SitesBLAST
Comparing SM_b21165 FitnessBrowser__Smeli:SM_b21165 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)
P21310 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 4 papers)
53% identity, 99% coverage: 3:509/511 of query aligns to 4:510/510 of P21310
- S144 (= S143) 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)
53% identity, 99% coverage: 3:509/511 of query aligns to 3:507/507 of 1gkmA
- active site: Y53 (= Y53), G60 (= G60), H83 (= H83), N193 (= N195), Y278 (= Y280), R281 (= R283), F327 (= F328), E412 (= E414)
- binding cysteine: G142 (= G144), L189 (= L191), N193 (= N195), F327 (= F328)
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
44% identity, 91% coverage: 26:492/511 of query aligns to 137:607/657 of P21213
- S254 (= S143) mutation to A: Complete loss of activity.
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
42% identity, 93% coverage: 35:510/511 of query aligns to 162:637/677 of Q20502
- D536 (= D405) 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, 92% coverage: 35:502/511 of query aligns to 42:531/539 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 (≠ K61) 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 (= A142) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S143) modified: 2,3-didehydroalanine (Ser)
- G154 (= G144) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N195) 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 (= R283) binding
- Y415 (≠ V386) mutation to V: Complete loss of activity.
2rjsA Sgtam bound to substrate mimic (see paper)
37% identity, 92% coverage: 35:502/511 of query aligns to 31:518/526 of 2rjsA
- active site: Y52 (= Y53), G59 (= G60), H82 (= H83), N192 (= N195), Y295 (= Y280), R298 (= R283), F343 (= F328), Q429 (≠ E414)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y53), G59 (= G60), H82 (= H83), G141 (= G144), L143 (= L146), N192 (= N195), Y295 (= Y280), R298 (= R283), F343 (= F328), Q429 (≠ E414)
2rjrA Substrate mimic bound to sgtam (see paper)
37% identity, 92% coverage: 35:502/511 of query aligns to 31:518/526 of 2rjrA
- active site: Y52 (= Y53), G59 (= G60), H82 (= H83), N192 (= N195), Y295 (= Y280), R298 (= R283), F343 (= F328), Q429 (≠ E414)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y53), G59 (= G60), H82 (= H83), G141 (= G144), L143 (= L146), N192 (= N195), F343 (= F328), Q429 (≠ E414)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
37% identity, 92% coverage: 35:502/511 of query aligns to 31:518/526 of 2qveA
- active site: Y52 (= Y53), G59 (= G60), H82 (= H83), N192 (= N195), Y295 (= Y280), R298 (= R283), F343 (= F328), Q429 (≠ E414)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y53), G59 (= G60), H82 (= H83), G141 (= G144), L143 (= L146), N192 (= N195), Y295 (= Y280), R298 (= R283), F343 (= F328), Q429 (≠ E414)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
37% identity, 92% coverage: 35:502/511 of query aligns to 32:519/527 of 3kdzA
- active site: F53 (≠ Y53), G60 (= G60), H83 (= H83), N193 (= N195), Y296 (= Y280), R299 (= R283), F344 (= F328), Q430 (≠ E414)
- binding tyrosine: F53 (≠ Y53), Y59 (≠ F59), G60 (= G60), H83 (= H83), G142 (= G144), N193 (= N195), Y296 (= Y280), R299 (= R283), F344 (= F328)
Q0VZ68 Tyrosine 2,3-aminomutase; Tyrosine ammonia-lyase; EC 5.4.3.6; EC 4.3.1.23 from Chondromyces crocatus (see paper)
35% identity, 84% coverage: 9:438/511 of query aligns to 7:455/531 of Q0VZ68
- F57 (= F59) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ LASIKI 62:67) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ LSHC 81:84) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ LSHCC 81:85) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ A186) mutation to R: Gain of aminomutase activity.
- K242 (≠ R244) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. 272:276, 14% identical) mutation Missing: Total loss of aminomutase activity.
- P377 (= P361) mutation to R: No effect.
- C396 (≠ S379) mutation to S: No effect.
- E399 (≠ M382) 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. 382:389, 0% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 410:416, 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, 90% coverage: 35:492/511 of query aligns to 35:507/514 of 3unvA
- active site: Y53 (= Y53), G60 (= G60), V83 (≠ H83), L191 (= L193), D291 (= D278), S294 (≠ C281), G340 (= G326), D427 (≠ N412)
- binding phenylalanine: Y53 (= Y53), G60 (= G60), G142 (= G144), L144 (= L146), N326 (= N313), F342 (= F328)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y53), G60 (= G60), G142 (= G144), N193 (= N195), N326 (= N313), F342 (= F328)
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
36% identity, 88% coverage: 40:487/511 of query aligns to 41:504/515 of 2o7dA
- active site: Y54 (= Y53), G61 (= G60), L84 (≠ H83), N195 (= N195), Y292 (= Y280), R295 (= R283), F342 (= F328), Q428 (≠ E414)
- binding caffeic acid: G61 (= G60), H83 (≠ S82), L84 (≠ H83), Y292 (= Y280), R295 (= R283), N424 (≠ S410), N427 (≠ Q413), Q428 (≠ E414)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
36% identity, 88% coverage: 40:487/511 of query aligns to 41:504/515 of 2o7eA
- active site: Y54 (= Y53), G61 (= G60), L84 (≠ H83), N195 (= N195), Y292 (= Y280), R295 (= R283), F342 (= F328), Q428 (≠ E414)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y53), G143 (= G144), L145 (= L146), N195 (= N195), Y292 (= Y280), R295 (= R283), N325 (= N313), F342 (= F328)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
31% identity, 100% coverage: 2:510/511 of query aligns to 25:567/567 of Q3M5Z3
- L108 (≠ H83) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (= A142) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S143) modified: 2,3-didehydroalanine (Ser)
- G169 (= G144) 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.
