SitesBLAST
Comparing SMa0306 FitnessBrowser__Smeli:SMa0306 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)
6s7qA Crystal structure of ergothioneine degrading enzyme ergothionase from treponema denticola in complex with desmethyl-ergothioneine sulfonic acid (see paper)
35% identity, 96% coverage: 25:546/546 of query aligns to 3:496/497 of 6s7qA
- active site: Y53 (= Y74), G60 (= G81), D275 (= D306), A324 (= A371)
- binding (2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic acid: Y53 (= Y74), V59 (= V80), G60 (= G81), S194 (= S225), F326 (= F373), T380 (≠ V426), K383 (≠ A429), E411 (= E457)
2rjsA Sgtam bound to substrate mimic (see paper)
32% identity, 93% coverage: 25:532/546 of query aligns to 2:501/526 of 2rjsA
- active site: Y52 (= Y74), G59 (= G81), H82 (= H114), N192 (≠ S225), Y295 (≠ L308), R298 (= R311), F343 (= F373), Q429 (≠ E457)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y74), G59 (= G81), H82 (= H114), G141 (≠ A174), L143 (≠ M176), N192 (≠ S225), Y295 (≠ L308), R298 (= R311), F343 (= F373), Q429 (≠ E457)
2rjrA Substrate mimic bound to sgtam (see paper)
32% identity, 93% coverage: 25:532/546 of query aligns to 2:501/526 of 2rjrA
- active site: Y52 (= Y74), G59 (= G81), H82 (= H114), N192 (≠ S225), Y295 (≠ L308), R298 (= R311), F343 (= F373), Q429 (≠ E457)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y74), G59 (= G81), H82 (= H114), G141 (≠ A174), L143 (≠ M176), N192 (≠ S225), F343 (= F373), Q429 (≠ E457)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
32% identity, 93% coverage: 25:532/546 of query aligns to 2:501/526 of 2qveA
- active site: Y52 (= Y74), G59 (= G81), H82 (= H114), N192 (≠ S225), Y295 (≠ L308), R298 (= R311), F343 (= F373), Q429 (≠ E457)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y74), G59 (= G81), H82 (= H114), G141 (≠ A174), L143 (≠ M176), N192 (≠ S225), Y295 (≠ L308), R298 (= R311), F343 (= F373), Q429 (≠ E457)
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)
32% identity, 93% coverage: 25:532/546 of query aligns to 13:514/539 of Q8GMG0
- Y63 (= Y74) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ N83) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H114) binding ; mutation to F: Complete loss of activity.
- A152 (≠ Q173) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (≠ A174) modified: 2,3-didehydroalanine (Ser)
- G154 (vs. gap) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (≠ S225) binding
- Y303 (≠ I303) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- R311 (= R311) binding
- Y415 (≠ A429) mutation to V: Complete loss of activity.
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
32% identity, 93% coverage: 25:532/546 of query aligns to 3:502/527 of 3kdzA
- active site: F53 (≠ Y74), G60 (= G81), H83 (= H114), N193 (≠ S225), Y296 (≠ L308), R299 (= R311), F344 (= F373), Q430 (≠ E457)
- binding tyrosine: F53 (≠ Y74), Y59 (≠ V80), G60 (= G81), H83 (= H114), G142 (≠ A174), N193 (≠ S225), Y296 (≠ L308), R299 (= R311), F344 (= F373)
P21310 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 4 papers)
29% identity, 92% coverage: 46:545/546 of query aligns to 26:499/510 of P21310
- S144 (≠ A174) 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)
29% identity, 92% coverage: 46:545/546 of query aligns to 25:496/507 of 1gkmA
- active site: Y53 (= Y74), G60 (= G81), H83 (= H114), N193 (≠ S225), Y278 (≠ L308), R281 (= R311), F327 (= F373), E412 (= E457)
- binding cysteine: G142 (≠ A174), L189 (= L221), N193 (≠ S225), F327 (= F373)
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
27% identity, 93% coverage: 28:534/546 of query aligns to 6:502/514 of 3unvA
- active site: Y53 (= Y74), G60 (= G81), V83 (≠ H114), L191 (≠ I223), D291 (= D306), S294 (= S309), G340 (= G360), D427 (≠ G455)
- binding phenylalanine: Y53 (= Y74), G60 (= G81), G142 (≠ A174), L144 (≠ M176), N326 (= N341), F342 (≠ V362)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y74), G60 (= G81), G142 (≠ A174), N193 (≠ S225), N326 (= N341), F342 (≠ V362)
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
26% identity, 94% coverage: 25:539/546 of query aligns to 114:607/657 of P21213
- S254 (≠ A174) mutation to A: 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)
27% identity, 89% coverage: 42:525/546 of query aligns to 19:495/531 of Q0VZ68
- F57 (≠ V80) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ LTPELM 95:100) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ RAHS 112:115) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ RAHSV 112:116) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ F216) mutation to R: Gain of aminomutase activity.
- K242 (≠ R274) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. 298:301, 7% identical) mutation Missing: Total loss of aminomutase activity.
