SitesBLAST
Comparing CCNA_01010 FitnessBrowser__Caulo:CCNA_01010 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)
54% identity, 99% coverage: 5:511/513 of query aligns to 1:510/510 of P21310
- M1 (≠ V5) modified: Initiator methionine, Removed
- S144 (= S147) 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)
54% identity, 99% coverage: 6:511/513 of query aligns to 1:507/507 of 1gkmA
- active site: Y53 (= Y57), G60 (= G64), H83 (= H87), N193 (= N199), Y278 (= Y284), R281 (= R287), F327 (= F333), E412 (= E418)
- binding cysteine: G142 (= G148), L189 (= L195), N193 (= N199), F327 (= F333)
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
44% identity, 93% coverage: 21:496/513 of query aligns to 131:607/657 of P21213
- S254 (= S147) mutation to A: Complete loss of activity.
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
44% identity, 91% coverage: 39:505/513 of query aligns to 162:632/677 of Q20502
- D536 (= D409) 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, 93% coverage: 30:505/513 of query aligns to 27:530/539 of Q8GMG0
- Y63 (= Y57) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ K65) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H87) binding ; mutation to F: Complete loss of activity.
- A152 (= A146) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S147) modified: 2,3-didehydroalanine (Ser)
- G154 (= G148) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N199) 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 (= R287) binding
- Y415 (≠ V390) 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)
39% identity, 86% coverage: 43:482/513 of query aligns to 34:495/531 of Q0VZ68
- F57 (= F63) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ LASVRI 66:71) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ LSHA 85:88) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ LSHAA 85:89) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (= G190) mutation to R: Gain of aminomutase activity.
- K242 (≠ R248) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. 277:279, 7% identical) mutation Missing: Total loss of aminomutase activity.
- P377 (= P366) mutation to R: No effect.
- C396 (≠ S383) mutation to S: No effect.
- E399 (≠ M386) 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. 386:393, 25% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 414:420, 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)
39% identity, 93% coverage: 30:505/513 of query aligns to 16:517/526 of 2rjsA
- active site: Y52 (= Y57), G59 (= G64), H82 (= H87), N192 (= N199), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (≠ E418)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y57), G59 (= G64), H82 (= H87), G141 (= G148), L143 (= L150), N192 (= N199), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (≠ E418)
2rjrA Substrate mimic bound to sgtam (see paper)
39% identity, 93% coverage: 30:505/513 of query aligns to 16:517/526 of 2rjrA
- active site: Y52 (= Y57), G59 (= G64), H82 (= H87), N192 (= N199), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (≠ E418)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y57), G59 (= G64), H82 (= H87), G141 (= G148), L143 (= L150), N192 (= N199), F343 (= F333), Q429 (≠ E418)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
39% identity, 93% coverage: 30:505/513 of query aligns to 16:517/526 of 2qveA
- active site: Y52 (= Y57), G59 (= G64), H82 (= H87), N192 (= N199), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (≠ E418)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y57), G59 (= G64), H82 (= H87), G141 (= G148), L143 (= L150), N192 (= N199), Y295 (= Y284), R298 (= R287), F343 (= F333), Q429 (≠ E418)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
39% identity, 93% coverage: 30:505/513 of query aligns to 17:518/527 of 3kdzA
- active site: F53 (≠ Y57), G60 (= G64), H83 (= H87), N193 (= N199), Y296 (= Y284), R299 (= R287), F344 (= F333), Q430 (≠ E418)
- binding tyrosine: F53 (≠ Y57), Y59 (≠ F63), G60 (= G64), H83 (= H87), G142 (= G148), N193 (= N199), Y296 (= Y284), R299 (= R287), F344 (= F333)
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
30% identity, 88% coverage: 39:491/513 of query aligns to 35:502/514 of 3unvA
- active site: Y53 (= Y57), G60 (= G64), V83 (≠ H87), L191 (= L197), D291 (= D282), S294 (≠ C285), G340 (= G331), D427 (≠ N416)
- binding phenylalanine: Y53 (= Y57), G60 (= G64), G142 (= G148), L144 (= L150), N326 (= N317), F342 (= F333)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y57), G60 (= G64), G142 (= G148), N193 (= N199), N326 (= N317), F342 (= F333)
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
38% identity, 89% coverage: 26:483/513 of query aligns to 23:496/515 of 2o7dA
- active site: Y54 (= Y57), G61 (= G64), L84 (≠ H87), N195 (= N199), Y292 (= Y284), R295 (= R287), F342 (= F333), Q428 (≠ E418)
- binding caffeic acid: G61 (= G64), H83 (≠ S86), L84 (≠ H87), Y292 (= Y284), R295 (= R287), N424 (≠ S414), N427 (≠ Q417), Q428 (≠ E418)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
38% identity, 89% coverage: 26:483/513 of query aligns to 23:496/515 of 2o7eA
- active site: Y54 (= Y57), G61 (= G64), L84 (≠ H87), N195 (= N199), Y292 (= Y284), R295 (= R287), F342 (= F333), Q428 (≠ E418)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y57), G143 (= G148), L145 (= L150), N195 (= N199), Y292 (= Y284), R295 (= R287), N325 (= N317), F342 (= F333)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
33% identity, 81% coverage: 39:455/513 of query aligns to 60:489/567 of Q3M5Z3
- L108 (≠ H87) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (= A146) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S147) modified: 2,3-didehydroalanine (Ser)
- G169 (= G148) 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.
