SitesBLAST
Comparing SMc00669 FitnessBrowser__Smeli:SMc00669 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, 98% coverage: 3:490/499 of query aligns to 112:607/657 of P21213
- S254 (vs. gap) 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)
37% identity, 98% coverage: 1:490/499 of query aligns to 1:493/510 of P21310
- M1 (= M1) modified: Initiator methionine, Removed
- S144 (vs. gap) 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)
38% identity, 90% coverage: 42:490/499 of query aligns to 42:490/507 of 1gkmA
- active site: Y53 (= Y53), G60 (= G60), H83 (= H83), N193 (= N192), Y278 (≠ L275), R281 (= R278), F327 (≠ A326), E412 (= E411)
- binding cysteine: G142 (vs. gap), L189 (= L188), N193 (= N192), F327 (≠ A326)
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
37% identity, 94% coverage: 23:491/499 of query aligns to 150:624/677 of Q20502
- D536 (= D402) mutation to N: In am130; causes strong resistance to nickel and zinc toxicity.
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, 96% coverage: 11:487/499 of query aligns to 8:506/531 of Q0VZ68
- F57 (≠ V59) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ LCDVII 62:67) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ LSHA 81:84) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ LSHAC 81:85) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ E183) mutation to R: Gain of aminomutase activity.
- K242 (≠ R241) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. 266:268, 7% identical) mutation Missing: Total loss of aminomutase activity.
- P377 (= P359) mutation to R: No effect.
- C396 (≠ S376) mutation to S: No effect.
- E399 (≠ M379) 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. 379:386, 38% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 407:413, 14% identical) mutation to SAGREDH: Total loss of aminomutase activity.; mutation to SANQEDH: Total loss of aminomutase activity.
2rjsA Sgtam bound to substrate mimic (see paper)
34% identity, 96% coverage: 5:484/499 of query aligns to 2:502/526 of 2rjsA
- active site: Y52 (= Y53), G59 (= G60), H82 (= H83), N192 (= N192), Y295 (≠ L275), R298 (= R278), F343 (≠ A326), Q429 (≠ E411)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y53), G59 (= G60), H82 (= H83), G141 (vs. gap), L143 (vs. gap), N192 (= N192), Y295 (≠ L275), R298 (= R278), F343 (≠ A326), Q429 (≠ E411)
2rjrA Substrate mimic bound to sgtam (see paper)
34% identity, 96% coverage: 5:484/499 of query aligns to 2:502/526 of 2rjrA
- active site: Y52 (= Y53), G59 (= G60), H82 (= H83), N192 (= N192), Y295 (≠ L275), R298 (= R278), F343 (≠ A326), Q429 (≠ E411)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y53), G59 (= G60), H82 (= H83), G141 (vs. gap), L143 (vs. gap), N192 (= N192), F343 (≠ A326), Q429 (≠ E411)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
34% identity, 96% coverage: 5:484/499 of query aligns to 2:502/526 of 2qveA
- active site: Y52 (= Y53), G59 (= G60), H82 (= H83), N192 (= N192), Y295 (≠ L275), R298 (= R278), F343 (≠ A326), Q429 (≠ E411)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y53), G59 (= G60), H82 (= H83), G141 (vs. gap), L143 (vs. gap), N192 (= N192), Y295 (≠ L275), R298 (= R278), F343 (≠ A326), Q429 (≠ E411)
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, 96% coverage: 5:484/499 of query aligns to 13:515/539 of Q8GMG0
- Y63 (= Y53) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ A61) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H83) binding ; mutation to F: Complete loss of activity.
- A152 (≠ Y142) 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 (= N192) binding
- Y303 (vs. gap) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- R311 (= R278) binding
- Y415 (= Y383) mutation to V: Complete loss of activity.
