SitesBLAST
Comparing 5209827 FitnessBrowser__PV4:5209827 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)
6s7qA Crystal structure of ergothioneine degrading enzyme ergothionase from treponema denticola in complex with desmethyl-ergothioneine sulfonic acid (see paper)
37% identity, 94% coverage: 30:549/552 of query aligns to 1:489/497 of 6s7qA
- active site: Y53 (= Y81), G60 (= G88), D275 (= D313), A324 (≠ T380)
- binding (2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic acid: Y53 (= Y81), V59 (= V87), G60 (= G88), S194 (= S232), F326 (= F382), T380 (≠ A436), K383 (= K439), E411 (= E467)
1gkmA Histidine ammonia-lyase (hal) from pseudomonas putida inhibited with l-cysteine (see paper)
28% identity, 86% coverage: 78:551/552 of query aligns to 50:492/507 of 1gkmA
- active site: Y53 (= Y81), G60 (= G88), H83 (= H121), N193 (≠ S232), Y278 (≠ L315), R281 (= R318), F327 (= F382), E412 (= E467)
- binding cysteine: G142 (≠ A181), L189 (= L228), N193 (≠ S232), F327 (= F382)
P21310 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 4 papers)
28% identity, 86% coverage: 78:551/552 of query aligns to 51:495/510 of P21310
- S144 (≠ E180) 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
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)
26% identity, 94% coverage: 32:551/552 of query aligns to 13:523/539 of Q8GMG0
- Y63 (= Y81) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ K94) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H121) binding ; mutation to F: Complete loss of activity.
- A152 (vs. gap) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (≠ E180) modified: 2,3-didehydroalanine (Ser)
- G154 (≠ A181) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (≠ S232) binding
- Y303 (≠ P310) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- R311 (= R318) binding
- Y415 (≠ K439) mutation to V: Complete loss of activity.
2rjsA Sgtam bound to substrate mimic (see paper)
26% identity, 94% coverage: 32:551/552 of query aligns to 2:510/526 of 2rjsA
- active site: Y52 (= Y81), G59 (= G88), H82 (= H121), N192 (≠ S232), Y295 (≠ L315), R298 (= R318), F343 (= F382), Q429 (≠ E467)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y81), G59 (= G88), H82 (= H121), G141 (≠ A181), L143 (≠ I183), N192 (≠ S232), Y295 (≠ L315), R298 (= R318), F343 (= F382), Q429 (≠ E467)
2rjrA Substrate mimic bound to sgtam (see paper)
26% identity, 94% coverage: 32:551/552 of query aligns to 2:510/526 of 2rjrA
- active site: Y52 (= Y81), G59 (= G88), H82 (= H121), N192 (≠ S232), Y295 (≠ L315), R298 (= R318), F343 (= F382), Q429 (≠ E467)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y81), G59 (= G88), H82 (= H121), G141 (≠ A181), L143 (≠ I183), N192 (≠ S232), F343 (= F382), Q429 (≠ E467)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
26% identity, 94% coverage: 32:551/552 of query aligns to 2:510/526 of 2qveA
- active site: Y52 (= Y81), G59 (= G88), H82 (= H121), N192 (≠ S232), Y295 (≠ L315), R298 (= R318), F343 (= F382), Q429 (≠ E467)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y81), G59 (= G88), H82 (= H121), G141 (≠ A181), L143 (≠ I183), N192 (≠ S232), Y295 (≠ L315), R298 (= R318), F343 (= F382), Q429 (≠ E467)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
26% identity, 94% coverage: 32:551/552 of query aligns to 3:511/527 of 3kdzA
- active site: F53 (≠ Y81), G60 (= G88), H83 (= H121), N193 (≠ S232), Y296 (≠ L315), R299 (= R318), F344 (= F382), Q430 (≠ E467)
- binding tyrosine: F53 (≠ Y81), Y59 (≠ V87), G60 (= G88), H83 (= H121), G142 (≠ A181), N193 (≠ S232), Y296 (≠ L315), R299 (= R318), F344 (= F382)
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
25% identity, 79% coverage: 107:544/552 of query aligns to 69:502/514 of 3unvA
- active site: V83 (≠ H121), L191 (≠ I230), D291 (= D313), S294 (= S316), G340 (≠ T380), D427 (≠ N465)
- binding phenylalanine: G142 (≠ A181), L144 (≠ I183), N326 (= N348), F342 (= F382)
- binding (3S)-3-amino-3-phenylpropanoic acid: G142 (≠ A181), N193 (≠ S232), N326 (= N348), F342 (= F382)
Sites not aligning to the query:
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
22% identity, 94% coverage: 32:550/552 of query aligns to 114:608/657 of P21213
- S254 (≠ E180) 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)
22% identity, 90% coverage: 51:549/552 of query aligns to 21:509/531 of Q0VZ68
- F57 (≠ V87) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ -----L 89) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ RAHS 119:122) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ RAHSA 119:123) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ I223) mutation to R: Gain of aminomutase activity.
- K242 (≠ Q276) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. 298:308, 14% identical) mutation Missing: Total loss of aminomutase activity.
- P377 (≠ D415) mutation to R: No effect.
- C396 (≠ H432) mutation to S: No effect.
- E399 (≠ G435) 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. 435:442, 13% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 463:469, 29% 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)
23% identity, 94% coverage: 32:549/552 of query aligns to 130:623/677 of Q20502
- D536 (= D458) mutation to N: In am130; causes strong resistance to nickel and zinc toxicity.
