SitesBLAST
Comparing WP_086509677.1 NCBI__GCF_002151265.1:WP_086509677.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1gkmA Histidine ammonia-lyase (hal) from pseudomonas putida inhibited with l-cysteine (see paper)
39% identity, 89% coverage: 30:498/527 of query aligns to 25:494/507 of 1gkmA
- active site: Y53 (= Y58), G60 (= G65), H83 (= H88), N193 (= N197), Y278 (≠ L280), R281 (= R283), F327 (≠ P331), E412 (= E416)
- binding cysteine: G142 (≠ Y147), L189 (= L193), N193 (= N197), F327 (≠ P331)
P21310 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 4 papers)
39% identity, 89% coverage: 30:498/527 of query aligns to 26:497/510 of P21310
- S144 (vs. gap) 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
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
35% identity, 93% coverage: 8:496/527 of query aligns to 114:609/657 of P21213
- S254 (vs. gap) mutation to A: Complete loss of activity.
Q0VZ68 Tyrosine 2,3-aminomutase; Tyrosine ammonia-lyase; EC 5.4.3.6; EC 4.3.1.23 from Chondromyces crocatus (see paper)
33% identity, 92% coverage: 20:504/527 of query aligns to 13:519/531 of Q0VZ68
- F57 (≠ L64) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ LCNVAL 67:72) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ MSHA 86:89) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ MSHAC 86:90) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (= G188) mutation to R: Gain of aminomutase activity.
- K242 (= K246) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. 273:273, 7% identical) mutation Missing: Total loss of aminomutase activity.
- P377 (= P364) mutation to R: No effect.
- C396 (≠ S381) mutation to S: No effect.
- E399 (≠ M384) 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. 384:391, 38% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 412:418, 29% identical) mutation to SAGREDH: Total loss of aminomutase activity.; mutation to SANQEDH: Total loss of aminomutase activity.
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
34% identity, 91% coverage: 18:497/527 of query aligns to 140:626/677 of Q20502
- D536 (= D407) mutation to N: In am130; causes strong resistance to nickel and zinc toxicity.
2rjsA Sgtam bound to substrate mimic (see paper)
33% identity, 92% coverage: 18:503/527 of query aligns to 12:523/526 of 2rjsA
- active site: Y52 (= Y58), G59 (= G65), H82 (= H88), N192 (= N197), Y295 (≠ L280), R298 (= R283), F343 (≠ P331), Q429 (≠ E416)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y58), G59 (= G65), H82 (= H88), G141 (≠ Y147), L143 (= L148), N192 (= N197), Y295 (≠ L280), R298 (= R283), F343 (≠ P331), Q429 (≠ E416)
2rjrA Substrate mimic bound to sgtam (see paper)
33% identity, 92% coverage: 18:503/527 of query aligns to 12:523/526 of 2rjrA
- active site: Y52 (= Y58), G59 (= G65), H82 (= H88), N192 (= N197), Y295 (≠ L280), R298 (= R283), F343 (≠ P331), Q429 (≠ E416)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y58), G59 (= G65), H82 (= H88), G141 (≠ Y147), L143 (= L148), N192 (= N197), F343 (≠ P331), Q429 (≠ E416)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
33% identity, 92% coverage: 18:503/527 of query aligns to 12:523/526 of 2qveA
- active site: Y52 (= Y58), G59 (= G65), H82 (= H88), N192 (= N197), Y295 (≠ L280), R298 (= R283), F343 (≠ P331), Q429 (≠ E416)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y58), G59 (= G65), H82 (= H88), G141 (≠ Y147), L143 (= L148), N192 (= N197), Y295 (≠ L280), R298 (= R283), F343 (≠ P331), Q429 (≠ E416)
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)
33% identity, 92% coverage: 18:503/527 of query aligns to 23:536/539 of Q8GMG0
- Y63 (= Y58) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ A66) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H88) binding ; mutation to F: Complete loss of activity.
- A152 (≠ Y147) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (vs. gap) modified: 2,3-didehydroalanine (Ser)
- G154 (vs. gap) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N197) binding
- Y303 (≠ H275) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- R311 (= R283) binding
- Y415 (= Y388) mutation to V: Complete loss of activity.
