SitesBLAST
Comparing WP_057509085.1 NCBI__GCF_001431535.1:WP_057509085.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
Q8PDA8 Tryptophan 2,3-dioxygenase; TDO; Tryptamin 2,3-dioxygenase; Tryptophan oxygenase; TO; TRPO; Tryptophan pyrrolase; Tryptophanase; EC 1.13.11.11 from Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) (see 2 papers)
85% identity, 99% coverage: 1:282/284 of query aligns to 1:282/298 of Q8PDA8
- FIIQH 51:55 (= FIIQH 51:55) binding
- H55 (= H55) mutation to A: Decrease in catalytic efficiency using L-tryptophan, 5-fluoro-D/L-tryptophan, 6-fluoro-D/L-tryptophan, 5-methyl-D/L-tryptophan and 6-methyl-D/L-tryptophan as substrate.; mutation to S: Decrease in catalytic efficiency using L-tryptophan, 5-fluoro-D/L-tryptophan, 6-fluoro-D/L-tryptophan, 5-methyl-D/L-tryptophan and 6-methyl-D/L-tryptophan as substrate.
- Y113 (= Y113) binding
- R117 (= R117) binding
- H240 (= H240) binding axial binding residue
- T254 (= T254) binding
7p46A Crystal structure of xanthomonas campestris tryptophan 2,3-dioxygenase (tdo) (see paper)
85% identity, 98% coverage: 5:282/284 of query aligns to 1:278/281 of 7p46A
- binding protoporphyrin ix containing fe: S51 (≠ H55), S54 (= S58), W98 (= W102), S120 (= S124), G121 (= G125), F122 (= F126), Y127 (= Y131), R128 (= R132), H236 (= H240), V240 (= V244), G249 (= G253), G251 (= G255), S253 (= S257)
- binding (2S)-2-amino-4-(2-aminophenyl)-4-oxobutanoic acid: F47 (= F51), S51 (≠ H55), Y109 (= Y113), R113 (= R117), S119 (= S123), G249 (= G253), T250 (= T254)
- binding tryptophan: K82 (= K86), A85 (= A89), Y216 (= Y220), S217 (≠ A221), E220 (= E224), D224 (= D228)
2nw9A Crystal structure of tryptophan 2,3-dioxygenase (tdo) from xanthomonas campestris in complex with ferrous heme and 6-fluoro-tryptophan. Northeast structural genomics target xcr13 (see paper)
87% identity, 92% coverage: 21:282/284 of query aligns to 2:263/265 of 2nw9A
- binding 6-fluoro-l-tryptophan: F32 (= F51), H36 (= H55), Y94 (= Y113), R98 (= R117), L101 (= L120), S104 (= S123), G234 (= G253), T235 (= T254)
- binding protoporphyrin ix containing fe: F32 (= F51), H36 (= H55), S39 (= S58), W83 (= W102), L86 (= L105), G106 (= G125), F107 (= F126), Y112 (= Y131), R113 (= R132), H221 (= H240), V225 (= V244), I229 (= I248), G234 (= G253), G236 (= G255), S238 (= S257)
1yw0A Crystal structure of the tryptophan 2,3-dioxygenase from xanthomonas campestris. Northeast structural genomics target xcr13.
80% identity, 92% coverage: 23:282/284 of query aligns to 1:241/243 of 1yw0A
Q1LK00 Tryptophan 2,3-dioxygenase; TDO; Tryptamin 2,3-dioxygenase; Tryptophan oxygenase; TO; TRPO; Tryptophan pyrrolase; Tryptophanase; EC 1.13.11.11 from Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans) (see paper)
49% identity, 95% coverage: 13:282/284 of query aligns to 32:299/299 of Q1LK00
- F68 (= F51) mutation to A: Abolishes catalytic activity.
- Y130 (= Y113) mutation to F: 15-fold increase in catalytic activity.
- R134 (= R117) mutation to A: Abolishes catalytic activity.
- T271 (= T254) mutation to A: Abolishes catalytic activity.
