SitesBLAST
Comparing BWI76_RS08740 FitnessBrowser__Koxy:BWI76_RS08740 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)
79% identity, 100% coverage: 1:505/507 of query aligns to 1:504/510 of P21310
- M1 (= M1) modified: Initiator methionine, Removed
- S144 (= S144) modified: 2,3-didehydroalanine (Ser); mutation S->A,T: Complete loss of activity.; mutation to C: No effect.
1gkmA Histidine ammonia-lyase (hal) from pseudomonas putida inhibited with l-cysteine (see paper)
79% identity, 99% coverage: 4:505/507 of query aligns to 3:501/507 of 1gkmA
- active site: Y53 (= Y54), G60 (= G61), H83 (= H84), N193 (= N197), Y278 (= Y282), R281 (= R285), F327 (= F331), E412 (= E416)
- binding cysteine: G142 (= G145), L189 (= L193), N193 (= N197), F327 (= F331)
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
44% identity, 95% coverage: 11:494/507 of query aligns to 121:607/657 of P21213
- S254 (= S144) mutation to A: Complete loss of activity.
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
44% identity, 92% coverage: 43:507/507 of query aligns to 169:633/677 of Q20502
- D536 (= D407) 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)
35% identity, 94% coverage: 11:488/507 of query aligns to 20:515/539 of Q8GMG0
- Y63 (= Y54) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ L62) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H84) binding ; mutation to F: Complete loss of activity.
- A152 (= A143) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S144) modified: 2,3-didehydroalanine (Ser)
- G154 (= G145) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N197) binding
- Y303 (≠ K277) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- R311 (= R285) binding
- Y415 (≠ V388) mutation to V: Complete loss of activity.
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, 84% coverage: 54:480/507 of query aligns to 51:495/531 of Q0VZ68
- F57 (= F60) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ LAQTRI 63:68) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ LSHA 82:85) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ LSHAA 82:86) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ A188) mutation to R: Gain of aminomutase activity.
- K242 (≠ R246) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. gap) mutation Missing: Total loss of aminomutase activity.
- P377 (≠ S364) mutation to R: No effect.
- C396 (≠ S381) mutation to S: No effect.
- E399 (≠ M384) 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. 384:391, 25% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 412:418, 14% identical) mutation to SAGREDH: Total loss of aminomutase activity.; mutation to SANQEDH: Total loss of aminomutase activity.
2rjsA Sgtam bound to substrate mimic (see paper)
35% identity, 94% coverage: 11:488/507 of query aligns to 9:502/526 of 2rjsA
- active site: Y52 (= Y54), G59 (= G61), H82 (= H84), N192 (= N197), Y295 (= Y282), R298 (= R285), F343 (= F331), Q429 (≠ E416)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y54), G59 (= G61), H82 (= H84), G141 (= G145), L143 (= L147), N192 (= N197), Y295 (= Y282), R298 (= R285), F343 (= F331), Q429 (≠ E416)
2rjrA Substrate mimic bound to sgtam (see paper)
35% identity, 94% coverage: 11:488/507 of query aligns to 9:502/526 of 2rjrA
- active site: Y52 (= Y54), G59 (= G61), H82 (= H84), N192 (= N197), Y295 (= Y282), R298 (= R285), F343 (= F331), Q429 (≠ E416)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y54), G59 (= G61), H82 (= H84), G141 (= G145), L143 (= L147), N192 (= N197), F343 (= F331), Q429 (≠ E416)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
35% identity, 94% coverage: 11:488/507 of query aligns to 9:502/526 of 2qveA
- active site: Y52 (= Y54), G59 (= G61), H82 (= H84), N192 (= N197), Y295 (= Y282), R298 (= R285), F343 (= F331), Q429 (≠ E416)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y54), G59 (= G61), H82 (= H84), G141 (= G145), L143 (= L147), N192 (= N197), Y295 (= Y282), R298 (= R285), F343 (= F331), Q429 (≠ E416)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
35% identity, 94% coverage: 11:488/507 of query aligns to 10:503/527 of 3kdzA
- active site: F53 (≠ Y54), G60 (= G61), H83 (= H84), N193 (= N197), Y296 (= Y282), R299 (= R285), F344 (= F331), Q430 (≠ E416)
- binding tyrosine: F53 (≠ Y54), Y59 (≠ F60), G60 (= G61), H83 (= H84), G142 (= G145), N193 (= N197), Y296 (= Y282), R299 (= R285), F344 (= F331)
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
32% identity, 92% coverage: 22:489/507 of query aligns to 23:502/514 of 3unvA
- active site: Y53 (= Y54), G60 (= G61), V83 (≠ H84), L191 (= L195), D291 (= D280), S294 (= S283), G340 (= G329), D427 (≠ N414)
- binding phenylalanine: Y53 (= Y54), G60 (= G61), G142 (= G145), L144 (= L147), N326 (= N315), F342 (= F331)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y54), G60 (= G61), G142 (= G145), N193 (= N197), N326 (= N315), F342 (= F331)
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
37% identity, 94% coverage: 10:487/507 of query aligns to 10:502/515 of 2o7dA
- active site: Y54 (= Y54), G61 (= G61), L84 (≠ H84), N195 (= N197), Y292 (= Y282), R295 (= R285), F342 (= F331), Q428 (≠ E416)
- binding caffeic acid: G61 (= G61), H83 (≠ S83), L84 (≠ H84), Y292 (= Y282), R295 (= R285), N424 (≠ S412), N427 (≠ Q415), Q428 (≠ E416)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
37% identity, 94% coverage: 10:487/507 of query aligns to 10:502/515 of 2o7eA
- active site: Y54 (= Y54), G61 (= G61), L84 (≠ H84), N195 (= N197), Y292 (= Y282), R295 (= R285), F342 (= F331), Q428 (≠ E416)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y54), G143 (= G145), L145 (= L147), N195 (= N197), Y292 (= Y282), R295 (= R285), N325 (= N315), F342 (= F331)
P0DO55 Phenylalanine/tyrosine ammonia-lyase 1; FuPAL1; EC 4.3.1.25 from Fritillaria unibracteata (Sichuan fritillary) (see paper)
31% identity, 88% coverage: 11:454/507 of query aligns to 70:532/722 of P0DO55
- F141 (≠ S83) mutation to H: Increased activity toward L-tyrosine (L-Tyr) but reduced ability to use L-phenylalanine (L-Phe) as substrate.