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
31% identity, 90% coverage: 34:481/499 of query aligns to 34:498/514 of 3unvA
- active site: Y53 (= Y53), G60 (= G60), V83 (≠ H83), L191 (= L190), D291 (= D273), S294 (= S276), G340 (≠ A324), D427 (≠ L409)
- binding phenylalanine: Y53 (= Y53), G60 (= G60), G142 (vs. gap), L144 (= L143), N326 (= N308), F342 (≠ A326)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y53), G60 (= G60), G142 (vs. gap), N193 (= N192), N326 (= N308), F342 (≠ A326)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
34% identity, 96% coverage: 5:484/499 of query aligns to 3:503/527 of 3kdzA
- active site: F53 (≠ Y53), G60 (= G60), H83 (= H83), N193 (= N192), Y296 (≠ L275), R299 (= R278), F344 (≠ A326), Q430 (≠ E411)
- binding tyrosine: F53 (≠ Y53), Y59 (≠ V59), G60 (= G60), H83 (= H83), G142 (vs. gap), N193 (= N192), Y296 (≠ L275), R299 (= R278), F344 (≠ A326)
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
36% identity, 93% coverage: 22:483/499 of query aligns to 23:502/515 of 2o7dA
- active site: Y54 (= Y53), G61 (= G60), L84 (≠ H83), N195 (= N192), Y292 (≠ L275), R295 (= R278), F342 (≠ A326), Q428 (≠ E411)
- binding caffeic acid: G61 (= G60), H83 (≠ S82), L84 (≠ H83), Y292 (≠ L275), R295 (= R278), N424 (≠ S407), N427 (≠ Q410), Q428 (≠ E411)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
36% identity, 93% coverage: 22:483/499 of query aligns to 23:502/515 of 2o7eA
- active site: Y54 (= Y53), G61 (= G60), L84 (≠ H83), N195 (= N192), Y292 (≠ L275), R295 (= R278), F342 (≠ A326), Q428 (≠ E411)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y53), G143 (= G141), L145 (= L143), N195 (= N192), Y292 (≠ L275), R295 (= R278), N325 (= N308), F342 (≠ A326)
6s7qA Crystal structure of ergothioneine degrading enzyme ergothionase from treponema denticola in complex with desmethyl-ergothioneine sulfonic acid (see paper)
28% identity, 97% coverage: 10:492/499 of query aligns to 9:491/497 of 6s7qA
- active site: Y53 (= Y53), G60 (= G60), D275 (= D273), A324 (≠ S322)
- binding (2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic acid: Y53 (= Y53), V59 (= V59), G60 (= G60), S194 (≠ N192), F326 (≠ A324), T380 (≠ I380), K383 (≠ Y383), E411 (= E411)
B2J528 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
30% identity, 73% coverage: 8:372/499 of query aligns to 30:410/569 of B2J528
- A167 (vs. gap) 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)
P0DO55 Phenylalanine/tyrosine ammonia-lyase 1; FuPAL1; EC 4.3.1.25 from Fritillaria unibracteata (Sichuan fritillary) (see paper)
28% identity, 89% coverage: 4:449/499 of query aligns to 62:532/722 of P0DO55
- F141 (≠ S82) mutation to H: Increased activity toward L-tyrosine (L-Tyr) but reduced ability to use L-phenylalanine (L-Phe) as substrate.
- S208 (vs. gap) mutation to A: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- I218 (= I149) mutation to P: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- E490 (≠ L409) mutation to N: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
29% identity, 72% coverage: 11:371/499 of query aligns to 33:409/567 of Q3M5Z3
- L108 (≠ H83) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (≠ Y142) 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)
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, 72% coverage: 11:371/499 of query aligns to 9:383/537 of 5ltmB
- active site: F54 (≠ Y53), G61 (= G60), L84 (≠ H83), N197 (= N192), Y288 (≠ L275), R291 (= R278), F337 (≠ A326)
- binding hydrocinnamic acid: F60 (≠ V59), A143 (≠ Y142), L145 (= L143), Y288 (≠ L275), R291 (= R278)
Sites not aligning to the query:
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, 100% coverage: 3:499/499 of query aligns to 25:541/687 of Q68G84
- Y80 (= Y53) 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 (= G141) modified: Crosslink with 175, 5-imidazolinone (Ala-Gly)
- N231 (= N192) 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 (= Q272) 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 (≠ L275) 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 (= R278) 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 (= N308) binding ; mutation to X: Abolishes enzyme activity; when associated with X-231.
- F371 (≠ A326) mutation to X: Abolishes enzyme activity; when associated with X-322.
- N458 (≠ Q410) 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, 100% coverage: 3:499/499 of query aligns to 25:541/698 of Q6GZ04
- Y80 (= Y53) mutation to F: Abolishes enzyme activity.
- L104 (= L75) mutation to A: Decreases enzyme activity.
- Q319 (= Q272) binding
- R325 (= R278) binding
Query Sequence
>SMc00669 FitnessBrowser__Smeli:SMc00669
MGEMISLDGPLTWREIASIAEGASLDLSGPARLRIAQARRIVDALVERGIRGYGINTGVG
ALCDVIISRENQQALSRNIILSHACGVGDPLGRVEARAVMAAQIANLTHGYSGVRVETAE
MLLALLNADIIPLIPSRGSVGYLTHAAAIGLVLIGHGSAMQGTERLSGADALARLGLAPL
RLEAKEGLSLVNGTPCATGLAALALARTERLFAWADAAAAMTYENLGSQANAFAELPLAL
RQSPGLSAVGEGLRDWLADSPMLAGTAGTRTQDPLSLRAVPQVHGAARDAFGQVAEIVDR
ELASVTDNPAVAGSPEAPEVHSQAHAVGAALGLAMDSLAVAVAEVAAISERRIDRLVNPL
VSGLPAFLAGDSGVSSGFMIAQYTAAALVAENRRLAAPASLDGGITSALQEDMLTHATPA
AWKALSIVDNLERILAIELLAAAQAYELQPQAQGKAQRTAALYGHIRSAIPAYRDDRPMN
EDFDRMRRLMRAAPAHGQL
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