SitesBLAST
Comparing Echvi_1046 FitnessBrowser__Cola:Echvi_1046 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
41% identity, 98% coverage: 6:473/477 of query aligns to 4:467/470 of 7xinA
- binding pyridoxal-5'-phosphate: F80 (= F82), T139 (= T141), A140 (= A142), S141 (= S143), H181 (= H182), T238 (= T239), D263 (= D264), A265 (= A266), N292 (= N293), H294 (= H295), K295 (= K296)
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, 98% coverage: 3:468/477 of query aligns to 12:483/490 of Q8RY79
- P92 (= P83) binding
- H193 (= H182) binding
- H308 (= H295) binding
- K309 (= K296) modified: N6-(pyridoxal phosphate)lysine
- F338 (≠ Y325) binding ; mutation to Y: Abolishes phenylacetaldehyde synthase activity.
6eeiB Crystal structure of arabidopsis thaliana phenylacetaldehyde synthase in complex with l-phenylalanine (see paper)
41% identity, 98% coverage: 3:468/477 of query aligns to 5:465/471 of 6eeiB
O82415 Tyrosine decarboxylase; PsTyDC; EC 4.1.1.25 from Papaver somniferum (Opium poppy) (see 3 papers)
38% identity, 99% coverage: 3:475/477 of query aligns to 20:512/512 of O82415
- P100 (= P83) binding
- S101 (≠ A84) mutation to A: No effect on catalytic activity.
- C170 (≠ S143) mutation to S: No effect on catalytic activity.
- H205 (= H182) binding ; mutation to N: Acquires the capacity to produce 4-hydroxyphenylacetaldehyde from L-tyrosine.
- N318 (= N293) mutation to S: No effect on catalytic activity.
- A319 (≠ P294) mutation to P: No effect on catalytic activity.
- H320 (= H295) binding
- K321 (= K296) modified: N6-(pyridoxal phosphate)lysine
- Y350 (= Y325) binding ; mutation to F: Acquires the capacity to produce 4-hydroxyphenylacetaldehyde from L-tyrosine.
6eemB Crystal structure of papaver somniferum tyrosine decarboxylase in complex with l-tyrosine (see paper)
38% identity, 99% coverage: 3:472/477 of query aligns to 4:486/488 of 6eemB
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)
39% identity, 97% coverage: 3:467/477 of query aligns to 20:494/514 of Q06086
- F346 (≠ Y325) mutation to Y: Abolishes 4-hydroxyphenylacetaldehyde synthase activity.
P14173 Aromatic-L-amino-acid decarboxylase; AADC; DOPA decarboxylase; DDC; EC 4.1.1.28 from Rattus norvegicus (Rat) (see 2 papers)
38% identity, 96% coverage: 3:462/477 of query aligns to 1:464/480 of P14173
- H192 (= H182) mutation to A: Abolishes decarboxylase activity.; mutation to Q: Reduces decarboxylase activity by 96%.
- D252 (= D245) mutation D->A,E: Abolishes decarboxylase activity.
- D271 (= D264) mutation to A: Abolishes decarboxylase activity.; mutation to E: Reduces decarboxylase activity by 65%.
- S296 (= S289) mutation to A: Abolishes decarboxylase activity.
- N300 (= N293) mutation to A: Reduces decarboxylase activity by 75%.
- H302 (= H295) mutation to Q: Reduces decarboxylase activity by 99.8%.
- K303 (= K296) mutation K->A,R: Abolishes decarboxylase activity.
- Y332 (= Y325) mutation Y->A,F: Abolishes decarboxylase activity.
- R355 (= R346) mutation to A: Abolishes decarboxylase activity.; mutation to K: No effect.
