SitesBLAST
Comparing PP_2552 FitnessBrowser__Putida:PP_2552 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
99% identity, 100% coverage: 2:470/470 of query aligns to 2:465/470 of 7xinA
- binding pyridoxal-5'-phosphate: F80 (= F80), T139 (= T139), A140 (= A140), S141 (= S141), H181 (= H181), T238 (= T238), D263 (= D263), A265 (= A265), N292 (= N292), H294 (= H294), K295 (= K295)
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)
41% identity, 99% coverage: 1:466/470 of query aligns to 12:482/490 of Q8RY79
- P92 (= P81) binding
- H193 (= H181) binding
- H308 (= H294) binding
- K309 (= K295) modified: N6-(pyridoxal phosphate)lysine
- F338 (≠ Y324) binding ; mutation to Y: Abolishes phenylacetaldehyde synthase activity.
6eeiB Crystal structure of arabidopsis thaliana phenylacetaldehyde synthase in complex with l-phenylalanine (see paper)
42% identity, 99% coverage: 1:466/470 of query aligns to 5:464/471 of 6eeiB
6eemB Crystal structure of papaver somniferum tyrosine decarboxylase in complex with l-tyrosine (see paper)
39% identity, 99% coverage: 1:466/470 of query aligns to 4:481/488 of 6eemB
O82415 Tyrosine decarboxylase; PsTyDC; EC 4.1.1.25 from Papaver somniferum (Opium poppy) (see 3 papers)
39% identity, 99% coverage: 1:466/470 of query aligns to 20:504/512 of O82415
- P100 (= P81) binding
- S101 (= S82) mutation to A: No effect on catalytic activity.
- C170 (≠ S141) mutation to S: No effect on catalytic activity.
- H205 (= H181) binding ; mutation to N: Acquires the capacity to produce 4-hydroxyphenylacetaldehyde from L-tyrosine.
- N318 (= N292) mutation to S: No effect on catalytic activity.
- A319 (= A293) mutation to P: No effect on catalytic activity.
- H320 (= H294) binding
- K321 (= K295) modified: N6-(pyridoxal phosphate)lysine
- Y350 (= Y324) binding ; mutation to F: Acquires the capacity to produce 4-hydroxyphenylacetaldehyde from L-tyrosine.
6eewA Crystal structure of catharanthus roseus tryptophan decarboxylase in complex with l-tryptophan (see paper)
40% identity, 99% coverage: 4:467/470 of query aligns to 7:474/479 of 6eewA
P14173 Aromatic-L-amino-acid decarboxylase; AADC; DOPA decarboxylase; DDC; EC 4.1.1.28 from Rattus norvegicus (Rat) (see 2 papers)
38% identity, 99% coverage: 1:467/470 of query aligns to 1:470/480 of P14173
- H192 (= H181) mutation to A: Abolishes decarboxylase activity.; mutation to Q: Reduces decarboxylase activity by 96%.
- D252 (= D244) mutation D->A,E: Abolishes decarboxylase activity.
- D271 (= D263) mutation to A: Abolishes decarboxylase activity.; mutation to E: Reduces decarboxylase activity by 65%.
- S296 (= S288) mutation to A: Abolishes decarboxylase activity.
- N300 (= N292) mutation to A: Reduces decarboxylase activity by 75%.
- H302 (= H294) mutation to Q: Reduces decarboxylase activity by 99.8%.
- K303 (= K295) mutation K->A,R: Abolishes decarboxylase activity.
- Y332 (= Y324) mutation Y->A,F: Abolishes decarboxylase activity.
- R355 (= R345) mutation to A: Abolishes decarboxylase activity.; mutation to K: No effect.
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)
40% identity, 99% coverage: 4:467/470 of query aligns to 25:492/500 of P17770
- P102 (= P81) binding
- H203 (= H181) binding
- H318 (= H294) binding
- K319 (= K295) modified: N6-(pyridoxal phosphate)lysine
- Y348 (= Y324) binding ; mutation to F: Acquires the capacity to produce indole-3-acetaldehyde from tryptophan.
- G370 (= G344) mutation to S: Acquires the capacity to produce dopamine from L-dopa and increased accumulation of phenylethylamine by gating indolic versus phenolic substrates.
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)
40% identity, 99% coverage: 1:466/470 of query aligns to 20:494/514 of Q06086
- F346 (≠ Y324) mutation to Y: Abolishes 4-hydroxyphenylacetaldehyde synthase activity.
