SitesBLAST
Comparing Echvi_0202 FitnessBrowser__Cola:Echvi_0202 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)
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
44% identity, 93% coverage: 32:505/508 of query aligns to 135:614/657 of P21213
- S254 (= S153) mutation to A: Complete loss of activity.
P21310 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 4 papers)
41% identity, 96% coverage: 18:503/508 of query aligns to 11:498/510 of P21310
- S144 (= S153) modified: 2,3-didehydroalanine (Ser); mutation S->A,T: Complete loss of activity.; mutation to C: No effect.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1gkmA Histidine ammonia-lyase (hal) from pseudomonas putida inhibited with l-cysteine (see paper)
40% identity, 96% coverage: 18:503/508 of query aligns to 10:495/507 of 1gkmA
- active site: Y53 (= Y63), G60 (= G70), H83 (= H93), N193 (= N205), Y278 (= Y287), R281 (= R290), F327 (= F336), E412 (= E420)
- binding cysteine: G142 (= G154), L189 (= L201), N193 (= N205), F327 (= F336)
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
41% identity, 93% coverage: 33:505/508 of query aligns to 152:630/677 of Q20502
- D536 (= D411) mutation to N: In am130; causes strong resistance to nickel and zinc toxicity.
Q8GMG0 MIO-dependent tyrosine 2,3-aminomutase; Tyrosine ammonia-lyase; EC 5.4.3.6; EC 4.3.1.23 from Streptomyces globisporus (see 3 papers)
37% identity, 95% coverage: 18:499/508 of query aligns to 20:528/539 of Q8GMG0
- Y63 (= Y63) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ Y71) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H93) binding ; mutation to F: Complete loss of activity.
- A152 (= A152) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S153) modified: 2,3-didehydroalanine (Ser)
- G154 (= G154) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N205) binding
- Y303 (≠ Q282) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- R311 (= R290) binding
- Y415 (= Y392) mutation to V: Complete loss of activity.
2rjsA Sgtam bound to substrate mimic (see paper)
37% identity, 95% coverage: 18:499/508 of query aligns to 9:515/526 of 2rjsA
- active site: Y52 (= Y63), G59 (= G70), H82 (= H93), N192 (= N205), Y295 (= Y287), R298 (= R290), F343 (= F336), Q429 (≠ E420)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y63), G59 (= G70), H82 (= H93), G141 (= G154), L143 (= L156), N192 (= N205), Y295 (= Y287), R298 (= R290), F343 (= F336), Q429 (≠ E420)
2rjrA Substrate mimic bound to sgtam (see paper)
37% identity, 95% coverage: 18:499/508 of query aligns to 9:515/526 of 2rjrA
- active site: Y52 (= Y63), G59 (= G70), H82 (= H93), N192 (= N205), Y295 (= Y287), R298 (= R290), F343 (= F336), Q429 (≠ E420)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y63), G59 (= G70), H82 (= H93), G141 (= G154), L143 (= L156), N192 (= N205), F343 (= F336), Q429 (≠ E420)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
37% identity, 95% coverage: 18:499/508 of query aligns to 9:515/526 of 2qveA
- active site: Y52 (= Y63), G59 (= G70), H82 (= H93), N192 (= N205), Y295 (= Y287), R298 (= R290), F343 (= F336), Q429 (≠ E420)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y63), G59 (= G70), H82 (= H93), G141 (= G154), L143 (= L156), N192 (= N205), Y295 (= Y287), R298 (= R290), F343 (= F336), Q429 (≠ E420)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
37% identity, 95% coverage: 18:499/508 of query aligns to 10:516/527 of 3kdzA
- active site: F53 (≠ Y63), G60 (= G70), H83 (= H93), N193 (= N205), Y296 (= Y287), R299 (= R290), F344 (= F336), Q430 (≠ E420)
- binding tyrosine: F53 (≠ Y63), Y59 (≠ F69), G60 (= G70), H83 (= H93), G142 (= G154), N193 (= N205), Y296 (= Y287), R299 (= R290), F344 (= F336)
Q0VZ68 Tyrosine 2,3-aminomutase; Tyrosine ammonia-lyase; EC 5.4.3.6; EC 4.3.1.23 from Chondromyces crocatus (see paper)
38% identity, 87% coverage: 33:472/508 of query aligns to 23:483/531 of Q0VZ68
- F57 (= F69) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ LQQVRI 72:77) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ QSHA 91:94) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ QSHAC 91:95) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ R196) mutation to R: Gain of aminomutase activity.
