SitesBLAST
Comparing RR42_RS16920 FitnessBrowser__Cup4G11:RR42_RS16920 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)
61% identity, 97% coverage: 14:521/526 of query aligns to 4:509/510 of P21310
- S144 (= S154) 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)
60% identity, 97% coverage: 14:521/526 of query aligns to 3:506/507 of 1gkmA
- active site: Y53 (= Y64), G60 (= G71), H83 (= H94), N193 (= N206), Y278 (= Y290), R281 (= R293), F327 (= F339), E412 (= E424)
- binding cysteine: G142 (= G155), L189 (= L202), N193 (= N206), F327 (= F339)
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
46% identity, 92% coverage: 14:497/526 of query aligns to 114:602/657 of P21213
- S254 (= S154) mutation to A: Complete loss of activity.
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
42% identity, 94% coverage: 13:505/526 of query aligns to 129:626/677 of Q20502
- D536 (= D415) 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)
38% identity, 96% coverage: 1:506/526 of query aligns to 1:525/539 of Q8GMG0
- Y63 (= Y64) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ K72) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H94) binding substrate; mutation to F: Complete loss of activity.
- A152 (= A153) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S154) modified: 2,3-didehydroalanine (Ser)
- G154 (= G155) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N206) binding substrate
- 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 (= R293) binding substrate
- Y415 (≠ V396) mutation to V: Complete loss of activity.
2rjsA Sgtam bound to substrate mimic (see paper)
38% identity, 93% coverage: 20:506/526 of query aligns to 8:512/526 of 2rjsA
- active site: Y52 (= Y64), G59 (= G71), H82 (= H94), N192 (= N206), Y295 (= Y290), R298 (= R293), F343 (= F339), Q429 (≠ E424)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y64), G59 (= G71), H82 (= H94), G141 (= G155), L143 (= L157), N192 (= N206), Y295 (= Y290), R298 (= R293), F343 (= F339), Q429 (≠ E424)
2rjrA Substrate mimic bound to sgtam (see paper)
38% identity, 93% coverage: 20:506/526 of query aligns to 8:512/526 of 2rjrA
- active site: Y52 (= Y64), G59 (= G71), H82 (= H94), N192 (= N206), Y295 (= Y290), R298 (= R293), F343 (= F339), Q429 (≠ E424)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y64), G59 (= G71), H82 (= H94), G141 (= G155), L143 (= L157), N192 (= N206), F343 (= F339), Q429 (≠ E424)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
38% identity, 93% coverage: 20:506/526 of query aligns to 8:512/526 of 2qveA
- active site: Y52 (= Y64), G59 (= G71), H82 (= H94), N192 (= N206), Y295 (= Y290), R298 (= R293), F343 (= F339), Q429 (≠ E424)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y64), G59 (= G71), H82 (= H94), G141 (= G155), L143 (= L157), N192 (= N206), Y295 (= Y290), R298 (= R293), F343 (= F339), Q429 (≠ E424)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
38% identity, 93% coverage: 20:506/526 of query aligns to 9:513/527 of 3kdzA
- active site: F53 (≠ Y64), G60 (= G71), H83 (= H94), N193 (= N206), Y296 (= Y290), R299 (= R293), F344 (= F339), Q430 (≠ E424)
- binding tyrosine: F53 (≠ Y64), Y59 (≠ F70), G60 (= G71), H83 (= H94), G142 (= G155), N193 (= N206), Y296 (= Y290), R299 (= R293), F344 (= F339)
Q0VZ68 Tyrosine 2,3-aminomutase; Tyrosine ammonia-lyase; EC 5.4.3.6; EC 4.3.1.23 from Chondromyces crocatus (see paper)
36% identity, 90% coverage: 20:492/526 of query aligns to 7:516/531 of Q0VZ68