P20711 Aromatic-L-amino-acid decarboxylase; AADC; DOPA decarboxylase; DDC; EC 4.1.1.28 from Homo sapiens (Human) (see 8 papers)
39% identity, 97% coverage: 3:467/477 of query aligns to 1:469/480 of P20711
- M17 (= M19) to V: in dbSNP:rs6264
- E61 (≠ K63) to D: in dbSNP:rs11575292
- A148 (= A142) binding
- S149 (= S143) binding
- P210 (= P203) to L: in dbSNP:rs6262
- M217 (= M210) to V: in dbSNP:rs6263
- M239 (≠ V232) to I: in dbSNP:rs11575377; to L: in dbSNP:rs11575376
- T246 (= T239) binding
- N300 (= N293) binding
- K303 (= K296) modified: N6-(pyridoxal phosphate)lysine
- R462 (≠ L460) 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, 96% coverage: 3:462/477 of query aligns to 1:464/486 of P80041
- M1 (= M3) modified: N-acetylmethionine
- T82 (≠ A84) binding
- H192 (= H182) binding
- K303 (= K296) modified: N6-(pyridoxal phosphate)lysine
8oraA Human holo aromatic l-amino acid decarboxylase (aadc) external aldimine with l-dopa methylester (see paper)
38% identity, 97% coverage: 3:467/477 of query aligns to 1:469/480 of 8oraA
- binding pyridoxal-5'-phosphate: F80 (= F82), S147 (≠ T141), A148 (= A142), S149 (= S143), H192 (= H182), T246 (= T239), D271 (= D264), A273 (= A266), N300 (= N293), H302 (= H295), K303 (= K296)
- binding methyl (2~{R})-2-azanyl-3-[3,4-bis(oxidanyl)phenyl]propanoate: Y79 (= Y81), H192 (= H182), T246 (= T239), K303 (= K296)
1js3A Crystal structure of dopa decarboxylase in complex with the inhibitor carbidopa (see paper)
38% identity, 100% coverage: 3:477/477 of query aligns to 1:463/464 of 1js3A
- binding carbidopa: W71 (= W73), Y79 (= Y81), F80 (= F82), T82 (≠ A84), H192 (= H182), H302 (= H295), K303 (= K296)
- binding pyridoxal-5'-phosphate: S147 (≠ T141), A148 (= A142), S149 (= S143), H192 (= H182), D271 (= D264), A273 (= A266), N300 (= N293), H302 (= H295), K303 (= K296)
6eewA Crystal structure of catharanthus roseus tryptophan decarboxylase in complex with l-tryptophan (see paper)
36% identity, 97% coverage: 3:467/477 of query aligns to 4:473/479 of 6eewA
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)
36% identity, 97% coverage: 3:467/477 of query aligns to 22:491/500 of P17770
- P102 (= P83) binding
- H203 (= H182) binding
- H318 (= H295) binding
- K319 (= K296) modified: N6-(pyridoxal phosphate)lysine
- Y348 (= Y325) binding ; mutation to F: Acquires the capacity to produce indole-3-acetaldehyde from tryptophan.
- G370 (= G345) mutation to S: Acquires the capacity to produce dopamine from L-dopa and increased accumulation of phenylethylamine by gating indolic versus phenolic substrates.
P19113 Histidine decarboxylase; HDC; EC 4.1.1.22 from Homo sapiens (Human) (see 3 papers)
38% identity, 98% coverage: 2:467/477 of query aligns to 1:469/662 of P19113
- T31 (= T32) to M: in dbSNP:rs17740607
- E49 (= E50) to V: in a colorectal cancer sample; somatic mutation
- E285 (= E276) to K: in a colorectal cancer sample; somatic mutation; dbSNP:rs1353958864
- K305 (= K296) mutation to G: Loss of enzyme activity.
- Y334 (= Y325) mutation to F: Loss of enzyme activity.
