SitesBLAST
Comparing Ac3H11_2558 FitnessBrowser__acidovorax_3H11:Ac3H11_2558 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)
60% identity, 95% coverage: 6:489/512 of query aligns to 2:487/510 of P21310
- S144 (= S148) 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, 95% coverage: 6:489/512 of query aligns to 1:484/507 of 1gkmA
- active site: Y53 (= Y58), G60 (= G65), H83 (= H88), N193 (= N200), Y278 (= Y284), R281 (= R287), F327 (= F332), E412 (= E417)
- binding cysteine: G142 (= G149), L189 (= L196), N193 (= N200), F327 (= F332)
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
45% identity, 96% coverage: 15:503/512 of query aligns to 121:616/657 of P21213
- S254 (= S148) mutation to A: Complete loss of activity.
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
41% identity, 95% coverage: 19:504/512 of query aligns to 141:633/677 of Q20502
- D536 (≠ T408) 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, 93% coverage: 15:489/512 of query aligns to 20:515/539 of Q8GMG0
- Y63 (= Y58) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ K66) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H88) binding ; mutation to F: Complete loss of activity.
- A152 (= A147) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S148) modified: 2,3-didehydroalanine (Ser)
- G154 (= G149) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N200) 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 (= R287) binding
- Y415 (≠ V389) mutation to V: Complete loss of activity.
2rjsA Sgtam bound to substrate mimic (see paper)
38% identity, 93% coverage: 15:489/512 of query aligns to 9:502/526 of 2rjsA
- active site: Y52 (= Y58), G59 (= G65), H82 (= H88), N192 (= N200), Y295 (= Y284), R298 (= R287), F343 (= F332), Q429 (≠ E417)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y58), G59 (= G65), H82 (= H88), G141 (= G149), L143 (= L151), N192 (= N200), Y295 (= Y284), R298 (= R287), F343 (= F332), Q429 (≠ E417)
2rjrA Substrate mimic bound to sgtam (see paper)
38% identity, 93% coverage: 15:489/512 of query aligns to 9:502/526 of 2rjrA
- active site: Y52 (= Y58), G59 (= G65), H82 (= H88), N192 (= N200), Y295 (= Y284), R298 (= R287), F343 (= F332), Q429 (≠ E417)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y58), G59 (= G65), H82 (= H88), G141 (= G149), L143 (= L151), N192 (= N200), F343 (= F332), Q429 (≠ E417)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
38% identity, 93% coverage: 15:489/512 of query aligns to 9:502/526 of 2qveA
- active site: Y52 (= Y58), G59 (= G65), H82 (= H88), N192 (= N200), Y295 (= Y284), R298 (= R287), F343 (= F332), Q429 (≠ E417)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y58), G59 (= G65), H82 (= H88), G141 (= G149), L143 (= L151), N192 (= N200), Y295 (= Y284), R298 (= R287), F343 (= F332), Q429 (≠ E417)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
37% identity, 93% coverage: 15:489/512 of query aligns to 10:503/527 of 3kdzA
- active site: F53 (≠ Y58), G60 (= G65), H83 (= H88), N193 (= N200), Y296 (= Y284), R299 (= R287), F344 (= F332), Q430 (≠ E417)
- binding tyrosine: F53 (≠ Y58), Y59 (≠ F64), G60 (= G65), H83 (= H88), G142 (= G149), N193 (= N200), Y296 (= Y284), R299 (= R287), F344 (= F332)
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, 88% coverage: 57:508/512 of query aligns to 50:522/531 of Q0VZ68
- F57 (= F64) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ LASTKI 67:72) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ LSHS 86:89) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ LSHSV 86:90) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (= G191) mutation to R: Gain of aminomutase activity.
- K242 (≠ R249) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. gap) mutation Missing: Total loss of aminomutase activity.
- P377 (= P365) mutation to R: No effect.
- C396 (≠ S382) mutation to S: No effect.
- E399 (≠ M385) 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. 385:392, 25% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 413:419, 14% identical) mutation to SAGREDH: Total loss of aminomutase activity.; mutation to SANQEDH: Total loss of aminomutase activity.