- S208 (≠ A143) mutation to A: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- I218 (≠ M153) mutation to P: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- E490 (≠ S412) mutation to N: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
6s7qA Crystal structure of ergothioneine degrading enzyme ergothionase from treponema denticola in complex with desmethyl-ergothioneine sulfonic acid (see paper)
27% identity, 98% coverage: 2:499/507 of query aligns to 1:494/497 of 6s7qA
- active site: Y53 (= Y54), G60 (= G61), D275 (= D280), A324 (≠ G329)
- binding (2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic acid: Y53 (= Y54), V59 (≠ F60), G60 (= G61), S194 (≠ N197), F326 (= F331), T380 (≠ I385), K383 (≠ V388), E411 (= E416)
P24481 Phenylalanine ammonia-lyase 1; EC 4.3.1.24 from Petroselinum crispum (Parsley) (Petroselinum hortense) (see paper)
32% identity, 89% coverage: 5:454/507 of query aligns to 63:526/716 of P24481
- S203 (= S144) modified: 2,3-didehydroalanine (Ser); mutation to A: Complete loss of activity.
- S210 (≠ A151) mutation to A: No loss of activity.
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: 35:454/507 of query aligns to 59:490/567 of Q3M5Z3
- L108 (≠ H84) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (= A143) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S144) modified: 2,3-didehydroalanine (Ser)
- G169 (= G145) 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.
6hqfA Structure of phenylalanine ammonia-lyase from petroselinum crispum in complex with (r)-apep
32% identity, 89% coverage: 5:454/507 of query aligns to 39:488/673 of 6hqfA
- active site: Y86 (= Y54), G93 (= G61), Y313 (= Y282), F362 (= F331)
- binding [(1R)-1-amino-2-phenylethyl]phosphonic acid: Y86 (= Y54), F92 (= F60), G178 (= G145), L180 (= L147), N234 (= N197), N346 (= N315), F362 (= F331), E446 (≠ S412)
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)
31% identity, 93% coverage: 24:497/507 of query aligns to 49:533/687 of Q68G84
- Y80 (= Y54) active site, Proton donor/acceptor; mutation Y->A,F: Abolishes enzyme activity.
- A175 (= A143) modified: Crosslink with 177, 5-imidazolinone (Ala-Gly)
- S176 (= S144) modified: 2,3-didehydroalanine (Ser)
- G177 (= G145) modified: Crosslink with 175, 5-imidazolinone (Ala-Gly)
- N231 (= N197) 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 (= Q279) 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 (= Y282) 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 (= R285) 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 (= N315) binding ; mutation to X: Abolishes enzyme activity; when associated with X-231.
- F371 (= F331) mutation to X: Abolishes enzyme activity; when associated with X-322.
- N458 (≠ Q415) binding
6f6tB Phenylalanine ammonia-lyase (pal) from petroselinum crispum complexed with s-appa
32% identity, 85% coverage: 24:454/507 of query aligns to 57:489/677 of 6f6tB
Query Sequence
>BWI76_RS08740 FitnessBrowser__Koxy:BWI76_RS08740
MNALTLIPGQLSLSQLRDVYSQPLKLALDESAFAAIDDSVACVNAILAEGRTAYGINTGF
GLLAQTRISTEDLENLQRSLVLSHAAGVGEPLDDDLARLIMVLKINSLSRGFSGIRLSVI
QALIGLVNAGVTPWIPAKGSVGASGDLAPLAHMSLTLLGEGKARVRGGEWLPATEALRQA
GLEPITLAAKEGLALLNGTQASTAFALRGLFEAEDLFSSAVVCGALTTEAALGSRRPFDP
RIHEARGQRGQIDAAALYRHLLTDDSAISQSHHNCTKVQDPYSLRCQPQVMGACLTQLRQ
AAEVLLVEANAVSDNPLVFASENDVISGGNFHAEPVAMAADNIALAIAEIGSLSERRIAL
MMDSHMSQLPPFLVKNGGVNSGFMIAQVTAAALASENKALSHPHSVDSLPTSANQEDHVS
MAPAAGRRLWAMAENTRGVLAVEWLASVQGLDMREGLTSSPLLEEARHLLRERVTHYTED
RFFAPDIENAIALLAARHLTRLLPAVL
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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