SitesBLAST
Comparing BPHYT_RS07555 FitnessBrowser__BFirm:BPHYT_RS07555 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)
P21310 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 4 papers)
64% identity, 99% coverage: 1:499/506 of query aligns to 4:503/510 of P21310
- S144 (= S141) 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)
63% identity, 99% coverage: 1:499/506 of query aligns to 3:500/507 of 1gkmA
- active site: Y53 (= Y51), G60 (= G58), H83 (= H81), N193 (= N193), Y278 (= Y277), R281 (= R280), F327 (= F326), E412 (= E411)
- binding cysteine: G142 (= G142), L189 (= L189), N193 (= N193), F327 (= F326)
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
44% identity, 97% coverage: 8:498/506 of query aligns to 121:616/657 of P21213
- S254 (= S141) mutation to A: Complete loss of activity.
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
42% identity, 97% coverage: 6:496/506 of query aligns to 134:630/677 of Q20502
- D536 (= D402) 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)
39% identity, 94% coverage: 8:485/506 of query aligns to 20:517/539 of Q8GMG0
- Y63 (= Y51) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ R59) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H81) binding ; mutation to F: Complete loss of activity.
- A152 (= A140) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S141) modified: 2,3-didehydroalanine (Ser)
- G154 (= G142) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N193) 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 (= R280) binding
- Y415 (≠ V383) mutation to V: Complete loss of activity.
2rjsA Sgtam bound to substrate mimic (see paper)
39% identity, 94% coverage: 8:485/506 of query aligns to 9:504/526 of 2rjsA
- active site: Y52 (= Y51), G59 (= G58), H82 (= H81), N192 (= N193), Y295 (= Y277), R298 (= R280), F343 (= F326), Q429 (≠ E411)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y51), G59 (= G58), H82 (= H81), G141 (= G142), L143 (= L144), N192 (= N193), Y295 (= Y277), R298 (= R280), F343 (= F326), Q429 (≠ E411)
2rjrA Substrate mimic bound to sgtam (see paper)
39% identity, 94% coverage: 8:485/506 of query aligns to 9:504/526 of 2rjrA
- active site: Y52 (= Y51), G59 (= G58), H82 (= H81), N192 (= N193), Y295 (= Y277), R298 (= R280), F343 (= F326), Q429 (≠ E411)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y51), G59 (= G58), H82 (= H81), G141 (= G142), L143 (= L144), N192 (= N193), F343 (= F326), Q429 (≠ E411)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
39% identity, 94% coverage: 8:485/506 of query aligns to 9:504/526 of 2qveA
- active site: Y52 (= Y51), G59 (= G58), H82 (= H81), N192 (= N193), Y295 (= Y277), R298 (= R280), F343 (= F326), Q429 (≠ E411)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y51), G59 (= G58), H82 (= H81), G141 (= G142), L143 (= L144), N192 (= N193), Y295 (= Y277), R298 (= R280), F343 (= F326), Q429 (≠ E411)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
38% identity, 94% coverage: 8:485/506 of query aligns to 10:505/527 of 3kdzA
- active site: F53 (≠ Y51), G60 (= G58), H83 (= H81), N193 (= N193), Y296 (= Y277), R299 (= R280), F344 (= F326), Q430 (≠ E411)
- binding tyrosine: F53 (≠ Y51), Y59 (≠ F57), G60 (= G58), H83 (= H81), G142 (= G142), N193 (= N193), Y296 (= Y277), R299 (= R280), F344 (= F326)
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, 94% coverage: 1:475/506 of query aligns to 1:495/531 of Q0VZ68
- F57 (= F57) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ LASTHI 60:65) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ LSHA 79:82) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ LSHAV 79:83) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ Q184) mutation to R: Gain of aminomutase activity.
- K242 (≠ R242) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. gap) mutation Missing: Total loss of aminomutase activity.
- P377 (≠ A359) mutation to R: No effect.
- C396 (≠ S376) mutation to S: No effect.
- E399 (≠ M379) 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. 379:386, 13% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 407:413, 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)
39% identity, 92% coverage: 32:494/506 of query aligns to 32:515/515 of 2o7dA
- active site: Y54 (= Y51), G61 (= G58), L84 (≠ H81), N195 (= N193), Y292 (= Y277), R295 (= R280), F342 (= F326), Q428 (≠ E411)
- binding caffeic acid: G61 (= G58), H83 (≠ S80), L84 (≠ H81), Y292 (= Y277), R295 (= R280), N424 (≠ S407), N427 (≠ Q410), Q428 (≠ E411)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
39% identity, 92% coverage: 32:494/506 of query aligns to 32:515/515 of 2o7eA
- active site: Y54 (= Y51), G61 (= G58), L84 (≠ H81), N195 (= N193), Y292 (= Y277), R295 (= R280), F342 (= F326), Q428 (≠ E411)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y51), G143 (= G142), L145 (= L144), N195 (= N193), Y292 (= Y277), R295 (= R280), N325 (= N310), F342 (= F326)
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
31% identity, 95% coverage: 8:489/506 of query aligns to 10:507/514 of 3unvA
- active site: Y53 (= Y51), G60 (= G58), V83 (≠ H81), L191 (= L191), D291 (= D275), S294 (= S278), G340 (= G324), D427 (≠ N409)
- binding phenylalanine: Y53 (= Y51), G60 (= G58), G142 (= G142), L144 (= L144), N326 (= N310), F342 (= F326)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y51), G60 (= G58), G142 (= G142), N193 (= N193), N326 (= N310), F342 (= F326)
6s7qA Crystal structure of ergothioneine degrading enzyme ergothionase from treponema denticola in complex with desmethyl-ergothioneine sulfonic acid (see paper)
29% identity, 97% coverage: 1:490/506 of query aligns to 5:490/497 of 6s7qA
- active site: Y53 (= Y51), G60 (= G58), D275 (= D275), A324 (≠ G324)
- binding (2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic acid: Y53 (= Y51), V59 (≠ F57), G60 (= G58), S194 (≠ N193), F326 (= F326), T380 (≠ I380), K383 (≠ V383), E411 (= E411)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
33% identity, 92% coverage: 8:471/506 of query aligns to 33:521/567 of Q3M5Z3
- L108 (≠ H81) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (= A140) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S141) modified: 2,3-didehydroalanine (Ser)
- G169 (= G142) 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.
