SitesBLAST
Comparing 8502206 FitnessBrowser__Miya:8502206 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)
7xinA Crystal structure of dodc from pseudomonas
33% identity, 91% coverage: 10:475/510 of query aligns to 4:456/470 of 7xinA
- binding pyridoxal-5'-phosphate: F80 (≠ I89), T139 (≠ G155), A140 (≠ G156), S141 (≠ T157), H181 (= H196), T238 (≠ V253), D263 (= D278), A265 (= A280), N292 (≠ D307), H294 (= H309), K295 (= K310)
A7B1V0 Tryptophan decarboxylase; Trp decarboxylase; EC 4.1.1.105 from Ruminococcus gnavus (strain ATCC 29149 / VPI C7-9) (see paper)
29% identity, 89% coverage: 37:488/510 of query aligns to 47:486/490 of A7B1V0
- K306 (= K310) modified: N6-(pyridoxal phosphate)lysine
6eemB Crystal structure of papaver somniferum tyrosine decarboxylase in complex with l-tyrosine (see paper)
30% identity, 91% coverage: 7:468/510 of query aligns to 4:469/488 of 6eemB
P14173 Aromatic-L-amino-acid decarboxylase; AADC; DOPA decarboxylase; DDC; EC 4.1.1.28 from Rattus norvegicus (Rat) (see 2 papers)
30% identity, 88% coverage: 37:486/510 of query aligns to 28:475/480 of P14173
- H192 (= H196) mutation to A: Abolishes decarboxylase activity.; mutation to Q: Reduces decarboxylase activity by 96%.
- D252 (= D259) mutation D->A,E: Abolishes decarboxylase activity.
- D271 (= D278) mutation to A: Abolishes decarboxylase activity.; mutation to E: Reduces decarboxylase activity by 65%.
- S296 (= S303) mutation to A: Abolishes decarboxylase activity.
- N300 (≠ D307) mutation to A: Reduces decarboxylase activity by 75%.
- H302 (= H309) mutation to Q: Reduces decarboxylase activity by 99.8%.
- K303 (= K310) mutation K->A,R: Abolishes decarboxylase activity.
- Y332 (= Y339) mutation Y->A,F: Abolishes decarboxylase activity.
- R355 (= R357) mutation to A: Abolishes decarboxylase activity.; mutation to K: No effect.
4obvC Ruminococcus gnavus tryptophan decarboxylase rumgna_01526 (alpha-fmt) (see paper)
28% identity, 89% coverage: 37:488/510 of query aligns to 32:468/471 of 4obvC
- binding alpha-(fluoromethyl)-D-tryptophan: P87 (= P95), A88 (= A96), S90 (≠ T98), F294 (= F313), P444 (≠ H464), E445 (≠ R465)
- binding {5-hydroxy-4-[(1E)-4-(1H-indol-3-yl)-3-oxobut-1-en-1-yl]-6-methylpyridin-3-yl}methyl dihydrogen phosphate: F83 (≠ W88), V84 (≠ I89), H105 (≠ A110), G144 (= G156), S145 (≠ T157), H177 (= H196), T234 (≠ V253), D259 (= D278), A261 (= A280), D288 (= D307), K291 (= K310), L321 (= L340), W331 (≠ K349), T338 (≠ S356)
6khpA Crystal structure of oryza sativa tdc with plp and tryptamine (see paper)
30% identity, 94% coverage: 7:486/510 of query aligns to 5:489/490 of 6khpA
- binding pyridoxal-5'-phosphate: F84 (≠ I89), T150 (≠ G155), T151 (≠ G156), S152 (≠ T157), H190 (= H196), D274 (= D278), A276 (= A280), K306 (= K310), V356 (≠ L355), G357 (≠ S356)
- binding 2-(1h-indol-3-yl)ethanamine: V105 (≠ A110), F107 (≠ L112), Y335 (= Y339)
6khnA Crystal structure of oryza sativa tdc with plp and serotonin (see paper)
30% identity, 94% coverage: 7:486/510 of query aligns to 5:489/490 of 6khnA
- binding pyridoxal-5'-phosphate: F84 (≠ I89), T150 (≠ G155), T151 (≠ G156), S152 (≠ T157), H190 (= H196), D274 (= D278), A276 (= A280), K306 (= K310), V356 (≠ L355), G357 (≠ S356)
- binding serotonin: F107 (≠ L112), Y335 (= Y339), G357 (≠ S356)
4obuA Ruminococcus gnavus tryptophan decarboxylase rumgna_01526 (apo) (see paper)
28% identity, 89% coverage: 37:488/510 of query aligns to 32:458/462 of 4obuA
P20711 Aromatic-L-amino-acid decarboxylase; AADC; DOPA decarboxylase; DDC; EC 4.1.1.28 from Homo sapiens (Human) (see 8 papers)
29% identity, 88% coverage: 38:486/510 of query aligns to 29:475/480 of P20711