8oraA Human holo aromatic l-amino acid decarboxylase (aadc) external aldimine with l-dopa methylester (see paper)
38% identity, 99% coverage: 1:467/470 of query aligns to 1:470/480 of 8oraA
- binding pyridoxal-5'-phosphate: F80 (= F80), S147 (≠ T139), A148 (= A140), S149 (= S141), H192 (= H181), T246 (= T238), D271 (= D263), A273 (= A265), N300 (= N292), H302 (= H294), K303 (= K295)
- binding methyl (2~{R})-2-azanyl-3-[3,4-bis(oxidanyl)phenyl]propanoate: Y79 (= Y79), H192 (= H181), T246 (= T238), K303 (= K295)
P20711 Aromatic-L-amino-acid decarboxylase; AADC; DOPA decarboxylase; DDC; EC 4.1.1.28 from Homo sapiens (Human) (see 8 papers)
38% identity, 99% coverage: 1:467/470 of query aligns to 1:470/480 of P20711
- M17 (≠ I17) to V: in dbSNP:rs6264
- E61 (≠ N61) to D: in dbSNP:rs11575292
- A148 (= A140) binding
- S149 (= S141) binding
- P210 (= P202) to L: in dbSNP:rs6262
- M217 (≠ L209) to V: in dbSNP:rs6263
- M239 (≠ V231) to I: in dbSNP:rs11575377; to L: in dbSNP:rs11575376
- T246 (= T238) binding
- N300 (= N292) binding
- K303 (= K295) modified: N6-(pyridoxal phosphate)lysine
- R462 (= R459) to Q: in dbSNP:rs11575542
P80041 Aromatic-L-amino-acid decarboxylase; AADC; DOPA decarboxylase; DDC; EC 4.1.1.28 from Sus scrofa (Pig) (see 2 papers)
39% identity, 99% coverage: 1:465/470 of query aligns to 1:468/486 of P80041
- M1 (= M1) modified: N-acetylmethionine
- T82 (≠ S82) binding
- H192 (= H181) binding
- K303 (= K295) modified: N6-(pyridoxal phosphate)lysine
P19113 Histidine decarboxylase; HDC; EC 4.1.1.22 from Homo sapiens (Human) (see 3 papers)
38% identity, 99% coverage: 1:466/470 of query aligns to 2:469/662 of P19113
- T31 (≠ M30) to M: in dbSNP:rs17740607
- E49 (≠ Q48) to V: in a colorectal cancer sample; somatic mutation
- E285 (= E275) to K: in a colorectal cancer sample; somatic mutation; dbSNP:rs1353958864
- K305 (= K295) mutation to G: Loss of enzyme activity.
- Y334 (= Y324) mutation to F: Loss of enzyme activity.
- S354 (≠ G344) mutation to G: Strongly decreases affinity for histidine. Strongly increases affinity for L-DOPA and confers enzyme activity toward L-DOPA.
4e1oC Human histidine decarboxylase complex with histidine methyl ester (hme) (see paper)
38% identity, 99% coverage: 1:466/470 of query aligns to 6:473/481 of 4e1oC
- binding pyridoxal-5'-phosphate: Y85 (≠ F80), T153 (= T139), V154 (≠ A140), S155 (= S141), H198 (= H181), T252 (= T238), D277 (= D263), A279 (= A265), K309 (= K295)
- binding histidine-methyl-ester: Y84 (= Y79), Y85 (≠ F80), L106 (= L101), H198 (= H181), T252 (= T238), K309 (= K295), Y338 (= Y324)
P05031 Aromatic-L-amino-acid decarboxylase; AADC; DOPA decarboxylase; DDC; EC 4.1.1.28 from Drosophila melanogaster (Fruit fly) (see 3 papers)
36% identity, 99% coverage: 1:464/470 of query aligns to 36:499/510 of P05031
- T117 (≠ S82) binding ; mutation to A: Decreased specific activity to L-DOPA. Increased specific activity to 5-HTP. Decreased ligand binding affinity.; mutation to S: Increased specific activity to L-DOPA and 5-HTP. Decreased ligand binding affinity.
- A183 (= A140) binding
- S184 (= S141) binding
- K197 (≠ R154) to N: in allele Ddc-R9
- H227 (= H181) active site; binding ; binding ; mutation to N: Enzymatic shift from L-dopa decarboxylation of to L-Dopa decarboxylation-oxidative deamination.; mutation to W: Decreased specific activity to L-DOPA and 5-HTP. Decreased ligand binding affinity.
