SitesBLAST
Comparing Pf1N1B4_1509 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1509 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)
Q0VZ68 Tyrosine 2,3-aminomutase; Tyrosine ammonia-lyase; EC 5.4.3.6; EC 4.3.1.23 from Chondromyces crocatus (see paper)
37% identity, 93% coverage: 16:491/514 of query aligns to 8:495/531 of Q0VZ68
- F57 (≠ Y67) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ SCVVAV 70:75) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ TFHG 89:92) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ TFHGC 89:93) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ R194) mutation to R: Gain of aminomutase activity.
- K242 (= K252) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. gap) mutation Missing: Total loss of aminomutase activity.
- P377 (≠ E366) mutation to R: No effect.
- C396 (≠ N387) mutation to S: No effect.
- E399 (≠ K391) 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. 391:398, 13% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 419:425, 43% identical) mutation to SAGREDH: Total loss of aminomutase activity.; mutation to SANQEDH: Total loss of aminomutase activity.
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, 89% coverage: 45:501/514 of query aligns to 47:517/539 of Q8GMG0
- Y63 (= Y61) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ D69) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H91) binding ; mutation to F: Complete loss of activity.
- A152 (= A150) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S151) modified: 2,3-didehydroalanine (Ser)
- G154 (= G152) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N203) binding
- Y303 (≠ H278) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- R311 (= R287) binding
- Y415 (≠ I395) mutation to V: Complete loss of activity.
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
35% identity, 93% coverage: 16:494/514 of query aligns to 121:596/657 of P21213
- S254 (= S151) mutation to A: Complete loss of activity.
2rjsA Sgtam bound to substrate mimic (see paper)
38% identity, 89% coverage: 45:501/514 of query aligns to 36:504/526 of 2rjsA
- active site: Y52 (= Y61), G59 (= G68), H82 (= H91), N192 (= N203), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (= Q423)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y61), G59 (= G68), H82 (= H91), G141 (= G152), L143 (= L154), N192 (= N203), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (= Q423)
2rjrA Substrate mimic bound to sgtam (see paper)
38% identity, 89% coverage: 45:501/514 of query aligns to 36:504/526 of 2rjrA
- active site: Y52 (= Y61), G59 (= G68), H82 (= H91), N192 (= N203), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (= Q423)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y61), G59 (= G68), H82 (= H91), G141 (= G152), L143 (= L154), N192 (= N203), F343 (= F333), Q429 (= Q423)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
38% identity, 89% coverage: 45:501/514 of query aligns to 36:504/526 of 2qveA
- active site: Y52 (= Y61), G59 (= G68), H82 (= H91), N192 (= N203), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (= Q423)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y61), G59 (= G68), H82 (= H91), G141 (= G152), L143 (= L154), N192 (= N203), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (= Q423)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
37% identity, 89% coverage: 45:501/514 of query aligns to 37:505/527 of 3kdzA
- active site: F53 (≠ Y61), G60 (= G68), H83 (= H91), N193 (= N203), Y296 (= Y284), R299 (= R287), F344 (= F333), Q430 (= Q423)
- binding tyrosine: F53 (≠ Y61), Y59 (= Y67), G60 (= G68), H83 (= H91), G142 (= G152), N193 (= N203), Y296 (= Y284), R299 (= R287), F344 (= F333)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
34% identity, 88% coverage: 9:461/514 of query aligns to 26:490/567 of Q3M5Z3
- L108 (≠ H91) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (= A150) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S151) modified: 2,3-didehydroalanine (Ser)
- G169 (= G152) 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.
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
31% identity, 95% coverage: 16:505/514 of query aligns to 10:507/514 of 3unvA
- active site: Y53 (= Y61), G60 (= G68), V83 (≠ H91), L191 (= L201), D291 (= D282), S294 (= S285), G340 (= G331), D427 (≠ H421)
- binding phenylalanine: Y53 (= Y61), G60 (= G68), G142 (= G152), L144 (= L154), N326 (= N317), F342 (= F333)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y61), G60 (= G68), G142 (= G152), N193 (= N203), N326 (= N317), F342 (= F333)
B2J528 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
34% identity, 90% coverage: 1:461/514 of query aligns to 18:490/569 of B2J528
- A167 (= A150) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S151) modified: 2,3-didehydroalanine (Ser)
- G169 (= G152) 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)
34% identity, 88% coverage: 16:468/514 of query aligns to 70:539/722 of P0DO55
- F141 (= F90) mutation to H: Increased activity toward L-tyrosine (L-Tyr) but reduced ability to use L-phenylalanine (L-Phe) as substrate.
- S208 (≠ A150) mutation to A: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- I218 (≠ V160) mutation to P: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- E490 (= E419) mutation to N: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
36% identity, 96% coverage: 19:510/514 of query aligns to 140:629/677 of Q20502
- D536 (≠ F414) mutation to N: In am130; causes strong resistance to nickel and zinc toxicity.
