SitesBLAST
Comparing BPHYT_RS15165 FitnessBrowser__BFirm:BPHYT_RS15165 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
38% identity, 85% coverage: 23:471/531 of query aligns to 3:468/531 of Q0VZ68
- F57 (≠ Y79) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ ACVVDV 82:87) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ RYHG 101:104) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ RYHGC 101:105) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ A206) mutation to R: Gain of aminomutase activity.
- K242 (= K264) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. gap) mutation Missing: Total loss of aminomutase activity.
- P377 (≠ V377) mutation to R: No effect.
- C396 (≠ H399) mutation to S: No effect.
- E399 (≠ K402) 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. 402:409, 13% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 430:436, 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, 87% coverage: 21:480/531 of query aligns to 13:488/539 of Q8GMG0
- Y63 (= Y73) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ D81) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H103) binding ; mutation to F: Complete loss of activity.
- A152 (= A162) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S163) modified: 2,3-didehydroalanine (Ser)
- G154 (= G164) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N215) binding
- Y303 (≠ R290) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- R311 (= R298) binding
- Y415 (≠ I406) mutation to V: Complete loss of activity.
2rjsA Sgtam bound to substrate mimic (see paper)
37% identity, 87% coverage: 21:480/531 of query aligns to 2:475/526 of 2rjsA
- active site: Y52 (= Y73), G59 (= G80), H82 (= H103), N192 (= N215), Y295 (= Y295), R298 (= R298), F343 (= F344), Q429 (= Q434)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y73), G59 (= G80), H82 (= H103), G141 (= G164), L143 (= L166), N192 (= N215), Y295 (= Y295), R298 (= R298), F343 (= F344), Q429 (= Q434)
2rjrA Substrate mimic bound to sgtam (see paper)
37% identity, 87% coverage: 21:480/531 of query aligns to 2:475/526 of 2rjrA
- active site: Y52 (= Y73), G59 (= G80), H82 (= H103), N192 (= N215), Y295 (= Y295), R298 (= R298), F343 (= F344), Q429 (= Q434)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y73), G59 (= G80), H82 (= H103), G141 (= G164), L143 (= L166), N192 (= N215), F343 (= F344), Q429 (= Q434)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
37% identity, 87% coverage: 21:480/531 of query aligns to 2:475/526 of 2qveA
- active site: Y52 (= Y73), G59 (= G80), H82 (= H103), N192 (= N215), Y295 (= Y295), R298 (= R298), F343 (= F344), Q429 (= Q434)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y73), G59 (= G80), H82 (= H103), G141 (= G164), L143 (= L166), N192 (= N215), Y295 (= Y295), R298 (= R298), F343 (= F344), Q429 (= Q434)
B2J528 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
36% identity, 86% coverage: 14:472/531 of query aligns to 19:490/569 of B2J528
- A167 (= A162) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S163) modified: 2,3-didehydroalanine (Ser)
- G169 (= G164) modified: Crosslink with 167, 5-imidazolinone (Ala-Gly)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
37% identity, 87% coverage: 21:480/531 of query aligns to 3:476/527 of 3kdzA
- active site: F53 (≠ Y73), G60 (= G80), H83 (= H103), N193 (= N215), Y296 (= Y295), R299 (= R298), F344 (= F344), Q430 (= Q434)
- binding tyrosine: F53 (≠ Y73), Y59 (= Y79), G60 (= G80), H83 (= H103), G142 (= G164), N193 (= N215), Y296 (= Y295), R299 (= R298), F344 (= F344)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
34% identity, 94% coverage: 19:518/531 of query aligns to 24:551/567 of Q3M5Z3
- L108 (≠ H103) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (= A162) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S163) modified: 2,3-didehydroalanine (Ser)
- G169 (= G164) 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.
5ltmB Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis (y78f-c503s-c565s) bound to cinnamate (see paper)
33% identity, 94% coverage: 21:518/531 of query aligns to 2:525/537 of 5ltmB
- active site: F54 (≠ Y73), G61 (= G80), L84 (≠ H103), N197 (= N215), Y288 (= Y295), R291 (= R298), F337 (= F344), Q426 (= Q434)
- binding hydrocinnamic acid: F60 (≠ Y79), A143 (= A162), L145 (= L166), Y288 (= Y295), R291 (= R298)
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
30% identity, 92% coverage: 25:512/531 of query aligns to 7:503/514 of 3unvA
- active site: Y53 (= Y73), G60 (= G80), V83 (≠ H103), L191 (= L213), D291 (= D293), S294 (= S296), G340 (= G342), D427 (≠ H432)
- binding phenylalanine: Y53 (= Y73), G60 (= G80), G142 (= G164), L144 (= L166), N326 (= N328), F342 (= F344)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y73), G60 (= G80), G142 (= G164), N193 (= N215), N326 (= N328), F342 (= F344)
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
33% identity, 87% coverage: 18:481/531 of query aligns to 111:576/657 of P21213
- S254 (= S163) mutation to A: Complete loss of activity.