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)
33% identity, 91% coverage: 8:465/506 of query aligns to 35:510/698 of Q6GZ04
- Y80 (= Y51) mutation to F: Abolishes enzyme activity.
- L104 (= L77) mutation to A: Decreases enzyme activity.
- Q319 (= Q274) binding
- R325 (= R280) 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)
33% identity, 91% coverage: 8:465/506 of query aligns to 35:510/687 of Q68G84
- Y80 (= Y51) active site, Proton donor/acceptor; mutation Y->A,F: Abolishes enzyme activity.
- A175 (= A140) modified: Crosslink with 177, 5-imidazolinone (Ala-Gly)
- S176 (= S141) modified: 2,3-didehydroalanine (Ser)
- G177 (= G142) modified: Crosslink with 175, 5-imidazolinone (Ala-Gly)
- N231 (= N193) 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 (= Q274) 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 (= Y277) 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 (= R280) 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 (= N310) binding ; mutation to X: Abolishes enzyme activity; when associated with X-231.
- F371 (= F326) mutation to X: Abolishes enzyme activity; when associated with X-322.
- N458 (≠ Q410) binding
P0DO55 Phenylalanine/tyrosine ammonia-lyase 1; FuPAL1; EC 4.3.1.25 from Fritillaria unibracteata (Sichuan fritillary) (see paper)
31% identity, 87% coverage: 8:449/506 of query aligns to 70:532/722 of P0DO55
- F141 (≠ S80) mutation to H: Increased activity toward L-tyrosine (L-Tyr) but reduced ability to use L-phenylalanine (L-Phe) as substrate.
- S208 (≠ A140) mutation to A: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- I218 (≠ M150) mutation to P: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- E490 (≠ S407) mutation to N: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
5ltmB Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis (y78f-c503s-c565s) bound to cinnamate (see paper)
32% identity, 92% coverage: 8:471/506 of query aligns to 9:495/537 of 5ltmB
- active site: F54 (≠ Y51), G61 (= G58), L84 (≠ H81), N197 (= N193), Y288 (= Y277), R291 (= R280), F337 (= F326), Q426 (≠ H413)
- binding hydrocinnamic acid: F60 (= F57), A143 (= A140), L145 (= L144), Y288 (= Y277), R291 (= R280)
4c5sC Structural investigations into the stereochemistry and activity of a phenylalanine-2,3-aminomutase from taxus chinensis (see paper)
33% identity, 91% coverage: 8:465/506 of query aligns to 27:492/642 of 4c5sC
- active site: A71 (≠ Y51), G78 (= G58), L99 (≠ H81), N213 (= N193), Y304 (= Y277), R307 (= R280), F353 (= F326), Q441 (≠ E411)
- binding (3S)-3-amino-2,2-difluoro-3-phenylpropanoic acid: G78 (= G58), G159 (= G142), L161 (= L144), N213 (= N193), Y304 (= Y277), R307 (= R280), N337 (= N310), F353 (= F326), E437 (≠ S407)
Query Sequence
>BPHYT_RS07555 FitnessBrowser__BFirm:BPHYT_RS07555
MTLKPGYLTLPQLRQIAREHVALQLDPASHAAIDACAQAVADIAAKGEPAYGINTGFGRL
ASTHIPHDQLELLQRNLVLSHAVGVGEPMSRPVVRLLIALKLSSLGRGHSGIRREVMEAL
ITLYNADVLPVIPVKGSVGASGDLAPLAHMSATLLGVGEVFAKGERMPATEGLALVGLKP
LTLQAKEGLALLNGTQASTALALYNMFAIEDLYRTALVSGALSVDAAMGSVKPFDARIHE
LRGHQGQIDAAGAYRSLLQGSGINVSHADCDKVQDPYSLRCQPQVMGACLDQMRHAANVL
LLEANAVSDNPLIFPDTGEVLSGGNFHAEPVAFAADNLALAAAEIGALAERRIALLIDAT
LSGLPPFLVRDGGVNSGFMIAHVTAAALASENKTLAHPASVDSLPTSANQEDHVSMATFA
ARKLGDIAENTANILSIELLAAAQGVDLRAPHKTSPSLQKVMDAVRKDVAHYELDHYFAP
DIAAVTRLVQDGTIAKLSPLSFASEQ
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