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
37% identity, 93% coverage: 15:491/512 of query aligns to 11:505/515 of 2o7dA
- active site: Y54 (= Y58), G61 (= G65), L84 (≠ H88), N195 (= N200), Y292 (= Y284), R295 (= R287), F342 (= F332), Q428 (≠ E417)
- binding caffeic acid: G61 (= G65), H83 (≠ S87), L84 (≠ H88), Y292 (= Y284), R295 (= R287), N424 (≠ S413), N427 (≠ Q416), Q428 (≠ E417)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
37% identity, 93% coverage: 15:491/512 of query aligns to 11:505/515 of 2o7eA
- active site: Y54 (= Y58), G61 (= G65), L84 (≠ H88), N195 (= N200), Y292 (= Y284), R295 (= R287), F342 (= F332), Q428 (≠ E417)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y58), G143 (= G149), L145 (= L151), N195 (= N200), Y292 (= Y284), R295 (= R287), N325 (= N317), F342 (= F332)
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
30% identity, 88% coverage: 42:491/512 of query aligns to 37:503/514 of 3unvA
- active site: Y53 (= Y58), G60 (= G65), V83 (≠ H88), L191 (= L198), D291 (= D282), S294 (= S285), G340 (= G330), D427 (≠ N415)
- binding phenylalanine: Y53 (= Y58), G60 (= G65), G142 (= G149), L144 (= L151), N326 (= N317), F342 (= F332)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y58), G60 (= G65), G142 (= G149), N193 (= N200), N326 (= N317), F342 (= F332)
6s7qA Crystal structure of ergothioneine degrading enzyme ergothionase from treponema denticola in complex with desmethyl-ergothioneine sulfonic acid (see paper)
29% identity, 94% coverage: 15:496/512 of query aligns to 10:490/497 of 6s7qA
- active site: Y53 (= Y58), G60 (= G65), D275 (= D282), A324 (≠ G330)
- binding (2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic acid: Y53 (= Y58), V59 (≠ F64), G60 (= G65), S194 (≠ N200), F326 (= F332), T380 (≠ I386), K383 (≠ V389), E411 (= E417)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
31% identity, 90% coverage: 14:475/512 of query aligns to 32:519/567 of Q3M5Z3
- L108 (≠ H88) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (= A147) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S148) modified: 2,3-didehydroalanine (Ser)
- G169 (= G149) modified: Crosslink with 167, 5-imidazolinone (Ala-Gly)
- C503 (≠ K459) 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.
5ltmB Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis (y78f-c503s-c565s) bound to cinnamate (see paper)
31% identity, 90% coverage: 14:476/512 of query aligns to 8:494/537 of 5ltmB
- active site: F54 (≠ Y58), G61 (= G65), L84 (≠ H88), N197 (= N200), Y288 (= Y284), R291 (= R287), F337 (= F332), Q426 (≠ D418)
- binding hydrocinnamic acid: F60 (= F64), A143 (= A147), L145 (= L151), Y288 (= Y284), R291 (= R287)
B2J528 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
30% identity, 86% coverage: 6:446/512 of query aligns to 24:487/569 of B2J528
- A167 (= A147) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S148) modified: 2,3-didehydroalanine (Ser)
- G169 (= G149) 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)
34% identity, 79% coverage: 27:429/512 of query aligns to 81:512/716 of P11544
- A211 (= A147) modified: Crosslink with 213, 5-imidazolinone (Ala-Gly)
- S212 (= S148) modified: 2,3-didehydroalanine (Ser)
- G213 (= G149) modified: Crosslink with 211, 5-imidazolinone (Ala-Gly)
- K468 (≠ M385) binding
- E496 (≠ S413) binding
P0DO55 Phenylalanine/tyrosine ammonia-lyase 1; FuPAL1; EC 4.3.1.25 from Fritillaria unibracteata (Sichuan fritillary) (see paper)
32% identity, 83% coverage: 28:454/512 of query aligns to 84:531/722 of P0DO55
- F141 (≠ S87) mutation to H: Increased activity toward L-tyrosine (L-Tyr) but reduced ability to use L-phenylalanine (L-Phe) as substrate.
- S208 (≠ A147) mutation to A: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- I218 (≠ M157) mutation to P: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- E490 (≠ N415) 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)
30% identity, 90% coverage: 28:486/512 of query aligns to 80:558/716 of P24481
- S203 (= S148) modified: 2,3-didehydroalanine (Ser); mutation to A: Complete loss of activity.
- S210 (≠ A155) mutation to A: No loss of activity.
Query Sequence
>Ac3H11_2558 FitnessBrowser__acidovorax_3H11:Ac3H11_2558
MTHNASSLTLHPGRVTLAELRRIHAGPVQLVLDASARAGLQKSLATVQRIVDEDQVVYGI
NTGFGKLASTKIAHERLAELQRNLVLSHSVGTGDPLPDDVVRLILATKAVSLARGHSGVR
PELVDALLALANANVLPVIPAKGSVGASGDLAPLAHMACVLIGEGQAKVDGKVVPGAEAM
RSIGLQPFVLGPKEGLALLNGTQVSTALALAGLFGAESVFSAALVAGCLSLEAIKGSVKP
FDARIHEARGQAGQIAVAAAVRALLDGSAIDPSHPHCGRVQDPYSIRCVPQVMGACLDNL
HHAARVLTIEANAASDNPLVFDNGDVISGGNFHAEPVAFVADIIALAVAEIGAISERRLS
LLLDPGLSGLPAFLIRDSGVNSGFMIAQVTAAALAAENQCLANPSSVTSLPTSANQEDHV
SMATYGARRLGDMVRNAAVMVGIEAMAAAQGMEFDRSLKSSPLIEAQFAAIRERVAYLEQ
DRYLAPDIEAMRAWAQQSTWPAALTQCLPSFA
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