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
26% identity, 93% coverage: 32:544/552 of query aligns to 5:504/515 of 2o7eA
- active site: Y54 (= Y81), G61 (= G88), L84 (vs. gap), N195 (≠ S232), Y292 (≠ L315), R295 (= R318), F342 (= F382), Q428 (≠ E467)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y81), G143 (≠ A181), L145 (≠ I183), N195 (≠ S232), Y292 (≠ L315), R295 (= R318), N325 (= N348), F342 (= F382)
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
26% identity, 93% coverage: 32:544/552 of query aligns to 5:504/515 of 2o7dA
- active site: Y54 (= Y81), G61 (= G88), L84 (vs. gap), N195 (≠ S232), Y292 (≠ L315), R295 (= R318), F342 (= F382), Q428 (≠ E467)
- binding caffeic acid: G61 (= G88), H83 (vs. gap), L84 (vs. gap), Y292 (≠ L315), R295 (= R318), N424 (≠ A463), N427 (≠ I466), Q428 (≠ E467)
B2J528 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
26% identity, 58% coverage: 30:349/552 of query aligns to 36:348/569 of B2J528
- A167 (vs. gap) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (≠ E180) modified: 2,3-didehydroalanine (Ser)
- G169 (≠ A181) modified: Crosslink with 167, 5-imidazolinone (Ala-Gly)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
24% identity, 55% coverage: 68:372/552 of query aligns to 65:371/567 of Q3M5Z3
- L108 (= L118) 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 (≠ E180) modified: 2,3-didehydroalanine (Ser)
- G169 (≠ A181) 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.
5ltmB Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis (y78f-c503s-c565s) bound to cinnamate (see paper)
24% identity, 55% coverage: 68:372/552 of query aligns to 41:345/537 of 5ltmB
- active site: F54 (≠ Y81), G61 (= G88), L84 (≠ H121), N197 (≠ S232), Y288 (≠ L315), R291 (= R318), F337 (≠ Q364)
- binding hydrocinnamic acid: F60 (≠ V87), A143 (= A181), L145 (≠ I183), Y288 (≠ L315), R291 (= R318)
Sites not aligning to the query:
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)
24% identity, 58% coverage: 32:349/552 of query aligns to 27:356/698 of Q6GZ04
- Y80 (= Y81) mutation to F: Abolishes enzyme activity.
- L104 (≠ A109) mutation to A: Decreases enzyme activity.
- Q319 (= Q312) binding
- R325 (= R318) 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)
24% identity, 58% coverage: 32:349/552 of query aligns to 27:356/687 of Q68G84
- Y80 (= Y81) active site, Proton donor/acceptor; mutation Y->A,F: Abolishes enzyme activity.
- A175 (≠ G179) modified: Crosslink with 177, 5-imidazolinone (Ala-Gly)
- S176 (≠ E180) modified: 2,3-didehydroalanine (Ser)
- G177 (≠ A181) modified: Crosslink with 175, 5-imidazolinone (Ala-Gly)
- N231 (≠ S232) 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 (= Q312) 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 (≠ L315) 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 (= R318) 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 (= N348) binding ; mutation to X: Abolishes enzyme activity; when associated with X-231.
Sites not aligning to the query:
- 371 F→X: Abolishes enzyme activity; when associated with X-322.
- 458 binding
4c5sC Structural investigations into the stereochemistry and activity of a phenylalanine-2,3-aminomutase from taxus chinensis (see paper)
26% identity, 58% coverage: 32:349/552 of query aligns to 19:338/642 of 4c5sC
- active site: A71 (≠ Y81), G78 (= G88), L99 (≠ H121), N213 (≠ S232), Y304 (≠ L315), R307 (= R318)
- binding (3S)-3-amino-2,2-difluoro-3-phenylpropanoic acid: G78 (= G88), G159 (≠ E180), L161 (≠ D182), N213 (≠ S232), Y304 (≠ L315), R307 (= R318), N337 (= N348)
Sites not aligning to the query:
Query Sequence
>5209827 FitnessBrowser__PV4:5209827
MMKKVNTLLATTALATSALAMTSGAAMASDTVVLDGQHLTQAQAWAIADGAKVDIAPQAA
SALVKAHDLLMEAARLGKPVYGLTVGVGLNKDHKLFDANGELSAEVMAASKSFNYSTLRA
HSAGVGEPMPVRLTRVALAVRLNTILSGHTGVQPYVAEIYQAYLNQGITPVIPSLGTVGE
ADILLASHVGLAMIGEWDVFYQGKRMSSVEAMSKAGVKPLKPIGKDALSILSNNSVAVAY
AMQGYQDAEHLLEVSPTVFGLSLEGLNGNVAPFLPQTNDIRPFPYLKATTEDILGSLSGS
YLWDLNSERPLQDPLSYRTTAYTLASAQKALSDLGQVIDIQINHSDDNPGVILGASKQYA
ENSQVAKYLVEGKGGVFPTTNFEPLPVALAVQQLSVALTHVSHNSAMRTIHLSDDHFTHL
PRFLSAPGNNGHAFGAIQKTFVDMQVRNKMLATPVSFDGIQIAGNIEDTFTNLKLASDNL
IQIVDNINTMYGLELLHSTQAIDLRKAANADLKLGKATQAMYQAYRQQVPFVELDRPFTP
DIQASHDFIVKY
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