SitesBLAST
Comparing Pf1N1B4_1581 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1581 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)
P21310 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 4 papers)
84% identity, 100% coverage: 1:510/510 of query aligns to 1:510/510 of P21310
- M1 (= M1) modified: Initiator methionine, Removed
- S144 (= S144) 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)
83% identity, 100% coverage: 2:510/510 of query aligns to 1:507/507 of 1gkmA
- active site: Y53 (= Y54), G60 (= G61), H83 (= H84), N193 (= N196), Y278 (= Y281), R281 (= R284), F327 (= F330), E412 (= E415)
- binding cysteine: G142 (= G145), L189 (= L192), N193 (= N196), F327 (= F330)
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
44% identity, 95% coverage: 11:493/510 of query aligns to 121:607/657 of P21213
- S254 (= S144) mutation to A: Complete loss of activity.
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
42% identity, 92% coverage: 26:493/510 of query aligns to 152:623/677 of Q20502
- D536 (= D406) 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, 92% coverage: 10:479/510 of query aligns to 7:495/531 of Q0VZ68
- F57 (= F60) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ LASTRI 63:68) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ LSHA 82:85) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ LSHAA 82:86) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ A187) mutation to R: Gain of aminomutase activity.
- K242 (≠ R245) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. gap) mutation Missing: Total loss of aminomutase activity.
- P377 (≠ K363) mutation to R: No effect.
- C396 (≠ S380) mutation to S: No effect.
- E399 (≠ M383) 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. 383:390, 25% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 411:417, 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)
33% identity, 93% coverage: 21:496/510 of query aligns to 22:510/514 of 3unvA
- active site: Y53 (= Y54), G60 (= G61), V83 (≠ H84), L191 (= L194), D291 (= D279), S294 (= S282), G340 (= G328), D427 (≠ N413)
- binding phenylalanine: Y53 (= Y54), G60 (= G61), G142 (= G145), L144 (= L147), N326 (= N314), F342 (= F330)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y54), G60 (= G61), G142 (= G145), N193 (= N196), N326 (= N314), F342 (= F330)
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)
35% identity, 95% coverage: 11:494/510 of query aligns to 20:522/539 of Q8GMG0
- Y63 (= Y54) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ L62) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H84) binding ; mutation to F: Complete loss of activity.
- A152 (= A143) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S144) modified: 2,3-didehydroalanine (Ser)
- G154 (= G145) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N196) 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 (= R284) binding
- Y415 (≠ V387) mutation to V: Complete loss of activity.
2rjsA Sgtam bound to substrate mimic (see paper)
35% identity, 95% coverage: 11:494/510 of query aligns to 9:509/526 of 2rjsA
- active site: Y52 (= Y54), G59 (= G61), H82 (= H84), N192 (= N196), Y295 (= Y281), R298 (= R284), F343 (= F330), Q429 (≠ E415)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y54), G59 (= G61), H82 (= H84), G141 (= G145), L143 (= L147), N192 (= N196), Y295 (= Y281), R298 (= R284), F343 (= F330), Q429 (≠ E415)
2rjrA Substrate mimic bound to sgtam (see paper)
35% identity, 95% coverage: 11:494/510 of query aligns to 9:509/526 of 2rjrA
- active site: Y52 (= Y54), G59 (= G61), H82 (= H84), N192 (= N196), Y295 (= Y281), R298 (= R284), F343 (= F330), Q429 (≠ E415)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y54), G59 (= G61), H82 (= H84), G141 (= G145), L143 (= L147), N192 (= N196), F343 (= F330), Q429 (≠ E415)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
35% identity, 95% coverage: 11:494/510 of query aligns to 9:509/526 of 2qveA