- V264 (≠ L222) to M: in allele Ddc-R11 and allele Ddc-R18
- D305 (= D263) binding
- N334 (= N292) binding
- 358:384 (vs. 316:342, 30% identical) Disordered
- R390 (= R348) to M: in allele Ddc-Ore
- S428 (≠ A386) to F: in allele Ddc-R33
- S489 (≠ R454) to A: in allele Ddc-2b
Sites not aligning to the query:
- 12 T → P: in allele Ddc-R6, allele Ddc-R9, allele Ddc-R16, allele Ddc-R20, allele Ddc-R25 and allele Ddc-R30
1js3A Crystal structure of dopa decarboxylase in complex with the inhibitor carbidopa (see paper)
38% identity, 99% coverage: 1:465/470 of query aligns to 1:456/464 of 1js3A
- binding carbidopa: W71 (= W71), Y79 (= Y79), F80 (= F80), T82 (≠ S82), H192 (= H181), H302 (= H294), K303 (= K295)
- binding pyridoxal-5'-phosphate: S147 (≠ T139), A148 (= A140), S149 (= S141), H192 (= H181), D271 (= D263), A273 (= A265), N300 (= N292), H302 (= H294), K303 (= K295)
7eiyA Human histidine decarboxylase mutant y334f soaking with histidine
37% identity, 99% coverage: 1:466/470 of query aligns to 1:460/467 of 7eiyA
- binding histidine: Y80 (≠ F80), H193 (= H181), T247 (= T238), K304 (= K295)
- binding pyridoxal-5'-phosphate: Y80 (≠ F80), T148 (= T139), V149 (≠ A140), S150 (= S141), H193 (= H181), T247 (= T238), D272 (= D263), A274 (= A265), K304 (= K295)
6khpA Crystal structure of oryza sativa tdc with plp and tryptamine (see paper)
38% identity, 99% coverage: 1:465/470 of query aligns to 5:482/490 of 6khpA
- binding pyridoxal-5'-phosphate: F84 (= F80), T150 (= T139), T151 (≠ A140), S152 (= S141), H190 (= H181), D274 (= D263), A276 (= A265), K306 (= K295), V356 (≠ L343), G357 (= G344)
- binding 2-(1h-indol-3-yl)ethanamine: V105 (≠ L101), F107 (≠ L103), Y335 (= Y324)
6khnA Crystal structure of oryza sativa tdc with plp and serotonin (see paper)
38% identity, 99% coverage: 1:465/470 of query aligns to 5:482/490 of 6khnA
- binding pyridoxal-5'-phosphate: F84 (= F80), T150 (= T139), T151 (≠ A140), S152 (= S141), H190 (= H181), D274 (= D263), A276 (= A265), K306 (= K295), V356 (≠ L343), G357 (= G344)
- binding serotonin: F107 (≠ L103), Y335 (= Y324), G357 (= G344)
Q6ZJK7 Tryptophan decarboxylase 1; 5-hydroxytryptophan decarboxylase TDC1; EC 4.1.1.28 from Oryza sativa subsp. japonica (Rice) (see paper)
37% identity, 99% coverage: 1:465/470 of query aligns to 25:506/514 of Q6ZJK7
- W95 (= W71) mutation to A: Abolishes enzymatic activity.
- F104 (= F80) binding
- S106 (= S82) mutation to A: Slightly increases enzymatic activity.
- F127 (≠ L103) mutation to A: Reduces enzymatic activity 5-fold.
- T175 (≠ A140) binding
- S176 (= S141) binding
- H214 (= H181) 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 (= D263) mutation to A: Abolishes enzymatic activity.
- A300 (= A265) mutation to G: Reduces enzymatic activity 7-fold.
- K330 (= K295) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Abolishes enzymatic activity.
- L336 (≠ F301) mutation to A: Reduces enzymatic activity 40-fold.
- E358 (≠ S323) mutation to A: Slightly decreases enzymatic activity.
- Y359 (= Y324) active site, Proton donor; mutation Y->A,F,H: Abolishes enzymatic activity.; mutation to Q: Reduces enzymatic activity 20-fold.
- L360 (= L325) mutation to A: Abolishes enzymatic activity.
- K361 (≠ Q326) mutation to A: No effect on enzymatic activity.
- V380 (≠ L343) binding ; mutation to A: Reduces enzymatic activity 5-fold.
- G381 (= G344) binding
Query Sequence
>PP_2552 FitnessBrowser__Putida:PP_2552
MTPEQFRQYGHQLIDLIADYRQTVGERPVMAQVEPGYLKAALPATAPQQGEPFAAILDDV
NNLVMPGLSHWQHPDFYGYFPSNGTLSSVLGDFLSTGLGVLGLSWQSSPALSELEETTLD
WLRQLLGLSGQWSGVIQDTASTSTLVALISARERATDYALVRGGLQAEPKPLIVYVSAHA
HSSVDKAALLAGFGRDNIRLIPTDERYALRPEALQAAIEQDLAAGNQPCAVVATTGTTTT
TALDPLRPVGEIAQANGLWLHVDSAMAGSAMILPECRWMWDGIELADSVVVNAHKWLGVA
FDCSIYYVRDPQHLIRVMSTNPSYLQSAVDGEVKNLRDWGIPLGRRFRALKLWFMLRSEG
VDALQARLRRDLDNAQWLAGQVEAAAEWEVLAPVQLQTLCIRHRPAGLEGEALDAHTKGW
AERLNASGAAYVTPATLDGRWMVRVSIGALPTERGDVQRLWARLQDVIKG
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