SitesBLAST
Comparing WP_019867171.1 NCBI__GCF_000384075.1:WP_019867171.1 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)
34% identity, 98% coverage: 5:507/511 of query aligns to 111:613/657 of P21213
- S254 (= S150) mutation to A: Complete loss of activity.
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
34% identity, 98% coverage: 6:507/511 of query aligns to 128:629/677 of Q20502
- D536 (≠ F414) 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)
34% identity, 96% coverage: 3:495/511 of query aligns to 8:514/539 of Q8GMG0
- Y63 (= Y60) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ D68) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H90) binding substrate; mutation to F: Complete loss of activity.
- A152 (= A149) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S150) modified: 2,3-didehydroalanine (Ser)
- G154 (= G151) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N202) binding substrate
- Y303 (≠ R279) 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 substrate
- Y415 (≠ I395) mutation to V: Complete loss of activity.
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
31% identity, 96% coverage: 9:497/511 of query aligns to 4:502/514 of 3unvA
- active site: Y53 (= Y60), G60 (= G67), V83 (≠ H90), L191 (≠ I200), D291 (= D282), S294 (= S285), G340 (= G331), D427 (≠ H421)
- binding phenylalanine: Y53 (= Y60), G60 (= G67), G142 (= G151), L144 (= L153), N326 (= N317), F342 (= F333)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y60), G60 (= G67), G142 (= G151), N193 (= N202), N326 (= N317), F342 (= F333)
2rjsA Sgtam bound to substrate mimic (see paper)
34% identity, 95% coverage: 8:495/511 of query aligns to 2:501/526 of 2rjsA
- active site: Y52 (= Y60), G59 (= G67), H82 (= H90), N192 (= N202), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (= Q423)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y60), G59 (= G67), H82 (= H90), G141 (= G151), L143 (= L153), N192 (= N202), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (= Q423)
2rjrA Substrate mimic bound to sgtam (see paper)
34% identity, 95% coverage: 8:495/511 of query aligns to 2:501/526 of 2rjrA
- active site: Y52 (= Y60), G59 (= G67), H82 (= H90), N192 (= N202), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (= Q423)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y60), G59 (= G67), H82 (= H90), G141 (= G151), L143 (= L153), N192 (= N202), F343 (= F333), Q429 (= Q423)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
34% identity, 95% coverage: 8:495/511 of query aligns to 2:501/526 of 2qveA
- active site: Y52 (= Y60), G59 (= G67), H82 (= H90), N192 (= N202), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (= Q423)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y60), G59 (= G67), H82 (= H90), G141 (= G151), L143 (= L153), N192 (= N202), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (= Q423)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
34% identity, 95% coverage: 8:495/511 of query aligns to 3:502/527 of 3kdzA
- active site: F53 (≠ Y60), G60 (= G67), H83 (= H90), N193 (= N202), Y296 (= Y284), R299 (= R287), F344 (= F333), Q430 (= Q423)
- binding tyrosine: F53 (≠ Y60), Y59 (≠ F66), G60 (= G67), H83 (= H90), G142 (= G151), N193 (= N202), Y296 (= Y284), R299 (= R287), F344 (= F333)
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, 94% coverage: 10:491/511 of query aligns to 3:498/531 of Q0VZ68
- F57 (= F66) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ SCTVSV 69:74) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ TFHG 88:91) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ TFHGC 88:92) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ K193) mutation to R: Gain of aminomutase activity.
- K242 (= K251) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. 269:277, 29% identical) mutation Missing: Total loss of aminomutase activity.
- P377 (= P366) mutation to R: No effect.
- C396 (≠ M385) 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.
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
36% identity, 90% coverage: 47:505/511 of query aligns to 41:512/515 of 2o7eA
- active site: Y54 (= Y60), G61 (= G67), L84 (≠ H90), N195 (= N202), Y292 (= Y284), R295 (= R287), F342 (= F333), Q428 (= Q423)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y60), G143 (= G151), L145 (= L153), N195 (= N202), Y292 (= Y284), R295 (= R287), N325 (= N317), F342 (= F333)
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
36% identity, 90% coverage: 47:505/511 of query aligns to 41:512/515 of 2o7dA
- active site: Y54 (= Y60), G61 (= G67), L84 (≠ H90), N195 (= N202), Y292 (= Y284), R295 (= R287), F342 (= F333), Q428 (= Q423)
- binding caffeic acid: G61 (= G67), H83 (≠ F89), L84 (≠ H90), Y292 (= Y284), R295 (= R287), N424 (≠ E419), N427 (= N422), Q428 (= Q423)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
32% identity, 93% coverage: 7:481/511 of query aligns to 25:518/567 of Q3M5Z3
- L108 (≠ H90) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (= A149) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S150) modified: 2,3-didehydroalanine (Ser)
- G169 (= G151) 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.
