SitesBLAST
Comparing N515DRAFT_2941 FitnessBrowser__Dyella79:N515DRAFT_2941 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)
37% identity, 84% coverage: 6:531/629 of query aligns to 114:566/657 of P21213
- S254 (= S163) 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)
36% identity, 92% coverage: 3:582/629 of query aligns to 1:495/510 of P21310
- M1 (≠ V3) modified: Initiator methionine, Removed
- S144 (= S163) modified: 2,3-didehydroalanine (Ser); mutation S->A,T: Complete loss of activity.; mutation to C: No effect.
1gkmA Histidine ammonia-lyase (hal) from pseudomonas putida inhibited with l-cysteine (see paper)
35% identity, 92% coverage: 5:582/629 of query aligns to 2:492/507 of 1gkmA
- active site: Y53 (= Y56), G60 (= G63), H83 (= H103), N193 (= N215), Y278 (= Y351), R281 (= R354), F327 (= F407), E412 (= E494)
- binding cysteine: G142 (= G164), L189 (= L211), N193 (= N215), F327 (= F407)
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
32% identity, 83% coverage: 10:532/629 of query aligns to 7:467/514 of 3unvA
- active site: Y53 (= Y56), G60 (= G63), V83 (≠ H103), L191 (= L213), D291 (= D349), S294 (≠ C352), G340 (= G405), D427 (≠ N492)
- binding phenylalanine: Y53 (= Y56), G60 (= G63), G142 (= G164), L144 (= L166), N326 (= N384), F342 (= F407)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y56), G60 (= G63), G142 (= G164), N193 (= N215), N326 (= N384), F342 (= F407)
Q0VZ68 Tyrosine 2,3-aminomutase; Tyrosine ammonia-lyase; EC 5.4.3.6; EC 4.3.1.23 from Chondromyces crocatus (see paper)
34% identity, 83% coverage: 6:528/629 of query aligns to 1:465/531 of Q0VZ68
- F57 (= F62) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ NADKLL 65:70) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ TTHA 101:104) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ TTHAV 101:105) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ S206) mutation to R: Gain of aminomutase activity.
- K242 (≠ R264) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. 311:324, 21% identical) mutation Missing: Total loss of aminomutase activity.
- P377 (= P440) mutation to R: No effect.
- C396 (≠ S459) mutation to S: No effect.
- E399 (≠ M462) 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. 462:469, 38% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 490:496, 14% identical) mutation to SAGREDH: Total loss of aminomutase activity.; mutation to SANQEDH: Total loss of aminomutase activity.
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)
34% identity, 84% coverage: 6:531/629 of query aligns to 13:479/539 of Q8GMG0
- Y63 (= Y56) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (= E78) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H103) binding ; mutation to F: Complete loss of activity.
- A152 (= A162) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S163) modified: 2,3-didehydroalanine (Ser)
- G154 (= G164) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N215) binding
- Y303 (≠ F332) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- R311 (= R354) binding
- Y415 (= Y466) mutation to V: Complete loss of activity.