P0DO55 Phenylalanine/tyrosine ammonia-lyase 1; FuPAL1; EC 4.3.1.25 from Fritillaria unibracteata (Sichuan fritillary) (see paper)
33% identity, 88% coverage: 6:472/531 of query aligns to 48:532/722 of P0DO55
- F141 (≠ Y102) mutation to H: Increased activity toward L-tyrosine (L-Tyr) but reduced ability to use L-phenylalanine (L-Phe) as substrate.
- S208 (≠ A162) mutation to A: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- I218 (≠ V172) mutation to P: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- E490 (= E430) mutation to N: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
37% identity, 84% coverage: 72:516/531 of query aligns to 53:509/515 of 2o7eA
- active site: Y54 (= Y73), G61 (= G80), L84 (≠ H103), N195 (= N215), Y292 (= Y295), R295 (= R298), F342 (= F344), Q428 (= Q434)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y73), G143 (= G164), L145 (= L166), N195 (= N215), Y292 (= Y295), R295 (= R298), N325 (= N328), F342 (= F344)
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
37% identity, 84% coverage: 72:516/531 of query aligns to 53:509/515 of 2o7dA
- active site: Y54 (= Y73), G61 (= G80), L84 (≠ H103), N195 (= N215), Y292 (= Y295), R295 (= R298), F342 (= F344), Q428 (= Q434)
- binding caffeic acid: G61 (= G80), H83 (≠ Y102), L84 (≠ H103), Y292 (= Y295), R295 (= R298), N424 (≠ E430), N427 (= N433), Q428 (= Q434)
P24481 Phenylalanine ammonia-lyase 1; EC 4.3.1.24 from Petroselinum crispum (Parsley) (Petroselinum hortense) (see paper)
32% identity, 89% coverage: 1:472/531 of query aligns to 37:526/716 of P24481
- S203 (= S163) modified: 2,3-didehydroalanine (Ser); mutation to A: Complete loss of activity.
- S210 (= S170) mutation to A: No loss of activity.
6hqfA Structure of phenylalanine ammonia-lyase from petroselinum crispum in complex with (r)-apep
33% identity, 89% coverage: 1:472/531 of query aligns to 13:488/673 of 6hqfA
- active site: Y86 (= Y73), G93 (= G80), Y313 (= Y295), F362 (= F344)
- binding [(1R)-1-amino-2-phenylethyl]phosphonic acid: Y86 (= Y73), F92 (≠ Y79), G178 (= G164), L180 (= L166), N234 (= N215), N346 (= N328), F362 (= F344), E446 (= E430)
6f6tB Phenylalanine ammonia-lyase (pal) from petroselinum crispum complexed with s-appa
33% identity, 89% coverage: 1:472/531 of query aligns to 14:489/677 of 6f6tB
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
33% identity, 93% coverage: 21:516/531 of query aligns to 130:623/677 of Q20502
- D536 (≠ F425) mutation to N: In am130; causes strong resistance to nickel and zinc toxicity.
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, 85% coverage: 22:472/531 of query aligns to 29:497/698 of Q6GZ04
- Y80 (= Y73) mutation to F: Abolishes enzyme activity.
- L104 (= L95) mutation to A: Decreases enzyme activity.
- Q319 (= Q292) binding
- R325 (= R298) 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)
35% identity, 88% coverage: 5:472/531 of query aligns to 13:497/687 of Q68G84
- Y80 (= Y73) active site, Proton donor/acceptor; mutation Y->A,F: Abolishes enzyme activity.
- A175 (= A162) modified: Crosslink with 177, 5-imidazolinone (Ala-Gly)
- S176 (= S163) modified: 2,3-didehydroalanine (Ser)
- G177 (= G164) modified: Crosslink with 175, 5-imidazolinone (Ala-Gly)
- N231 (= N215) 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 (= Q292) 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 (= Y295) 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 (= R298) 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 (= N328) binding ; mutation to X: Abolishes enzyme activity; when associated with X-231.
- F371 (= F344) mutation to X: Abolishes enzyme activity; when associated with X-322.
- N458 (= N433) binding
Query Sequence
>BPHYT_RS15165 FitnessBrowser__BFirm:BPHYT_RS15165
MAEHDLIDVPNAGANVNDAAVVIGGRKLTIEEVVAIAQHRAPVALSDDPAWRARIQRGAD
FLRRHLAAGATVYGVNTGYGDACVVDVPMELVEALPLQLTRYHGCGMGQYLDDAQTLAVI
AARLNSLAYGFSGVRPVLLERLADLVNHRVLPRIPSEGSVGASGDLTPLSYVAAALAGER
DVMFEGQLRNVREVWAELGHAPLTLAPKEGLALMNGTAVMTGLACLAFARADHLTRLTAR
LTALCTVALDGRAAHFDAMLFEVKPHAGQAEAAAWIRDDLSGRDDTPGHRLQDRYSIRCA
PHVIGVARDALSWVRRDVENELNSANDNPLIDPDNERVLHGGNFYGGHIAFAMDSLKVAV
ANLADLMDRQLALLVDVNFNNGLPRNLSGAAPARAAINHGFKAVQISSSAWTAEALKNTM
PASVFSRSTEAHNQDKVSMGTIAARDCLRVLELTEQVAAAHTLATVQAARLRLKIDSATP
VPAPLQAFMDSVGAQSPFVDEDRALEHELRALTARIAACDLASDSRGGPSA
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