- P377 (= P406) mutation to R: No effect.
- C396 (≠ H422) mutation to S: No effect.
- E399 (≠ L425) 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. 425:432, 0% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 453:459, 43% identical) mutation to SAGREDH: Total loss of aminomutase activity.; mutation to SANQEDH: Total loss of aminomutase activity.
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
26% identity, 95% coverage: 25:541/546 of query aligns to 130:625/677 of Q20502
- D536 (= D448) mutation to N: In am130; causes strong resistance to nickel and zinc toxicity.
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
27% identity, 88% coverage: 54:534/546 of query aligns to 34:504/515 of 2o7dA
- active site: Y54 (= Y74), G61 (= G81), L84 (≠ H114), N195 (≠ S225), Y292 (≠ L308), R295 (= R311), F342 (= F373), Q428 (≠ E457)
- binding caffeic acid: G61 (= G81), H83 (≠ A113), L84 (≠ H114), Y292 (≠ L308), R295 (= R311), N424 (≠ A453), N427 (≠ V456), Q428 (≠ E457)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
27% identity, 88% coverage: 54:534/546 of query aligns to 34:504/515 of 2o7eA
- active site: Y54 (= Y74), G61 (= G81), L84 (≠ H114), N195 (≠ S225), Y292 (≠ L308), R295 (= R311), F342 (= F373), Q428 (≠ E457)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y74), G143 (≠ A174), L145 (≠ M176), N195 (≠ S225), Y292 (≠ L308), R295 (= R311), N325 (= N341), F342 (= F373)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
27% identity, 60% coverage: 17:346/546 of query aligns to 18:352/567 of Q3M5Z3
- L108 (≠ H114) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (vs. gap) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (≠ Q173) modified: 2,3-didehydroalanine (Ser)
- G169 (≠ A174) 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)
28% identity, 63% coverage: 1:346/546 of query aligns to 1:352/569 of B2J528
- A167 (vs. gap) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (≠ Q173) modified: 2,3-didehydroalanine (Ser)
- G169 (≠ A174) 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)
27% identity, 59% coverage: 24:346/546 of query aligns to 1:326/537 of 5ltmB
Sites not aligning to the query:
P11544 Phenylalanine/tyrosine ammonia-lyase; Bifunctional phenylalanine ammonia-lyase; Bifunctional PAL; EC 4.3.1.25 from Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides) (see paper)
31% identity, 62% coverage: 16:352/546 of query aligns to 51:406/716 of P11544
- A211 (≠ G172) modified: Crosslink with 213, 5-imidazolinone (Ala-Gly)
- S212 (≠ Q173) modified: 2,3-didehydroalanine (Ser)
- G213 (≠ A174) modified: Crosslink with 211, 5-imidazolinone (Ala-Gly)
Sites not aligning to the query:
P0DO55 Phenylalanine/tyrosine ammonia-lyase 1; FuPAL1; EC 4.3.1.25 from Fritillaria unibracteata (Sichuan fritillary) (see paper)
26% identity, 92% coverage: 17:519/546 of query aligns to 58:553/722 of P0DO55
- F141 (≠ E105) mutation to H: Increased activity toward L-tyrosine (L-Tyr) but reduced ability to use L-phenylalanine (L-Phe) as substrate.
- S208 (≠ Q173) mutation to A: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- I218 (= I182) mutation to P: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- E490 (≠ A453) 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)
28% identity, 60% coverage: 63:390/546 of query aligns to 99:417/716 of P24481
- S203 (≠ Q173) modified: 2,3-didehydroalanine (Ser); mutation to A: Complete loss of activity.
- S210 (= S180) mutation to A: No loss of activity.
Query Sequence
>SMa0306 FitnessBrowser__Smeli:SMa0306
MRIDSLFHSVVGACLLFSSPVMADVLLNGRNATPEMIVRVAKGEAVTVDGESLDKVERAY
AVLLQGAKEGQEIYGLTVGVGWNKDRKMVDATGELTPELMEASREFNEGLLRAHSVGVGP
DAAVPVVRAAMAVRLNNILTGGPGVQPHVAEMLLAFLNKGITPTMPSRGSVGQADMTLLS
HIGLAMLGEGDVDYQGRRMSAAEALKAAGIEPLKPFGKDGLAILSSNAYAAGLAALAIHD
AEQLLSTSRLVYALSLEGLNGNVSPLLEDVAALRPFPSHLSSTTELRALLEGSYLWQADD
KRILQDPLSFRTAPYLLGSFADSLARTKALVQIQINSSDDNPGIVVGVEPKSDLFQARRG
YVEGGAVLPTANFEPLPWIIAFEELGIVLAHHTTASSERVLKLNNPTHTKLARYLGTENT
HHAFLVVEAPLMALATENRALAQPTSFDSRPIAGGVEDVGTNAPLVVERIRAQIDNSFTI
LSMEMLHAAQAADLRLKGHPERKLSTATTSFHDAFRQRVPFLDRDRSMTPDIAAGTAFLK
EYALTN
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