- E61 (≠ A70) to D: in dbSNP:rs11575292
- A148 (vs. gap) binding
- S149 (≠ T157) binding
- P210 (= P217) to L: in dbSNP:rs6262
- M217 (= M224) to V: in dbSNP:rs6263
- M239 (≠ V246) to I: in dbSNP:rs11575377; to L: in dbSNP:rs11575376
- T246 (≠ V253) binding
- N300 (≠ D307) binding
- K303 (= K310) modified: N6-(pyridoxal phosphate)lysine
- R462 (≠ L473) to Q: in dbSNP:rs11575542
Sites not aligning to the query:
- 17 M → V: in dbSNP:rs6264
8oraA Human holo aromatic l-amino acid decarboxylase (aadc) external aldimine with l-dopa methylester (see paper)
29% identity, 91% coverage: 23:486/510 of query aligns to 17:475/480 of 8oraA
- binding pyridoxal-5'-phosphate: F80 (≠ I89), S147 (≠ G156), A148 (vs. gap), S149 (≠ T157), H192 (= H196), T246 (≠ V253), D271 (= D278), A273 (= A280), N300 (≠ D307), H302 (= H309), K303 (= K310)
- binding methyl (2~{R})-2-azanyl-3-[3,4-bis(oxidanyl)phenyl]propanoate: Y79 (≠ W88), H192 (= H196), T246 (≠ V253), K303 (= K310)
Q8RY79 Phenylacetaldehyde synthase; AtPAAS; 3,4-dihydroxyphenylacetaldehyde synthase; DHPAA synthase; Aromatic L-amino acid decarboxylase; Aromatic aldehyde synthase; AtAAS; EC 4.1.1.109; EC 4.1.1.107 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
29% identity, 91% coverage: 7:472/510 of query aligns to 12:474/490 of Q8RY79
- P92 (≠ T90) binding
- H193 (= H196) binding
- H308 (= H309) binding
- K309 (= K310) modified: N6-(pyridoxal phosphate)lysine
- F338 (≠ Y339) binding ; mutation to Y: Abolishes phenylacetaldehyde synthase activity.
6eeiB Crystal structure of arabidopsis thaliana phenylacetaldehyde synthase in complex with l-phenylalanine (see paper)
29% identity, 91% coverage: 7:472/510 of query aligns to 5:456/471 of 6eeiB
P80041 Aromatic-L-amino-acid decarboxylase; AADC; DOPA decarboxylase; DDC; EC 4.1.1.28 from Sus scrofa (Pig) (see 2 papers)
30% identity, 92% coverage: 7:476/510 of query aligns to 1:465/486 of P80041
- M1 (≠ L7) modified: N-acetylmethionine
- T82 (= T91) binding
- H192 (= H196) binding
- K303 (= K310) modified: N6-(pyridoxal phosphate)lysine
O82415 Tyrosine decarboxylase; PsTyDC; EC 4.1.1.25 from Papaver somniferum (Opium poppy) (see 3 papers)
29% identity, 91% coverage: 7:468/510 of query aligns to 20:492/512 of O82415
- P100 (≠ T90) binding
- S101 (≠ T91) mutation to A: No effect on catalytic activity.
- C170 (≠ M158) mutation to S: No effect on catalytic activity.
- H205 (= H196) binding ; mutation to N: Acquires the capacity to produce 4-hydroxyphenylacetaldehyde from L-tyrosine.
- N318 (≠ D307) mutation to S: No effect on catalytic activity.
- A319 (≠ P308) mutation to P: No effect on catalytic activity.
- H320 (= H309) binding
- K321 (= K310) modified: N6-(pyridoxal phosphate)lysine
- Y350 (= Y339) binding ; mutation to F: Acquires the capacity to produce 4-hydroxyphenylacetaldehyde from L-tyrosine.
1js3A Crystal structure of dopa decarboxylase in complex with the inhibitor carbidopa (see paper)
30% identity, 94% coverage: 7:487/510 of query aligns to 1:464/464 of 1js3A
- binding carbidopa: W71 (≠ I80), Y79 (≠ W88), F80 (≠ I89), T82 (= T91), H192 (= H196), H302 (= H309), K303 (= K310)
- binding pyridoxal-5'-phosphate: S147 (≠ G156), A148 (vs. gap), S149 (≠ T157), H192 (= H196), D271 (= D278), A273 (= A280), N300 (≠ D307), H302 (= H309), K303 (= K310)
Q6ZJK7 Tryptophan decarboxylase 1; 5-hydroxytryptophan decarboxylase TDC1; EC 4.1.1.28 from Oryza sativa subsp. japonica (Rice) (see paper)
30% identity, 95% coverage: 2:486/510 of query aligns to 20:513/514 of Q6ZJK7
- W95 (≠ I80) mutation to A: Abolishes enzymatic activity.