- K242 (≠ R254) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. gap) mutation Missing: Total loss of aminomutase activity.
- P377 (vs. gap) mutation to R: No effect.
- C396 (≠ I389) mutation to S: No effect.
- E399 (vs. gap) mutation to A: Loss of aminomutase activity and increased product racemization. Gain of ammonia-lyase activity.; mutation to K: Loss of aminomutase and ammonia-lyase activity. Higher enantiomeric excess of (R)-beta-tyrosine.; mutation to M: Loss of aminomutase and ammonia-lyase activity.
- 399:406 (vs. 390:395, 38% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 416:422, 14% identical) mutation to SAGREDH: Total loss of aminomutase activity.; mutation to SANQEDH: Total loss of aminomutase activity.
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
32% identity, 93% coverage: 18:488/508 of query aligns to 10:497/514 of 3unvA
- active site: Y53 (= Y62), G60 (= G70), V83 (≠ H93), L191 (= L203), D291 (= D285), S294 (= S288), G340 (= G334), D427 (≠ G418)
- binding phenylalanine: Y53 (= Y62), G60 (= G70), G142 (= G154), L144 (= L156), N326 (= N320), F342 (= F336)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y62), G60 (= G70), G142 (= G154), N193 (= N205), N326 (= N320), F342 (= F336)
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
35% identity, 87% coverage: 18:458/508 of query aligns to 11:466/515 of 2o7dA
- active site: Y54 (= Y63), G61 (= G70), L84 (≠ H93), N195 (= N205), Y292 (= Y287), R295 (= R290), F342 (= F336), Q428 (≠ E420)
- binding caffeic acid: G61 (= G70), H83 (≠ S92), L84 (≠ H93), Y292 (= Y287), R295 (= R290), N424 (≠ S416), N427 (≠ Q419), Q428 (≠ E420)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
35% identity, 87% coverage: 18:458/508 of query aligns to 11:466/515 of 2o7eA
- active site: Y54 (= Y63), G61 (= G70), L84 (≠ H93), N195 (= N205), Y292 (= Y287), R295 (= R290), F342 (= F336), Q428 (≠ E420)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y63), G143 (= G154), L145 (= L156), N195 (= N205), Y292 (= Y287), R295 (= R290), N325 (= N320), F342 (= F336)
6s7qA Crystal structure of ergothioneine degrading enzyme ergothionase from treponema denticola in complex with desmethyl-ergothioneine sulfonic acid (see paper)
29% identity, 96% coverage: 17:503/508 of query aligns to 9:494/497 of 6s7qA
- active site: Y53 (= Y63), G60 (= G70), D275 (= D285), A324 (≠ G334)
- binding (2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic acid: Y53 (= Y63), V59 (≠ F69), G60 (= G70), S194 (≠ N205), F326 (= F336), T380 (≠ I389), K383 (≠ Y392), E411 (= E420)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
29% identity, 88% coverage: 13:458/508 of query aligns to 28:490/567 of Q3M5Z3
- L108 (≠ H93) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (= A152) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S153) modified: 2,3-didehydroalanine (Ser)
- G169 (= G154) modified: Crosslink with 167, 5-imidazolinone (Ala-Gly)
Sites not aligning to the query:
- 1:21 mutation Missing: No effect on enzyme activity.
- 503 C→S: Prevents formation of artifactual disulfide bonds and increases solubility; when associated with S-565.
- 565 C→S: Prevents formation of artifactual disulfide bonds and increases solubility; when associated with S-503.
5ltmB Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis (y78f-c503s-c565s) bound to cinnamate (see paper)
29% identity, 88% coverage: 13:458/508 of query aligns to 4:464/537 of 5ltmB
- active site: F54 (≠ Y63), G61 (= G70), L84 (≠ H93), N197 (= N205), Y288 (= Y287), R291 (= R290), F337 (= F336), Q426 (≠ E420)
- binding hydrocinnamic acid: F60 (= F69), A143 (= A152), L145 (= L156), Y288 (= Y287), R291 (= R290)
B2J528 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
29% identity, 88% coverage: 13:458/508 of query aligns to 28:490/569 of B2J528
- A167 (= A152) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S153) modified: 2,3-didehydroalanine (Ser)
- G169 (= G154) modified: Crosslink with 167, 5-imidazolinone (Ala-Gly)
Q68G84 Phenylalanine aminomutase (L-beta-phenylalanine forming); Phenylalanine ammonia-lyase; EC 5.4.3.10; EC 4.3.1.24 from Taxus chinensis (Chinese yew) (Taxus wallichiana var. chinensis) (see 2 papers)
28% identity, 90% coverage: 42:498/508 of query aligns to 61:531/687 of Q68G84
- Y80 (= Y63) active site, Proton donor/acceptor; mutation Y->A,F: Abolishes enzyme activity.