2noxB Crystal structure of tryptophan 2,3-dioxygenase from ralstonia metallidurans (see paper)
48% identity, 95% coverage: 13:282/284 of query aligns to 3:266/266 of 2noxB
- binding protoporphyrin ix containing fe: F39 (= F51), H43 (= H55), T46 (≠ S58), W90 (= W102), L93 (= L105), S112 (= S124), G113 (= G125), F114 (= F126), Y119 (= Y131), R120 (= R132), H228 (= H240), V232 (= V244), E242 (≠ S258), Y246 (≠ F262), L247 (= L263)
P20351 Tryptophan 2,3-dioxygenase; TDO; Protein vermilion; Tryptamin 2,3-dioxygenase; Tryptophan oxygenase; TO; TRPO; Tryptophan pyrrolase; Tryptophanase; EC 1.13.11.11 from Drosophila melanogaster (Fruit fly) (see paper)
30% identity, 91% coverage: 24:282/284 of query aligns to 27:357/379 of P20351
- D123 (≠ E112) mutation to A: Strongly reduced enzyme activity.
- Y236 (vs. gap) mutation to F: Strongly reduced enzyme activity.
- R309 (= R237) mutation to A: Strongly reduced enzyme activity.
- H312 (= H240) binding axial binding residue
- Y335 (≠ F262) mutation to F: Strongly reduced enzyme activity.
4hkaA Crystal structure of drosophila melanogaster tryptophan 2,3- dioxygenase in complex with heme (see paper)
30% identity, 91% coverage: 24:282/284 of query aligns to 4:334/345 of 4hkaA
- binding protoporphyrin ix containing fe: H38 (= H55), Y41 (≠ S58), F45 (≠ L62), L93 (= L105), F101 (≠ Y113), F114 (= F126), Q115 (= Q127), F119 (≠ Y131), Y136 (vs. gap), W285 (= W236), H289 (= H240), V293 (= V244), Y312 (≠ F262), L313 (= L263)
5ti9C Crystal structure of human tdo in complex with trp and dioxygen, northeast structural genomics consortium target hr6161 (see paper)
29% identity, 92% coverage: 22:282/284 of query aligns to 1:307/326 of 5ti9C
- binding protoporphyrin ix containing fe: H37 (= H55), Y40 (≠ S58), L93 (= L105), S112 (= S124), G113 (= G125), F114 (= F126), F119 (≠ Y131), R120 (= R132), W259 (= W236), H263 (= H240), V267 (= V244), M270 (≠ V247), G276 (= G253), G278 (= G255), S280 (= S257), L286 (= L263)
- binding N'-Formylkynurenine: F33 (= F51), H37 (= H55), R105 (= R117), L108 (= L120), A111 (≠ S123), S112 (= S124), G113 (= G125), L271 (≠ I248), G276 (= G253), T277 (= T254)
- binding tryptophan: R64 (≠ W82), E66 (≠ C84), W159 (vs. gap), R162 (vs. gap), T163 (vs. gap), P164 (= P166), I230 (vs. gap), F239 (≠ Y216), P242 (≠ E219)
Q09474 Tryptophan 2,3-dioxygenase; TDO; Tryptamin 2,3-dioxygenase; Tryptophan oxygenase; TO; TRPO; Tryptophan pyrrolase; Tryptophanase; EC 1.13.11.11 from Caenorhabditis elegans (see paper)
28% identity, 91% coverage: 23:280/284 of query aligns to 38:369/403 of Q09474
- PLD 133:135 (≠ PSE 110:112) PLD motif; required for enzymatic activity; mutation Missing: Abolishes catalytic activity. Animals have an extended lifespan, an extended reproductive lifespan, have fewer hatched progeny and display increased motility.
