active site: H169 (= H122), H174 (= H127), E214 (= E167), S233 (= S186)
- binding fe (iii) ion: H169 (= H122), H174 (= H127), E214 (= E167)
- binding 7,8-dihydrobiopterin: V129 (= V82), L132 (= L85), L133 (≠ I86), Y138 (≠ F91), P165 (= P118), E170 (= E123), Y209 (≠ F162)
3e2tA The catalytic domain of chicken tryptophan hydroxylase 1 with bound tryptophan (see paper)
33% identity, 81% coverage: 19:232/263 of query aligns to 62:278/307 of 3e2tA
- active site: H169 (= H122), H174 (= H127), E214 (= E167), S233 (= S186)
- binding fe (iii) ion: H169 (= H122), H174 (= H127), E214 (= E167)
- binding imidazole: H169 (= H122), H174 (= H127), E214 (= E167)
- binding tryptophan: R154 (= R107), Y161 (= Y114), T162 (≠ I115), E164 (= E117), P165 (= P118), H169 (= H122), F215 (= F168), S233 (= S186), I263 (= I217)
P70080 Tryptophan 5-hydroxylase 1; Tryptophan 5-monooxygenase 1; EC 1.14.16.4 from Gallus gallus (Chicken) (see paper)
33% identity, 81% coverage: 19:232/263 of query aligns to 166:382/445 of P70080
- Y236 (≠ L85) binding L-tryptophan
- R258 (= R107) binding L-tryptophan
- T266 (≠ I115) binding L-tryptophan
- H273 (= H122) binding Fe cation
- H278 (= H127) binding Fe cation
- E318 (= E167) binding Fe cation
- S337 (= S186) binding L-tryptophan
- I367 (= I217) binding L-tryptophan
8cjnA Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor km-06-070 (see paper)
33% identity, 81% coverage: 19:232/263 of query aligns to 62:278/291 of 8cjnA
- binding fe (iii) ion: H169 (= H122), H174 (= H127), E214 (= E167)
- binding 3-ethyl-7-[(4-phenylphenyl)methyl]-8-(5,6,7,8-tetrahydroimidazo[1,2-a]pyridin-2-ylmethyl)purine-2,6-dione: Y132 (≠ L85), L133 (≠ I86), P135 (= P88), F138 (= F91), Y152 (≠ F105), E164 (= E117), P165 (= P118), H169 (= H122), E214 (= E167)
8cjkA Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor km-06-098 (see paper)
33% identity, 81% coverage: 19:232/263 of query aligns to 62:278/291 of 8cjkA
- binding fe (iii) ion: H169 (= H122), H174 (= H127), E214 (= E167)
- binding 3-ethyl-8-[(2-methylimidazo[2,1-b][1,3]thiazol-6-yl)methyl]-7-[[4-(1-methylpyrazol-3-yl)phenyl]methyl]purine-2,6-dione: Y132 (≠ L85), L133 (≠ I86), P135 (= P88), F138 (= F91), P163 (≠ E116), P165 (= P118), H169 (= H122), E214 (= E167)
Sites not aligning to the query:
7zifA Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor km-480 (see paper)
33% identity, 81% coverage: 19:232/263 of query aligns to 62:278/291 of 7zifA
- binding fe (iii) ion: H169 (= H122), H174 (= H127), E214 (= E167)
- binding (2R)-2-azanyl-5-[[2-[3-methyl-2,6-bis(oxidanylidene)-7-(phenylmethyl)purin-8-yl]sulfanyl-3H-benzimidazol-5-yl]amino]-5-oxidanylidene-pentanoic acid: Y132 (≠ L85), L133 (≠ I86), P135 (= P88), F138 (= F91), Y161 (= Y114), T162 (≠ I115), P165 (= P118), H169 (= H122), E214 (= E167)