- A175 (= A152) modified: Crosslink with 177, 5-imidazolinone (Ala-Gly)
- S176 (= S153) modified: 2,3-didehydroalanine (Ser)
- G177 (= G154) modified: Crosslink with 175, 5-imidazolinone (Ala-Gly)
- N231 (= N205) binding ; mutation to A: Abolishes the formation of the MIO cofactor and thereby abolishes enzyme activity.; mutation to X: Abolishes enzyme activity; when associated with X-355.
- Q319 (= Q284) binding ; mutation to M: Increases deamination activity with beta-Phe. Increases beta-regioselectivity in the amination of cinnamate. Abolishes enzyme activity; when associated with K-325.
- Y322 (= Y287) mutation to A: Abolishes the formation of the MIO cofactor and thereby abolishes enzyme activity.; mutation to X: Abolishes enzyme activity; when associated with X-371.
- R325 (= R290) binding ; mutation to K: Increases deamination activity with beta-Phe. Increases beta-regioselectivity in the amination of cinnamate. Abolishes enzyme activity; when associated with M-319.
- N355 (= N320) binding ; mutation to X: Abolishes enzyme activity; when associated with X-231.
- F371 (= F336) mutation to X: Abolishes enzyme activity; when associated with X-322.
- N458 (≠ Q419) binding
P11544 Phenylalanine/tyrosine ammonia-lyase; Bifunctional phenylalanine ammonia-lyase; Bifunctional PAL; EC 4.3.1.25 from Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides) (see paper)
30% identity, 78% coverage: 63:458/508 of query aligns to 110:538/716 of P11544
- A211 (= A152) modified: Crosslink with 213, 5-imidazolinone (Ala-Gly)
- S212 (= S153) modified: 2,3-didehydroalanine (Ser)
- G213 (= G154) modified: Crosslink with 211, 5-imidazolinone (Ala-Gly)
- K468 (≠ M388) binding
- E496 (≠ S416) binding
Q6GZ04 Phenylalanine aminomutase (L-beta-phenylalanine forming); Phenylalanine ammonia-lyase; EC 5.4.3.10; EC 4.3.1.24 from Taxus canadensis (Canadian yew) (see paper)
28% identity, 90% coverage: 42:498/508 of query aligns to 61:531/698 of Q6GZ04
- Y80 (= Y63) mutation to F: Abolishes enzyme activity.
- L104 (= L89) mutation to A: Decreases enzyme activity.
- Q319 (= Q284) binding
- R325 (= R290) binding
Query Sequence
>Echvi_0202 FitnessBrowser__Cola:Echvi_0202
MIEVLEKQEAYRVGEMPVTLERIYRVVSEGKRLELSSAAIERIQQCRAYLDDKIYKDEAA
LYYGINTGFGYLQQVRIDRNEIQQLQYNLLQSHACGVGEKVPKELVRLMLLTKIESLSRG
HSGVQLETVQRLVDFYNHDVLPVVYNQGSLGASGDLSPLSHLSLPLIGMGEVYFEGKVCP
SAQVLEQFGWQPVTLRSKEGLSLINGTQFMLSYGVHITQRAEALFRWADLIAAISVDGFN
GNLQPFNALIHRIRAHEGQVDTAASLRHYLEGSEIAQSKEKQVQDPYSFRCIPQVHGASK
DTLAFVKGTFEREADSVTDNPNIFPDEDEILSGGNFHGQPLALAFDYLAIAMAEIGSISE
RRTYQLLSGQRGLPLFLVDDPGLHSGLMIPQYTAASVVSENKQLCTPASVDSIVSSNGQE
DHVSMGANGATKCLRVLDNLEKILAIELLTAAQALEFRRPARSSEIVERLIGVYRDHVSF
NAQDRVLSVDIKNTIKFLRDRSVEEFEK
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