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
33% identity, 92% coverage: 18:503/527 of query aligns to 13:524/527 of 3kdzA
- active site: F53 (≠ Y58), G60 (= G65), H83 (= H88), N193 (= N197), Y296 (≠ L280), R299 (= R283), F344 (≠ P331), Q430 (≠ E416)
- binding tyrosine: F53 (≠ Y58), Y59 (≠ L64), G60 (= G65), H83 (= H88), G142 (≠ Y147), N193 (= N197), Y296 (≠ L280), R299 (= R283), F344 (≠ P331)
6s7qA Crystal structure of ergothioneine degrading enzyme ergothionase from treponema denticola in complex with desmethyl-ergothioneine sulfonic acid (see paper)
31% identity, 93% coverage: 8:495/527 of query aligns to 3:490/497 of 6s7qA
- active site: Y53 (= Y58), G60 (= G65), D275 (= D278), A324 (= A329)
- binding (2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic acid: Y53 (= Y58), V59 (≠ L64), G60 (= G65), S194 (≠ N197), F326 (≠ P331), T380 (≠ M384), K383 (≠ Y388), E411 (= E416)
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
28% identity, 90% coverage: 15:489/527 of query aligns to 10:502/514 of 3unvA
- active site: Y53 (= Y58), G60 (= G65), V83 (≠ H88), L191 (= L195), D291 (= D278), S294 (= S281), G340 (≠ A329), D427 (≠ L414)
- binding phenylalanine: Y53 (= Y58), G60 (= G65), G142 (vs. gap), L144 (= L148), N326 (= N313), F342 (≠ P331)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y58), G60 (= G65), G142 (vs. gap), N193 (= N197), N326 (= N313), F342 (≠ P331)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
33% identity, 92% coverage: 15:497/527 of query aligns to 11:513/515 of 2o7eA
- active site: Y54 (= Y58), G61 (= G65), L84 (≠ H88), N195 (= N197), Y292 (≠ L280), R295 (= R283), F342 (≠ P331), Q428 (≠ E416)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y58), G143 (≠ Y147), L145 (= L148), N195 (= N197), Y292 (≠ L280), R295 (= R283), N325 (= N313), F342 (≠ P331)
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
33% identity, 92% coverage: 15:497/527 of query aligns to 11:513/515 of 2o7dA
- active site: Y54 (= Y58), G61 (= G65), L84 (≠ H88), N195 (= N197), Y292 (≠ L280), R295 (= R283), F342 (≠ P331), Q428 (≠ E416)
- binding caffeic acid: G61 (= G65), H83 (≠ S87), L84 (≠ H88), Y292 (≠ L280), R295 (= R283), N424 (≠ S412), N427 (≠ Q415), Q428 (≠ E416)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
30% identity, 90% coverage: 3:474/527 of query aligns to 21:519/567 of Q3M5Z3
- L108 (≠ H88) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (≠ Y147) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (vs. gap) modified: 2,3-didehydroalanine (Ser)
- G169 (vs. gap) modified: Crosslink with 167, 5-imidazolinone (Ala-Gly)
- C503 (vs. gap) mutation to S: Prevents formation of artifactual disulfide bonds and increases solubility; when associated with S-565.
Sites not aligning to the query:
- 1:21 mutation Missing: No effect on enzyme activity.
- 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)
30% identity, 89% coverage: 7:474/527 of query aligns to 1:493/537 of 5ltmB
- active site: F54 (≠ Y58), G61 (= G65), L84 (≠ H88), N197 (= N197), Y288 (≠ L280), R291 (= R283), F337 (≠ P331), Q426 (≠ E416)
- binding hydrocinnamic acid: F60 (≠ L64), A143 (≠ Y147), L145 (= L148), Y288 (≠ L280), R291 (= R283)
B2J528 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
29% identity, 85% coverage: 8:453/527 of query aligns to 26:489/569 of B2J528
- A167 (≠ Y147) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (vs. gap) modified: 2,3-didehydroalanine (Ser)
- G169 (vs. gap) 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)
29% identity, 84% coverage: 9:453/527 of query aligns to 29:496/687 of Q68G84
- Y80 (= Y58) active site, Proton donor/acceptor; mutation Y->A,F: Abolishes enzyme activity.
- A175 (vs. gap) modified: Crosslink with 177, 5-imidazolinone (Ala-Gly)
- S176 (vs. gap) modified: 2,3-didehydroalanine (Ser)
- G177 (= G146) modified: Crosslink with 175, 5-imidazolinone (Ala-Gly)
- N231 (= N197) 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 (= Q277) 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 (≠ L280) 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 (= R283) 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 (= N313) binding ; mutation to X: Abolishes enzyme activity; when associated with X-231.
- F371 (≠ P331) mutation to X: Abolishes enzyme activity; when associated with X-322.
- N458 (≠ Q415) binding
4c5sC Structural investigations into the stereochemistry and activity of a phenylalanine-2,3-aminomutase from taxus chinensis (see paper)
28% identity, 84% coverage: 11:453/527 of query aligns to 23:478/642 of 4c5sC
- active site: A71 (≠ Y58), G78 (= G65), L99 (≠ H88), N213 (= N197), Y304 (≠ L280), R307 (= R283), F353 (≠ P331), Q441 (≠ E416)
- binding (3S)-3-amino-2,2-difluoro-3-phenylpropanoic acid: G78 (= G65), G159 (= G146), L161 (= L148), N213 (= N197), Y304 (≠ L280), R307 (= R283), N337 (= N313), F353 (≠ P331), E437 (≠ S412)
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, 84% coverage: 9:453/527 of query aligns to 29:496/698 of Q6GZ04
- Y80 (= Y58) mutation to F: Abolishes enzyme activity.
- L104 (≠ S81) mutation to A: Decreases enzyme activity.
- Q319 (= Q277) binding
- R325 (= R283) binding
Query Sequence
>WP_086509677.1 NCBI__GCF_002151265.1:WP_086509677.1
MSDHAERIVLGAAPVEWQQVVRVARHGALLSLTKAAWKRIAAARQAVEKIAASTVPHYGI
NTGLGALCNVALERDELQRLSHHTLMSHACGVGAPLRTEQVRAIICCAVINYSHGYSGIS
PAVVKGLLHLLNEQVTPIVPSRGSVGYLTHMAHIGLALIGHGEVEFDGQRMPARQALDAI
GMPPLTLGPKDGLSLVNGTPAMTGLACLALEDVARLAAWADIVGAMSFEALGGQWDALLP
QVTSLKRHQGVQHTGDNLRRLLQGSRRLARCQGQHLQDALSLRSIPQVHGACRDQFAHAA
RQIDHELDSATDNPLVVATEESYRIISNANPHGASVAMACDLLAIAVCEWSSISERRTYR
LVTPQASRLPPFLSNDVGVKSGMMIAQYTAASLVADNKRLAQPAVVDNFLTSGLQEDHLS
LGESAALKLDQALDNAFQVLAIEYLLAAQAFDLIDDQNFAPGTELAWKALREVIPFYDEE
HPLHQDLQTARHLLRDTSRQADFVKLAPHLHPGMSQTCLISASIPAA
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