- F104 (≠ I89) binding
- S106 (≠ T91) mutation to A: Slightly increases enzymatic activity.
- F127 (≠ L112) mutation to A: Reduces enzymatic activity 5-fold.
- T175 (≠ G156) binding
- S176 (≠ T157) binding
- H214 (= H196) binding ; mutation H->A,F,Q: Reduces enzymatic activity 50-fold.; mutation to Q: Reduces enzymatic activity 20-fold.; mutation to Y: Abolishes enzymatic activity.
- D298 (= D278) mutation to A: Abolishes enzymatic activity.
- A300 (= A280) mutation to G: Reduces enzymatic activity 7-fold.
- K330 (= K310) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Abolishes enzymatic activity.
- L336 (= L316) mutation to A: Reduces enzymatic activity 40-fold.
- E358 (≠ S338) mutation to A: Slightly decreases enzymatic activity.
- Y359 (= Y339) active site, Proton donor; mutation Y->A,F,H: Abolishes enzymatic activity.; mutation to Q: Reduces enzymatic activity 20-fold.
- L360 (= L340) mutation to A: Abolishes enzymatic activity.
- K361 (≠ G341) mutation to A: No effect on enzymatic activity.
- V380 (≠ L355) binding ; mutation to A: Reduces enzymatic activity 5-fold.
- G381 (≠ S356) binding
6eewA Crystal structure of catharanthus roseus tryptophan decarboxylase in complex with l-tryptophan (see paper)
28% identity, 94% coverage: 7:486/510 of query aligns to 4:479/479 of 6eewA
Q06086 4-hydroxyphenylacetaldehyde synthase; HPAA synthase; 3,4-dihydroxyphenylacetaldehyde synthase; DHPAA synthase; Aromatic acetaldehyde synthase; PcAAS; EC 4.1.1.108; EC 4.1.1.107 from Petroselinum crispum (Parsley) (Petroselinum hortense) (see paper)
30% identity, 90% coverage: 5:461/510 of query aligns to 18:475/514 of Q06086
- F346 (≠ Y339) mutation to Y: Abolishes 4-hydroxyphenylacetaldehyde synthase activity.
P17770 Aromatic-L-amino-acid decarboxylase; AADC; DOPA decarboxylase; Tryptophan decarboxylase; CrTDC; EC 4.1.1.28 from Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) (see 3 papers)
28% identity, 95% coverage: 7:489/510 of query aligns to 22:500/500 of P17770
- P102 (≠ T90) binding
- H203 (= H196) binding
- H318 (= H309) binding
- K319 (= K310) modified: N6-(pyridoxal phosphate)lysine
- Y348 (= Y339) binding ; mutation to F: Acquires the capacity to produce indole-3-acetaldehyde from tryptophan.
- G370 (≠ S356) mutation to S: Acquires the capacity to produce dopamine from L-dopa and increased accumulation of phenylethylamine by gating indolic versus phenolic substrates.
P18486 3,4-dihydroxyphenylacetaldehyde synthase; DHPAA synthase; DOPAL synthase; Alpha-methyldopa resistant protein; AMD-r protein; EC 4.1.1.107 from Drosophila melanogaster (Fruit fly) (see paper)
31% identity, 91% coverage: 7:471/510 of query aligns to 1:460/510 of P18486
- N192 (≠ H196) mutation to H: Enzymatic shift from L-dopa decarboxylation-oxidative deamination to L-Dopa decarboxylation.
Query Sequence
>8502206 FitnessBrowser__Miya:8502206
MQRHETLDLEDFEALLHRAATMIADRVERIGPCAQGPVVPPATFDELAALIPSDWPEAGA
GAHAVLDDVARCIEPYATRIGHPRFLAWITTSPAPAGTLGDIVCTGLNQAPLSFKGGPAA
TVLEHVVLGWLARLFDLPQAADEGMDGAGGTIVSGGTMANLMGLTVARHTHFPEAATRGL
AGIGRIPVLYVSDQGHMSIERSAVLLGLGADNVRAIPSGADNRMDVAALRAAITMDREAG
LAPFCVVAQAGSVTTGAVDPLPDIADTCADEGLWFHVDAAYGGAAMLTDEGRALLAGIHR
ADSICVDPHKWFFIPLECGVTLFRSKAQQLATFRARASYLGEENPHDLKNTTFILSRANR
ALKVWFAFRTYGRERLRRIVTRNMELARHFRDLCAASPEWRVLAPVQLSIACARYVPQGG
GWTEEDVDRLQVRLLERLEASGEGFLTPAMVRGRAGVRLCVANHRTSEADIRLLFDLMTT
LGRELVAQGPQGPHASQPPQAPQTTQTPQV
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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