5ltmB Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis (y78f-c503s-c565s) bound to cinnamate (see paper)
34% identity, 90% coverage: 9:473/514 of query aligns to 2:481/537 of 5ltmB
- active site: F54 (≠ Y61), G61 (= G68), L84 (≠ H91), N197 (= N203), Y288 (= Y284), R291 (= R287), F337 (= F333), Q426 (= Q423)
- binding hydrocinnamic acid: F60 (≠ Y67), A143 (= A150), L145 (= L154), Y288 (= Y284), R291 (= R287)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
36% identity, 90% coverage: 37:498/514 of query aligns to 30:502/515 of 2o7eA
- active site: Y54 (= Y61), G61 (= G68), L84 (≠ H91), N195 (= N203), Y292 (= Y284), R295 (= R287), F342 (= F333), Q428 (= Q423)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y61), G143 (= G152), L145 (= L154), N195 (= N203), Y292 (= Y284), R295 (= R287), N325 (= N317), F342 (= F333)
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
36% identity, 90% coverage: 37:498/514 of query aligns to 30:502/515 of 2o7dA
- active site: Y54 (= Y61), G61 (= G68), L84 (≠ H91), N195 (= N203), Y292 (= Y284), R295 (= R287), F342 (= F333), Q428 (= Q423)
- binding caffeic acid: G61 (= G68), H83 (≠ F90), L84 (≠ H91), Y292 (= Y284), R295 (= R287), N424 (≠ E419), N427 (= N422), Q428 (= Q423)
P24481 Phenylalanine ammonia-lyase 1; EC 4.3.1.24 from Petroselinum crispum (Parsley) (Petroselinum hortense) (see paper)
35% identity, 82% coverage: 50:468/514 of query aligns to 100:533/716 of P24481
- S203 (= S151) modified: 2,3-didehydroalanine (Ser); mutation to A: Complete loss of activity.
- S210 (= S158) mutation to A: No loss of activity.
6hqfA Structure of phenylalanine ammonia-lyase from petroselinum crispum in complex with (r)-apep
35% identity, 82% coverage: 50:468/514 of query aligns to 76:495/673 of 6hqfA
- active site: Y86 (= Y61), G93 (= G68), Y313 (= Y284), F362 (= F333)
- binding [(1R)-1-amino-2-phenylethyl]phosphonic acid: Y86 (= Y61), F92 (≠ Y67), G178 (= G152), L180 (= L154), N234 (= N203), N346 (= N317), F362 (= F333), E446 (= E419)
6f6tB Phenylalanine ammonia-lyase (pal) from petroselinum crispum complexed with s-appa
35% identity, 82% coverage: 50:468/514 of query aligns to 77:496/677 of 6f6tB
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)
35% identity, 89% coverage: 12:467/514 of query aligns to 31:502/698 of Q6GZ04
- Y80 (= Y61) mutation to F: Abolishes enzyme activity.
- L104 (≠ H79) mutation to A: Decreases enzyme activity.
- Q319 (= Q281) binding
- R325 (= R287) binding
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)
34% identity, 89% coverage: 12:467/514 of query aligns to 31:502/687 of Q68G84
- Y80 (= Y61) active site, Proton donor/acceptor; mutation Y->A,F: Abolishes enzyme activity.
- A175 (= A150) modified: Crosslink with 177, 5-imidazolinone (Ala-Gly)
- S176 (= S151) modified: 2,3-didehydroalanine (Ser)
- G177 (= G152) modified: Crosslink with 175, 5-imidazolinone (Ala-Gly)
- N231 (= N203) 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 (= Q281) 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 (= Y284) 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 (= R287) 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 (= N317) binding ; mutation to X: Abolishes enzyme activity; when associated with X-231.
- F371 (= F333) mutation to X: Abolishes enzyme activity; when associated with X-322.
- N458 (= N422) binding
Query Sequence
>Pf1N1B4_1509 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1509
MTTPTLEPVTFGELPLRIEDVLALANRQVPTQLQGDPEFRQRIAKGPQFLDSLLDKEGVI
YGVTTGYGDSCVVAVPLHHVEALPRHLYTFHGCGLGKLLDAQATRAVLAARLQSLCQGVS
GVRVELLERLQAFLEYDILPLIPEEGSVGASGDLTPLSYVAATLSGEREVMFRGERRQAA
DVHSELGWEPLVLRPKEALALMNGTAVMTGLACLAYARADYLLQLATRITALNVVALQGN
PEHFDERLFAAKPHPGQMQVAAWLRKDLAIDAPTAPLHRLQDRYSLRCAPHVLGVLADSL
NWLRSFIEIELNSANDNPIIDAEAERVLHGGHFYGGHIAFAMDSLKTLVANVADLLDRQL
ALLVDERYNHGLPSNLSGATADRAMLNHGFKAVQIGTSAWTAEALKNTMPASVFSRSTEC
HNQDKVSMGTISARDAIRVLELTEQVAAATLLAANQGVWLRGQAEDARPLPPALAAMHEE
LAKDFPPVIEDRALEGELRLCLQRIAEQHWRLHA
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