2rjsA Sgtam bound to substrate mimic (see paper)
34% identity, 84% coverage: 6:531/629 of query aligns to 2:466/526 of 2rjsA
- active site: Y52 (= Y56), G59 (= G63), H82 (= H103), N192 (= N215), Y295 (= Y351), R298 (= R354), F343 (= F407), Q429 (≠ E494)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y56), G59 (= G63), H82 (= H103), G141 (= G164), L143 (= L166), N192 (= N215), Y295 (= Y351), R298 (= R354), F343 (= F407), Q429 (≠ E494)
2rjrA Substrate mimic bound to sgtam (see paper)
34% identity, 84% coverage: 6:531/629 of query aligns to 2:466/526 of 2rjrA
- active site: Y52 (= Y56), G59 (= G63), H82 (= H103), N192 (= N215), Y295 (= Y351), R298 (= R354), F343 (= F407), Q429 (≠ E494)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y56), G59 (= G63), H82 (= H103), G141 (= G164), L143 (= L166), N192 (= N215), F343 (= F407), Q429 (≠ E494)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
34% identity, 84% coverage: 6:531/629 of query aligns to 2:466/526 of 2qveA
- active site: Y52 (= Y56), G59 (= G63), H82 (= H103), N192 (= N215), Y295 (= Y351), R298 (= R354), F343 (= F407), Q429 (≠ E494)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y56), G59 (= G63), H82 (= H103), G141 (= G164), L143 (= L166), N192 (= N215), Y295 (= Y351), R298 (= R354), F343 (= F407), Q429 (≠ E494)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
34% identity, 84% coverage: 6:531/629 of query aligns to 3:467/527 of 3kdzA
- active site: F53 (≠ Y56), G60 (= G63), H83 (= H103), N193 (= N215), Y296 (= Y351), R299 (= R354), F344 (= F407), Q430 (≠ E494)
- binding tyrosine: F53 (≠ Y56), Y59 (≠ F62), G60 (= G63), H83 (= H103), G142 (= G164), N193 (= N215), Y296 (= Y351), R299 (= R354), F344 (= F407)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
34% identity, 76% coverage: 56:532/629 of query aligns to 54:466/515 of 2o7eA
- active site: Y54 (= Y56), G61 (= G63), L84 (≠ H103), N195 (= N215), Y292 (= Y351), R295 (= R354), F342 (= F407), Q428 (≠ E494)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y56), G143 (= G164), L145 (= L166), N195 (= N215), Y292 (= Y351), R295 (= R354), N325 (= N384), F342 (= F407)
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
34% identity, 76% coverage: 56:532/629 of query aligns to 54:466/515 of 2o7dA
- active site: Y54 (= Y56), G61 (= G63), L84 (≠ H103), N195 (= N215), Y292 (= Y351), R295 (= R354), F342 (= F407), Q428 (≠ E494)
- binding caffeic acid: G61 (= G63), H83 (≠ T102), L84 (≠ H103), Y292 (= Y351), R295 (= R354), N424 (≠ S490), N427 (≠ A493), Q428 (≠ E494)
B2J528 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
30% identity, 83% coverage: 12:532/629 of query aligns to 32:490/569 of B2J528
- A167 (= A162) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S163) modified: 2,3-didehydroalanine (Ser)
- G169 (= G164) modified: Crosslink with 167, 5-imidazolinone (Ala-Gly)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
28% identity, 84% coverage: 2:532/629 of query aligns to 22:490/567 of Q3M5Z3
- L108 (≠ H103) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (= A162) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S163) modified: 2,3-didehydroalanine (Ser)
- G169 (= G164) 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.
P11544 Phenylalanine/tyrosine ammonia-lyase; Bifunctional phenylalanine ammonia-lyase; Bifunctional PAL; EC 4.3.1.25 from Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides) (see paper)
29% identity, 84% coverage: 6:532/629 of query aligns to 60:538/716 of P11544
- A211 (= A162) modified: Crosslink with 213, 5-imidazolinone (Ala-Gly)
- S212 (= S163) modified: 2,3-didehydroalanine (Ser)
- G213 (= G164) modified: Crosslink with 211, 5-imidazolinone (Ala-Gly)
- K468 (≠ M462) binding
- E496 (≠ S490) binding
P0DO55 Phenylalanine/tyrosine ammonia-lyase 1; FuPAL1; EC 4.3.1.25 from Fritillaria unibracteata (Sichuan fritillary) (see paper)
27% identity, 90% coverage: 6:570/629 of query aligns to 63:568/722 of P0DO55
- F141 (≠ N98) mutation to H: Increased activity toward L-tyrosine (L-Tyr) but reduced ability to use L-phenylalanine (L-Phe) as substrate.