Sites not aligning to the query:
- 1:21 mutation Missing: No effect on enzyme activity.
- 565 C→S: Prevents formation of artifactual disulfide bonds and increases solubility; when associated with S-503.
B2J528 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
33% identity, 87% coverage: 15:461/511 of query aligns to 33:490/569 of B2J528
- A167 (= A149) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S150) modified: 2,3-didehydroalanine (Ser)
- G169 (= G151) modified: Crosslink with 167, 5-imidazolinone (Ala-Gly)
5ltmB Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis (y78f-c503s-c565s) bound to cinnamate (see paper)
32% identity, 93% coverage: 7:481/511 of query aligns to 1:492/537 of 5ltmB
- active site: F54 (≠ Y60), G61 (= G67), L84 (≠ H90), N197 (= N202), Y288 (= Y284), R291 (= R287), F337 (= F333), Q426 (= Q423)
- binding hydrocinnamic acid: F60 (= F66), A143 (= A149), L145 (= L153), Y288 (= Y284), R291 (= R287)
P0DO55 Phenylalanine/tyrosine ammonia-lyase 1; FuPAL1; EC 4.3.1.25 from Fritillaria unibracteata (Sichuan fritillary) (see paper)
32% identity, 93% coverage: 5:478/511 of query aligns to 60:549/722 of P0DO55
- F141 (= F89) mutation to H: Increased activity toward L-tyrosine (L-Tyr) but reduced ability to use L-phenylalanine (L-Phe) as substrate.
- S208 (≠ A149) mutation to A: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- I218 (≠ L159) 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.
P24481 Phenylalanine ammonia-lyase 1; EC 4.3.1.24 from Petroselinum crispum (Parsley) (Petroselinum hortense) (see paper)
31% identity, 93% coverage: 5:478/511 of query aligns to 54:543/716 of P24481
- S203 (= S150) modified: 2,3-didehydroalanine (Ser); mutation to A: Complete loss of activity.
- S210 (= S157) mutation to A: No loss of activity.
6f6tB Phenylalanine ammonia-lyase (pal) from petroselinum crispum complexed with s-appa
31% identity, 93% coverage: 5:478/511 of query aligns to 31:506/677 of 6f6tB
6hqfA Structure of phenylalanine ammonia-lyase from petroselinum crispum in complex with (r)-apep
31% identity, 99% coverage: 5:510/511 of query aligns to 30:535/673 of 6hqfA
- active site: Y86 (= Y60), G93 (= G67), Y313 (= Y284), F362 (= F333)
- binding [(1R)-1-amino-2-phenylethyl]phosphonic acid: Y86 (= Y60), F92 (= F66), G178 (= G151), L180 (= L153), N234 (= N202), N346 (= N317), F362 (= F333), E446 (= E419)
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, 89% coverage: 10:462/511 of query aligns to 62:539/716 of P11544
- A211 (= A149) modified: Crosslink with 213, 5-imidazolinone (Ala-Gly)
- S212 (= S150) modified: 2,3-didehydroalanine (Ser)
- G213 (= G151) modified: Crosslink with 211, 5-imidazolinone (Ala-Gly)
- K468 (= K391) binding (E)-cinnamate
- E496 (= E419) binding (E)-cinnamate
P21310 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 4 papers)
31% identity, 91% coverage: 42:504/511 of query aligns to 36:495/510 of P21310
- S144 (= S150) 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
Query Sequence
>WP_019867171.1 NCBI__GCF_000384075.1:WP_019867171.1
MMTDKKSIVFNGLPLSIEDICLIAARQAEIGLSTHEGFVTRIDKGAAFVDTLLKEQGFVY
GVTTGFGDSCTVSVPLHLVEELPRNLYTFHGCGLGQHFDAQQTRAILATRLTSLARGFSG
VRYQLLQQITTLLEQDILPLIPQEGSVGASGDLTPLSYLAAALSGEREVWYQGERRTTQA
VFAQLNIAPLALKPKEGLAIMNGTAAMTGIACLAYQRAGYLSQLCTRITSLASVALQGNA
YHFDEKLFSVKPHPGQNCVAGRIRADLQVTGSAPRNDTRLQDRYSLRCAPHVIGVLEDSL
PWLRQFIETELNSANDNPIIDAEGEHVLHGGHFYGGHIAFAMDSLKTAVANLADLMDRQM
AQLMDPKFNHGLPANLSGADAEQRMVNHGFKALQIAVSAWTAEALKLTMPASVFSRSTEC
HNQDKVSMGTIAARDCIRILELAEQVAAAVLFAVVQGVELRGNVGYLSPALQQTLDWVRQ
ISPFLNTDRALEQELRACLVLIRQQYWPLYD
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