5tpgA Optimization of spirocyclic proline tryptophanhydroxylase-1 inhibitors (see paper)
33% identity, 81% coverage: 19:232/263 of query aligns to 42:258/271 of 5tpgA
- active site: H149 (= H122), H154 (= H127), E194 (= E167), S213 (= S186)
- binding (3S)-8-(2-amino-6-{(1R)-1-[5-chloro-3'-(methylsulfonyl)[1,1'-biphenyl]-2-yl]-2,2,2-trifluoroethoxy}pyrimidin-4-yl)-2,8-diazaspiro[4.5]decane-3-carboxylic acid: Y112 (≠ L85), P115 (= P88), F118 (= F91), R134 (= R107), Y141 (= Y114), T142 (≠ I115), P143 (≠ E116), E144 (= E117), A186 (≠ F159), Y189 (≠ F162), E194 (= E167), S213 (= S186), S214 (= S187)
- binding fe (iii) ion: H149 (= H122), H154 (= H127), E194 (= E167)
5j6dA Discovery of acyl guanidine tryptophan hydroxylase-1 inhibitors (see paper)
33% identity, 81% coverage: 19:232/263 of query aligns to 64:280/292 of 5j6dA
- active site: H171 (= H122), H176 (= H127), E216 (= E167), S235 (= S186)
- binding 4-[(N-{[2-(3-methoxyphenoxy)-6-(piperidin-1-yl)phenyl]methyl}carbamimidoyl)carbamoyl]-L-phenylalanine: Y134 (≠ L85), L135 (≠ I86), R156 (= R107), Y163 (= Y114), T164 (≠ I115), P165 (≠ E116), P167 (= P118), H171 (= H122), A208 (≠ F159), Y211 (≠ F162), F212 (≠ W163), E216 (= E167), S235 (= S186), S236 (= S187), I265 (= I217)
- binding fe (iii) ion: H171 (= H122), H176 (= H127), E216 (= E167)
Sites not aligning to the query:
7zikA Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor lp533401 (see paper)
33% identity, 81% coverage: 19:232/263 of query aligns to 47:263/275 of 7zikA
- binding fe (iii) ion: H154 (= H122), H159 (= H127), E199 (= E167)
- binding (2~{R})-2-azanyl-3-[4-[2-azanyl-6-[(1~{R})-1-[4-chloranyl-2-(3-methylpyrazol-1-yl)phenyl]-2,2,2-tris(fluoranyl)ethoxy]pyrimidin-4-yl]phenyl]propanoic acid: Y117 (≠ L85), R139 (= R107), Y146 (= Y114), T147 (≠ I115), H154 (= H122), A191 (≠ F159), F195 (≠ W163), E199 (= E167), G215 (= G183), S218 (= S186), S219 (= S187), C246 (≠ Y215), I248 (= I217)
8cjjA Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor km-06-057 (see paper)
33% identity, 81% coverage: 19:232/263 of query aligns to 62:278/292 of 8cjjA
- binding fe (iii) ion: H169 (= H122), H174 (= H127), E214 (= E167)
- binding 3-ethyl-7-(phenylmethyl)-8-(5,6,7,8-tetrahydroimidazo[1,2-a]pyridin-2-ylmethyl)purine-2,6-dione: Y132 (≠ L85), L133 (≠ I86), P135 (= P88), F138 (= F91), P165 (= P118), H169 (= H122), E214 (= E167)
Query Sequence
>WP_012757074.1 NCBI__GCF_000023185.1:WP_012757074.1
MTKESSYTAKLPGPDGLYDYTPDEDVIWGELYRRQMTLLSDTACREYLDGVKMLGLKPDK
VPQLLDVNRRLNETTGFGVEGVPALIPPSRFYELLSQGKFPLATFLRRREHIDYIEEPDL
FHEVFGHCPMLTNQSYANFVRHFGETAVRLGKGYSWHLFRIFWFTVEFGLINTPQGRRCF
GAGIVSSPNEAKAAMEGKACEFRPFDLLSVLRTPYRIDILQPIYYLIDSFADLEAIVEQD
IEATILKAKQLGDFAPAFEAKAS
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