6pyzC Crystal structure of human tryptophan 2,3-dioxygenase in complex with pf-06840003 in active site (see paper)
29% identity, 92% coverage: 22:282/284 of query aligns to 2:314/333 of 6pyzC
- binding (3S)-3-(5-fluoro-1H-indol-3-yl)pyrrolidine-2,5-dione: Y4 (= Y24), Y7 (= Y27), F34 (= F51), H38 (= H55), A112 (≠ S123), S113 (= S124), T284 (= T254)
- binding protoporphyrin ix containing fe: H38 (= H55), Y41 (≠ S58), L94 (= L105), G114 (= G125), F115 (= F126), F120 (≠ Y131), R121 (= R132), H270 (= H240), M273 (≠ T243), V274 (= V244), M277 (≠ V247), G283 (= G253), G285 (= G255), S287 (= S257), Y292 (≠ F262), L293 (= L263)
- binding alpha-methyl-L-tryptophan: R65 (≠ W82), E67 (≠ C84), W167 (≠ A162), R170 (vs. gap), T171 (≠ A165), P172 (= P166), F246 (≠ Y216)
6a4iD Crystal structure of human tdo inhibitor complex
32% identity, 81% coverage: 22:251/284 of query aligns to 1:250/290 of 6a4iD
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y24), Y6 (= Y27), F33 (= F51), H37 (= H55), A111 (≠ S123)
- binding protoporphyrin ix containing fe: F33 (= F51), H37 (= H55), Y40 (≠ S58), F101 (≠ Y113), S112 (= S124), G113 (= G125), F114 (= F126), F119 (≠ Y131), H239 (= H240), V243 (= V244), M246 (≠ V247)
- binding tryptophan: R64 (≠ W82), W153 (≠ A162), R156 (vs. gap), T157 (≠ A165), P158 (= P166), I206 (≠ E207), F215 (≠ Y216)
Sites not aligning to the query:
6a4iB Crystal structure of human tdo inhibitor complex
28% identity, 92% coverage: 22:282/284 of query aligns to 1:295/309 of 6a4iB
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y24), Y6 (= Y27), F33 (= F51), H37 (= H55), L108 (= L120), A111 (≠ S123)
- binding protoporphyrin ix containing fe: F33 (= F51), H37 (= H55), Y40 (≠ S58), L93 (= L105), S112 (= S124), G113 (= G125), F114 (= F126), F119 (≠ Y131), R120 (= R132), W255 (= W236), H259 (= H240), V263 (= V244), L274 (= L263)
- binding tryptophan: R64 (≠ W82), E66 (≠ C84), W153 (≠ A162), R156 (vs. gap), T157 (≠ A165), P158 (= P166), P238 (≠ E219)
6a4iA Crystal structure of human tdo inhibitor complex
28% identity, 92% coverage: 22:282/284 of query aligns to 1:313/322 of 6a4iA
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y24), Y6 (= Y27), F33 (= F51), H37 (= H55), A111 (≠ S123)
- binding protoporphyrin ix containing fe: F33 (= F51), H37 (= H55), Y40 (≠ S58), L93 (= L105), F101 (≠ Y113), S112 (= S124), G113 (= G125), F114 (= F126), F119 (≠ Y131), W270 (= W236), H274 (= H240), M277 (≠ T243), V278 (= V244), M281 (≠ V247), L292 (= L263)
- binding tryptophan: R64 (≠ W82), W158 (≠ G155), R161 (= R158), T162 (≠ R160), P163 (≠ Q161), I241 (vs. gap), F250 (vs. gap), P253 (vs. gap)
8r5qC Structure of apo tdo with a bound inhibitor
40% identity, 44% coverage: 22:147/284 of query aligns to 1:139/317 of 8r5qC
- binding 3-chloranyl-~{N}-[(1~{S})-1-(6-chloranylpyridin-3-yl)-2-phenyl-ethyl]aniline: Y3 (= Y24), Y6 (= Y27), L7 (= L28), F33 (= F51), H37 (= H55), F101 (≠ Y113), P110 (= P122), G113 (= G125), Q115 (= Q127), S116 (= S128)
- binding alpha-methyl-L-tryptophan: R64 (≠ W82), E66 (≠ C84)
Sites not aligning to the query:
5ti9D Crystal structure of human tdo in complex with trp and dioxygen, northeast structural genomics consortium target hr6161 (see paper)
40% identity, 42% coverage: 22:139/284 of query aligns to 2:128/332 of 5ti9D
- binding protoporphyrin ix containing fe: F34 (= F51), H38 (= H55), Y41 (≠ S58), L94 (= L105), S113 (= S124), G114 (= G125), F115 (= F126), F120 (≠ Y131), R121 (= R132)
- binding N'-Formylkynurenine: F34 (= F51), H38 (= H55), R106 (= R117), L109 (= L120), A112 (≠ S123), S113 (= S124), G114 (= G125)
- binding tryptophan: R65 (≠ W82), E67 (≠ C84)
Sites not aligning to the query:
- binding protoporphyrin ix containing fe: 137, 286, 289, 290, 300, 301
- binding tryptophan: 170, 173, 174, 175, 253, 262, 265
P48775 Tryptophan 2,3-dioxygenase; TDO; Tryptamin 2,3-dioxygenase; Tryptophan oxygenase; TO; TRPO; Tryptophan pyrrolase; Tryptophanase; EC 1.13.11.11 from Homo sapiens (Human) (see 3 papers)
36% identity, 49% coverage: 1:139/284 of query aligns to 18:166/406 of P48775
- Y42 (= Y24) mutation to A: Reduces enzyme activity by 99%.