- C565 (≠ K508) mutation to S: Prevents formation of artifactual disulfide bonds and increases solubility; when associated with S-503.
Sites not aligning to the query:
- 1:21 mutation Missing: No effect on enzyme activity.
5ltmB Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis (y78f-c503s-c565s) bound to cinnamate (see paper)
31% identity, 98% coverage: 2:504/511 of query aligns to 1:526/537 of 5ltmB
- active site: F54 (≠ Y53), G61 (= G60), L84 (≠ H83), N197 (= N195), Y288 (= Y280), R291 (= R283), F337 (= F328), Q426 (≠ H416)
- binding hydrocinnamic acid: F60 (= F59), A143 (= A142), L145 (= L146), Y288 (= Y280), R291 (= R283)
6s7qA Crystal structure of ergothioneine degrading enzyme ergothionase from treponema denticola in complex with desmethyl-ergothioneine sulfonic acid (see paper)
28% identity, 97% coverage: 3:497/511 of query aligns to 3:494/497 of 6s7qA
- active site: Y53 (= Y53), G60 (= G60), D275 (= D278), A324 (≠ G326)
- binding (2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic acid: Y53 (= Y53), V59 (≠ F59), G60 (= G60), S194 (≠ N195), F326 (= F328), T380 (≠ I383), K383 (≠ V386), E411 (= E414)
B2J528 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
32% identity, 85% coverage: 22:453/511 of query aligns to 45:491/569 of B2J528
- A167 (= A142) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S143) modified: 2,3-didehydroalanine (Ser)
- G169 (= G144) modified: Crosslink with 167, 5-imidazolinone (Ala-Gly)
P11544 Phenylalanine/tyrosine ammonia-lyase; Bifunctional phenylalanine ammonia-lyase; Bifunctional PAL; EC 4.3.1.25 from Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides) (see paper)
32% identity, 79% coverage: 52:453/511 of query aligns to 109:539/716 of P11544
- A211 (= A142) modified: Crosslink with 213, 5-imidazolinone (Ala-Gly)
- S212 (= S143) modified: 2,3-didehydroalanine (Ser)
- G213 (= G144) modified: Crosslink with 211, 5-imidazolinone (Ala-Gly)
- K468 (≠ M382) binding
- E496 (≠ S410) binding
P0DO55 Phenylalanine/tyrosine ammonia-lyase 1; FuPAL1; EC 4.3.1.25 from Fritillaria unibracteata (Sichuan fritillary) (see paper)
29% identity, 85% coverage: 53:485/511 of query aligns to 114:572/722 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 (≠ A142) mutation to A: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- I218 (≠ M152) mutation to P: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- E490 (≠ S410) 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)
30% identity, 86% coverage: 50:487/511 of query aligns to 77:526/687 of Q68G84
- Y80 (= Y53) active site, Proton donor/acceptor; mutation Y->A,F: Abolishes enzyme activity.
- A175 (= A142) modified: Crosslink with 177, 5-imidazolinone (Ala-Gly)
- S176 (= S143) modified: 2,3-didehydroalanine (Ser)
- G177 (= G144) modified: Crosslink with 175, 5-imidazolinone (Ala-Gly)
- N231 (= N195) 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 (= Y280) 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 (= F328) mutation to X: Abolishes enzyme activity; when associated with X-322.
- N458 (≠ Q413) binding
Query Sequence
>SM_b21165 FitnessBrowser__Smeli:SM_b21165
MTVILRPGSVPLSDLETIYWTGAPARLDAAFDAGIAKAAARIAEIVAGNAPVYGINTGFG
KLASIKIDSSDVATLQRNLILSHCCGVGQPLTEDIVRLIMALKLISLGRGASGVRLELVR
LIEAMLDKGVIPLIPEKGSVGASGDLAPLAHMAAVMMGHGEAFFAGERMKGDAALKAAGL
SPVTLAAKEGLALINGTQVSTALALAGLFRAHRAGQAALITGALSTDAAMGSSAPFHPDI
HTLRGHKGQIDTAAALRQLLTGSPIRQSHIEGDERVQDPYCIRCQPQVDGACLDLLRSVA
ATLTIEANAVTDNPLVLSDNSVVSGGNFHAEPVAFAADQIALAVCEIGAISQRRIALLVD
PALSYGLPAFLAKKPGLNSGLMIAEVTSAALMSENKQLSHPASVDSTPTSANQEDHVSMA
CHGARRLLQMTENLFSIIGIEALAAVQGIEFRAPLTTSPELQKAAAAVRGVSSSIEEDRY
MADDLKAAGDLVASGRLAAAVSAGILPKLEN
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