SitesBLAST
Comparing RR42_RS16920 FitnessBrowser__Cup4G11:RR42_RS16920 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)
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 ; 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
- 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
- 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
- F57 (= F70) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ LAQTRI 73:78) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ LSHS 92:95) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ LSHSV 92:96) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (= G197) mutation to R: Gain of aminomutase activity.
- K242 (≠ R255) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. 281:284, 14% identical) mutation Missing: Total loss of aminomutase activity.
- P377 (≠ S372) mutation to R: No effect.
- C396 (≠ S389) mutation to S: No effect.
- E399 (≠ M392) 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. 392:399, 25% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 420:426, 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)
30% identity, 92% coverage: 21:502/526 of query aligns to 10:507/514 of 3unvA
- active site: Y53 (= Y64), G60 (= G71), V83 (≠ H94), L191 (= L204), D291 (= D288), S294 (= S291), G340 (= G337), D427 (≠ N422)
- binding phenylalanine: Y53 (= Y64), G60 (= G71), G142 (= G155), L144 (= L157), N326 (= N323), F342 (= F339)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y64), G60 (= G71), G142 (= G155), N193 (= N206), N326 (= N323), F342 (= F339)
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
38% identity, 87% coverage: 46:504/526 of query aligns to 36:511/515 of 2o7dA
- active site: Y54 (= Y64), G61 (= G71), L84 (≠ H94), N195 (= N206), Y292 (= Y290), R295 (= R293), F342 (= F339), Q428 (≠ E424)
- binding caffeic acid: G61 (= G71), H83 (≠ S93), L84 (≠ H94), Y292 (= Y290), R295 (= R293), N424 (≠ S420), N427 (≠ Q423), Q428 (≠ E424)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
38% identity, 87% coverage: 46:504/526 of query aligns to 36:511/515 of 2o7eA
- active site: Y54 (= Y64), G61 (= G71), L84 (≠ H94), N195 (= N206), Y292 (= Y290), R295 (= R293), F342 (= F339), Q428 (≠ E424)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y64), G143 (= G155), L145 (= L157), N195 (= N206), Y292 (= Y290), R295 (= R293), N325 (= N323), F342 (= F339)
6s7qA Crystal structure of ergothioneine degrading enzyme ergothionase from treponema denticola in complex with desmethyl-ergothioneine sulfonic acid (see paper)
28% identity, 93% coverage: 13:503/526 of query aligns to 4:490/497 of 6s7qA
- active site: Y53 (= Y64), G60 (= G71), D275 (= D288), A324 (≠ G337)
- binding (2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic acid: Y53 (= Y64), V59 (≠ F70), G60 (= G71), S194 (≠ N206), F326 (= F339), T380 (≠ I393), K383 (≠ V396), E411 (= E424)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
32% identity, 83% coverage: 20:453/526 of query aligns to 32:487/567 of Q3M5Z3
- L108 (≠ H94) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (= A153) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S154) modified: 2,3-didehydroalanine (Ser)
- G169 (= G155) 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.
B2J528 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
31% identity, 85% coverage: 8:453/526 of query aligns to 20:487/569 of B2J528
- A167 (= A153) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S154) modified: 2,3-didehydroalanine (Ser)
- G169 (= G155) 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)
31% identity, 83% coverage: 20:453/526 of query aligns to 8:461/537 of 5ltmB
- active site: F54 (≠ Y64), G61 (= G71), L84 (≠ H94), N197 (= N206), Y288 (= Y290), R291 (= R293), F337 (= F339), Q426 (≠ D425)
- binding hydrocinnamic acid: F60 (= F70), A143 (= A153), L145 (= L157), Y288 (= Y290), R291 (= R293)
P24481 Phenylalanine ammonia-lyase 1; EC 4.3.1.24 from Petroselinum crispum (Parsley) (Petroselinum hortense) (see paper)
30% identity, 85% coverage: 34:482/526 of query aligns to 80:547/716 of P24481
- S203 (= S154) modified: 2,3-didehydroalanine (Ser); mutation to A: Complete loss of activity.
- S210 (≠ A161) mutation to A: No loss of activity.
P0DO55 Phenylalanine/tyrosine ammonia-lyase 1; FuPAL1; EC 4.3.1.25 from Fritillaria unibracteata (Sichuan fritillary) (see paper)
29% identity, 91% coverage: 6:482/526 of query aligns to 55:553/722 of P0DO55
- F141 (≠ S93) mutation to H: Increased activity toward L-tyrosine (L-Tyr) but reduced ability to use L-phenylalanine (L-Phe) as substrate.
- S208 (≠ A153) mutation to A: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- I218 (≠ M163) mutation to P: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- E490 (≠ S420) mutation to N: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
6hqfA Structure of phenylalanine ammonia-lyase from petroselinum crispum in complex with (r)-apep
29% identity, 92% coverage: 34:519/526 of query aligns to 56:554/673 of 6hqfA
- active site: Y86 (= Y64), G93 (= G71), Y313 (= Y290), F362 (= F339)
- binding [(1R)-1-amino-2-phenylethyl]phosphonic acid: Y86 (= Y64), F92 (= F70), G178 (= G155), L180 (= L157), N234 (= N206), N346 (= N323), F362 (= F339), E446 (≠ S420)
Query Sequence
>RR42_RS16920 FitnessBrowser__Cup4G11:RR42_RS16920
MSATQANQTSRPLLTLQPGSVTLADLRRIHRGEVSLAMDASAWAGVRASQATVQDIIDAD
AVVYGINTGFGKLAQTRIPHDKLAELQRNLVLSHSVGTGADLHSDTVRLILAIKAVSLAR
GHSGIRPEIIEALLALTNAGVTPCIPAKGSVGASGDLAPLAHMSCTLIGVGEVMIDGVRR
PAAEGLAHAGLAPFTLGPKEGLALLNGTQVSTALALAGLFAAEDIFAAGLVAGALSLEAI
KGSVKPFDARIHAARGQAGQIAVAGAVRALLDGSKIVDSHVSCGRVQDPYSIRCQPQVMG
ACLDNLQHAARVLQIEANAASDNPLVFPEQGDVISGGNFHAEPVAFAADIIALAIAEIGA
ISERRLALLLDSGLSGLPPFLVRDGGLHSGFMIAQVTAAALASENKSLAHPASVDSLPTS
ANQEDHVSMATYGARRLGDMAENTAVVVGIEAMAAAQGIEFHRPLESSPLIESEIARIRE
RVAFVEGDRYFAPDIEAMKQWVQQGDAGAGWPEAVRQVLPSQVGVA
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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