6s7qA Crystal structure of ergothioneine degrading enzyme ergothionase from treponema denticola in complex with desmethyl-ergothioneine sulfonic acid (see paper)
26% identity, 94% coverage: 20:502/513 of query aligns to 16:495/497 of 6s7qA
- active site: Y53 (= Y57), G60 (= G64), D275 (= D282), A324 (≠ G331)
- binding (2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic acid: Y53 (= Y57), V59 (≠ F63), G60 (= G64), S194 (≠ N199), F326 (= F333), T380 (≠ I387), K383 (≠ V390), E411 (= E418)
5ltmB Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis (y78f-c503s-c565s) bound to cinnamate (see paper)
33% identity, 81% coverage: 39:455/513 of query aligns to 36:463/537 of 5ltmB
- active site: F54 (≠ Y57), G61 (= G64), L84 (≠ H87), N197 (= N199), Y288 (= Y284), R291 (= R287), F337 (= F333), Q426 (≠ H420)
- binding hydrocinnamic acid: F60 (= F63), A143 (= A146), L145 (= L150), Y288 (= Y284), R291 (= R287)
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)
32% identity, 83% coverage: 32:455/513 of query aligns to 55:496/687 of Q68G84
- Y80 (= Y57) active site, Proton donor/acceptor; mutation Y->A,F: Abolishes enzyme activity.
- A175 (= A146) modified: Crosslink with 177, 5-imidazolinone (Ala-Gly)
- S176 (= S147) modified: 2,3-didehydroalanine (Ser)
- G177 (= G148) modified: Crosslink with 175, 5-imidazolinone (Ala-Gly)
- N231 (= N199) 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 (= Q281) 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 (= Y284) 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 (= R287) 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 (= N317) binding ; mutation to X: Abolishes enzyme activity; when associated with X-231.
- F371 (= F333) mutation to X: Abolishes enzyme activity; when associated with X-322.
- N458 (≠ Q417) binding
B2J528 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
30% identity, 84% coverage: 25:455/513 of query aligns to 44:489/569 of B2J528
- A167 (= A146) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S147) modified: 2,3-didehydroalanine (Ser)
- G169 (= G148) modified: Crosslink with 167, 5-imidazolinone (Ala-Gly)
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)
32% identity, 83% coverage: 32:455/513 of query aligns to 55:496/698 of Q6GZ04
- Y80 (= Y57) mutation to F: Abolishes enzyme activity.
- L104 (≠ I83) mutation to A: Decreases enzyme activity.
- Q319 (= Q281) binding
- R325 (= R287) binding
P0DO55 Phenylalanine/tyrosine ammonia-lyase 1; FuPAL1; EC 4.3.1.25 from Fritillaria unibracteata (Sichuan fritillary) (see paper)
29% identity, 92% coverage: 25:497/513 of query aligns to 82:574/722 of P0DO55
- F141 (≠ S86) mutation to H: Increased activity toward L-tyrosine (L-Tyr) but reduced ability to use L-phenylalanine (L-Phe) as substrate.
- S208 (≠ A146) mutation to A: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- I218 (≠ M156) mutation to P: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- E490 (≠ S414) mutation to N: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
Query Sequence
>CCNA_01010 FitnessBrowser__Caulo:CCNA_01010
MERPVTELVLNPGAVPLAEWKAIYRGASARLAESAWPVIAESAAAVQRILAKGEPVYGIN
TGFGKLASVRIGDADLETLQRNIVLSHAAGVGEPSPVPVIRLMMALKLASLAQGASGVRV
ETVRMLEEMLVEGLTPVVPCQGSVGASGDLAPLSHMAATMIGVGEIFVGGQRLPAAQALA
QAGLEPLTLGPKEGLALLNGTQFSTANALAGLFEAERLFQSALVTGALSTEAAKGSDTPF
DPRIHTLRRHVGQIETAAALRALMSASEIRASHLKEDERVQDPYCLRCQPQVMGAALDIL
RQAATTLATEANCVSDNPLIFPEADEALSGGNFHAEPVAFAADMIALAVCEIGSIAERRI
AMLVDPALSGLPAFLTPKPGLNSGFMIPQVTAAALVSENKQRAYPASVDSIPTSANQEDH
VSMAAHGARRLLAMVENADAVLGIELLAAAQGCDFHAPLRSSAALEAVRALTRSKVPHLS
DDRHFHPDMEAANTLVRSGAVIAAVGALPGVTA
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