- S354 (≠ G345) 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, 97% coverage: 3:467/477 of query aligns to 6:473/481 of 4e1oC
- binding pyridoxal-5'-phosphate: Y85 (≠ F82), T153 (= T141), V154 (≠ A142), S155 (= S143), H198 (= H182), T252 (= T239), D277 (= D264), A279 (= A266), K309 (= K296)
- binding histidine-methyl-ester: Y84 (= Y81), Y85 (≠ F82), L106 (≠ Q103), H198 (= H182), T252 (= T239), K309 (= K296), Y338 (= Y325)
7eiyA Human histidine decarboxylase mutant y334f soaking with histidine
38% identity, 97% coverage: 3:467/477 of query aligns to 1:460/467 of 7eiyA
- binding histidine: Y80 (≠ F82), H193 (= H182), T247 (= T239), K304 (= K296)
- binding pyridoxal-5'-phosphate: Y80 (≠ F82), T148 (= T141), V149 (≠ A142), S150 (= S143), H193 (= H182), T247 (= T239), D272 (= D264), A274 (= A266), K304 (= K296)
P05031 Aromatic-L-amino-acid decarboxylase; AADC; DOPA decarboxylase; DDC; EC 4.1.1.28 from Drosophila melanogaster (Fruit fly) (see 3 papers)
37% identity, 96% coverage: 3:462/477 of query aligns to 36:496/510 of P05031
- T117 (≠ A84) 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 (= A142) binding
- S184 (= S143) binding
- K197 (≠ S158) to N: in allele Ddc-R9
- H227 (= H182) 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 (≠ L223) to M: in allele Ddc-R11 and allele Ddc-R18
- D305 (= D264) binding
- N334 (= N293) binding
- 358:384 (vs. 317:343, 33% identical) Disordered
- R390 (= R349) to M: in allele Ddc-Ore
- S428 (≠ D387) to F: in allele Ddc-R33
- S489 (≠ Q455) 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
6khpA Crystal structure of oryza sativa tdc with plp and tryptamine (see paper)
34% identity, 97% coverage: 3:465/477 of query aligns to 5:481/490 of 6khpA
- binding pyridoxal-5'-phosphate: F84 (= F82), T150 (= T141), T151 (≠ A142), S152 (= S143), H190 (= H182), D274 (= D264), A276 (= A266), K306 (= K296), V356 (≠ L344), G357 (= G345)
- binding 2-(1h-indol-3-yl)ethanamine: V105 (≠ Q103), F107 (≠ M105), Y335 (= Y325)
6khnA Crystal structure of oryza sativa tdc with plp and serotonin (see paper)
34% identity, 97% coverage: 3:465/477 of query aligns to 5:481/490 of 6khnA
- binding pyridoxal-5'-phosphate: F84 (= F82), T150 (= T141), T151 (≠ A142), S152 (= S143), H190 (= H182), D274 (= D264), A276 (= A266), K306 (= K296), V356 (≠ L344), G357 (= G345)
- binding serotonin: F107 (≠ M105), Y335 (= Y325), G357 (= G345)
A0A2I6B3P0 4-hydroxyphenylacetaldehyde synthase; HPAA synthase; Rr4HPAAS; RrHPAAS; EC 4.1.1.108 from Rhodiola rosea (Roseroot) (Sedum rhodiola) (see paper)
34% identity, 99% coverage: 3:472/477 of query aligns to 17:488/490 of A0A2I6B3P0
- K314 (= K296) modified: N6-(pyridoxal phosphate)lysine
Query Sequence
>Echvi_1046 FitnessBrowser__Cola:Echvi_1046
MIMDKQEFRKRAHQVVDWMADYMEQKAHYRVTPEVQPGDIFGQLPNQAPEQPESFDDIFE
DFKEVILPGMTHWQHPAFFGYFPANNSEPSILAEMLMSTLGAQCMSWLTSPAATELEEKV
INWLRDAKGLDASWKGVIQDTASTATLCALLAARERASGFSINAEGFSGQENYRVYSSEH
AHSSVDKATRIAGLGLANLVKIPVDEDFKMLPEALEEAILADLENGFTPICVVSALGTTS
SGAIDPIEAIGKIAHRHSLWHHIDAAYAGTALLLPEFRWMIKGHELADSYVFNPHKWMFT
NFDCSVLFIKNAEAFIHTFSMTPEYLKTTQDDHVHNYRDWGIQLGRRFRALKLWMVIRSF
GLEGIREKLRHHLALTKMAKKRVEIEDNLIIEAPTDLNVICFRFVEKSLSTTVLNALNQA
WLQRVNQTGRVFFTHTVLDGKYVIRWVIGQTDVLQEHIDLAWTVLMEELEKVKAALL
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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