- Y45 (= Y27) mutation to A: Reduces enzyme activity by 99%.
- F72 (= F51) mutation to A: Abolishes enzyme activity.
- FIITH 72:76 (≠ FIIQH 51:55) binding
- H76 (= H55) mutation to A: Abolishes enzyme activity.
- M108 (≠ V87) to I: in HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization; dbSNP:rs1553957997
- F140 (≠ Y113) mutation to A: Reduces enzyme activity by 99%.
- R144 (= R117) binding ; mutation to A: Reduces enzyme activity by 99%.
- S151 (= S124) mutation to A: Reduces enzyme activity by 90%.
Sites not aligning to the query:
- 175 Y→G: Reduces enzyme activity.
- 328 binding axial binding residue; H→A: Abolishes enzyme activity.
- 342 binding
8qv7B Crystal structure of human tdo with alpha-methyl-l-tryptophan
40% identity, 42% coverage: 22:139/284 of query aligns to 1:127/310 of 8qv7B
Sites not aligning to the query:
7lu7AAA Tryptophan 2,3-dioxygenase
40% identity, 42% coverage: 22:139/284 of query aligns to 2:128/341 of 7lu7AAA
- binding (1~{R})-1-cyclohexyl-2-[(5~{S})-5~{H}-imidazo[1,5-b]isoindol-5-yl]ethanol: Y4 (= Y24), Y7 (= Y27), F34 (= F51), H38 (= H55), A112 (≠ S123), G114 (= G125)
- binding protoporphyrin ix containing fe: F34 (= F51), H38 (= H55), Y41 (≠ S58), L94 (= L105), S113 (= S124), G114 (= G125), F115 (= F126), F120 (≠ Y131), R121 (= R132)
- binding alpha-methyl-L-tryptophan: R65 (≠ W82), E67 (≠ C84)
Sites not aligning to the query:
8r5qB Structure of apo tdo with a bound inhibitor
40% identity, 42% coverage: 22:139/284 of query aligns to 1:127/318 of 8r5qB
- binding 3-chloranyl-~{N}-[(1~{S})-1-(6-chloranylpyridin-3-yl)-2-phenyl-ethyl]aniline: Y3 (= Y24), Y6 (= Y27), L7 (= L28), F33 (= F51), H37 (= H55), F101 (≠ Y113), P110 (= P122), G113 (= G125), Q115 (= Q127), S116 (= S128)
- binding alpha-methyl-L-tryptophan: R64 (≠ W82), E66 (≠ C84)
Sites not aligning to the query:
Query Sequence
>WP_057509085.1 NCBI__GCF_001431535.1:WP_057509085.1
MSVDNNQRDLEAGILTDLQDRLTYGGYLRLDQLLSAQQPLSSPAHHDEMLFIIQHQTSEL
WLKLLAHELGAAIGFLQRDQVWQCQKVLARSKLVLRQLTEQWSVLETLTPSEYMGFRDVL
GPSSGFQSLQYRYIEFLLGNKNAQMLKVFEHDEAGQQRLRQALEAPSLYEEFLQYLSRFG
HDIPAQYLDRDWTQPHVADDALHPVFERIYQNTDRYWREYALCEDLVDLETAFQLWRFRH
MRTVMRVIGFKRGTGGSSGVGFLAKALELTFFPELFQVRTTLEG
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