- S208 (≠ A162) mutation to A: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- I218 (≠ L172) mutation to P: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- E490 (≠ S490) mutation to N: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
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)
29% identity, 84% coverage: 3:533/629 of query aligns to 24:498/687 of Q68G84
- Y80 (= Y56) active site, Proton donor/acceptor; mutation Y->A,F: Abolishes enzyme activity.
- A175 (= A162) modified: Crosslink with 177, 5-imidazolinone (Ala-Gly)
- S176 (= S163) modified: 2,3-didehydroalanine (Ser)
- G177 (= G164) modified: Crosslink with 175, 5-imidazolinone (Ala-Gly)
- N231 (= N215) 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 (= Q348) 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 (= Y351) 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 (= R354) 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 (= N384) binding ; mutation to X: Abolishes enzyme activity; when associated with X-231.
- F371 (= F407) mutation to X: Abolishes enzyme activity; when associated with X-322.
- N458 (≠ A493) 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)
29% identity, 84% coverage: 3:533/629 of query aligns to 24:498/698 of Q6GZ04
- Y80 (= Y56) mutation to F: Abolishes enzyme activity.
- L104 (= L99) mutation to A: Decreases enzyme activity.
- Q319 (= Q348) binding
- R325 (= R354) binding
5ltmB Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis (y78f-c503s-c565s) bound to cinnamate (see paper)
28% identity, 83% coverage: 13:532/629 of query aligns to 9:464/537 of 5ltmB
- active site: F54 (≠ Y56), G61 (= G63), L84 (≠ H103), N197 (= N215), Y288 (= Y351), R291 (= R354), F337 (= F407), Q426 (≠ T489)
- binding hydrocinnamic acid: F60 (= F62), A143 (= A162), L145 (= L166), Y288 (= Y351), R291 (= R354)
4c5sC Structural investigations into the stereochemistry and activity of a phenylalanine-2,3-aminomutase from taxus chinensis (see paper)
29% identity, 84% coverage: 3:533/629 of query aligns to 16:480/642 of 4c5sC
- active site: A71 (≠ Y56), G78 (= G63), L99 (≠ H103), N213 (= N215), Y304 (= Y351), R307 (= R354), F353 (= F407), Q441 (≠ E494)
- binding (3S)-3-amino-2,2-difluoro-3-phenylpropanoic acid: G78 (= G63), G159 (= G164), L161 (= L166), N213 (= N215), Y304 (= Y351), R307 (= R354), N337 (= N384), F353 (= F407), E437 (≠ S490)
Query Sequence
>N515DRAFT_2941 FitnessBrowser__Dyella79:N515DRAFT_2941
MSVEQIRLDGSSLTRAQLVAAARQRVPVALDEAQLARVQRAADFLADKVSCGEPTYGVTT
GFGSNADKLLGAHRLRDELPGGHPEKPEGTLLEELQHNLITTHAVCVGKPFAEDVVRAML
VIRINTLMRGHSGIRVATLRALAALLNSGVVPVVPEKGSVGASGDLAPLSHLAIVLLGGG
EAFYQGERLPGAEALERVGLAPIRLSFKEGLALNNGTAQMLATAALALDTLEYLLDTADL
AAAMTLDAFAGRSGALRPEVHALRPHPGQVETAGHVRDLLTESTLVDIPYHLVPRFKQWA
ADAWTAPEDQALSFDIGWDWVPANQRHGREAFYSRFLPFKGGKKHQPQDAYCLRCMPQVH
GAVRDAWAQACRVIDIELNAVTDNPLIFPDAEGAQFIEEQVISAGHFHGMPLALAMSYVK
AAIPVLASISERRLNKLVDPATNDGLPAFLTGNEDGTDSGFMIVQYTAAALVNDLATRAH
PASVYSVPTSANAEDHVSMGANEARHVLEMLDDLSHVIALELYTAAQALDFRQAMLNAAR
RLAARGDWKALAAKVSNAPREDHAHYAQFAAEVQQLTLALAEVGDFHAGEAVRKAHDVLR
GHIGFMSRDRAMDGDVRTVCELVQRRAVG
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