SitesBLAST
Comparing WP_035134897.1 NCBI__GCF_000769915.1:WP_035134897.1 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)
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
44% identity, 96% coverage: 19:498/502 of query aligns to 125:614/657 of P21213
- S254 (= S146) mutation to A: Complete loss of activity.
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
45% identity, 95% coverage: 27:501/502 of query aligns to 152:633/677 of Q20502
- D536 (= D404) mutation to N: In am130; causes strong resistance to nickel and zinc toxicity.
P21310 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 4 papers)
42% identity, 89% coverage: 46:491/502 of query aligns to 44:493/510 of P21310
- S144 (= S146) 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)
42% identity, 89% coverage: 46:491/502 of query aligns to 43:490/507 of 1gkmA
- active site: Y53 (= Y56), G60 (= G63), H83 (= H86), N193 (= N198), Y278 (= Y280), R281 (= R283), F327 (= F329), E412 (= E413)
- binding cysteine: G142 (= G147), L189 (= L194), N193 (= N198), F327 (= F329)
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)
34% identity, 95% coverage: 7:485/502 of query aligns to 15:515/539 of Q8GMG0
- Y63 (= Y56) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ S64) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H86) binding substrate; mutation to F: Complete loss of activity.
- A152 (= A145) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S146) modified: 2,3-didehydroalanine (Ser)
- G154 (= G147) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N198) binding substrate
- Y303 (≠ H275) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- R311 (= R283) binding substrate
- Y415 (= Y385) 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)
35% identity, 97% coverage: 7:493/502 of query aligns to 3:511/531 of Q0VZ68
- F57 (= F62) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ LYNVKI 65:70) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ KSHA 84:87) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ KSHAC 84:88) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ K189) mutation to R: Gain of aminomutase activity.
- K242 (≠ R247) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. gap) mutation Missing: Total loss of aminomutase activity.
- P377 (vs. gap) mutation to R: No effect.
- C396 (≠ S378) mutation to S: No effect.
- E399 (≠ M381) 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. 381:388, 38% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 409:415, 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)
34% identity, 95% coverage: 7:485/502 of query aligns to 4:502/526 of 2rjsA
- active site: Y52 (= Y56), G59 (= G63), H82 (= H86), N192 (= N198), Y295 (= Y280), R298 (= R283), F343 (= F329), Q429 (≠ E413)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y56), G59 (= G63), H82 (= H86), G141 (= G147), L143 (= L149), N192 (= N198), Y295 (= Y280), R298 (= R283), F343 (= F329), Q429 (≠ E413)
2rjrA Substrate mimic bound to sgtam (see paper)
34% identity, 95% coverage: 7:485/502 of query aligns to 4:502/526 of 2rjrA
- active site: Y52 (= Y56), G59 (= G63), H82 (= H86), N192 (= N198), Y295 (= Y280), R298 (= R283), F343 (= F329), Q429 (≠ E413)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y56), G59 (= G63), H82 (= H86), G141 (= G147), L143 (= L149), N192 (= N198), F343 (= F329), Q429 (≠ E413)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
34% identity, 95% coverage: 7:485/502 of query aligns to 4:502/526 of 2qveA
- active site: Y52 (= Y56), G59 (= G63), H82 (= H86), N192 (= N198), Y295 (= Y280), R298 (= R283), F343 (= F329), Q429 (≠ E413)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y56), G59 (= G63), H82 (= H86), G141 (= G147), L143 (= L149), N192 (= N198), Y295 (= Y280), R298 (= R283), F343 (= F329), Q429 (≠ E413)
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
34% identity, 95% coverage: 7:485/502 of query aligns to 5:503/527 of 3kdzA
- active site: F53 (≠ Y56), G60 (= G63), H83 (= H86), N193 (= N198), Y296 (= Y280), R299 (= R283), F344 (= F329), Q430 (≠ E413)
- binding tyrosine: F53 (≠ Y56), Y59 (≠ F62), G60 (= G63), H83 (= H86), G142 (= G147), N193 (= N198), Y296 (= Y280), R299 (= R283), F344 (= F329)
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
32% identity, 96% coverage: 3:486/502 of query aligns to 1:502/514 of 3unvA
- active site: Y53 (= Y56), G60 (= G63), V83 (≠ H86), L191 (= L196), D291 (= D278), S294 (= S281), G340 (= G327), D427 (≠ G411)
- binding phenylalanine: Y53 (= Y56), G60 (= G63), G142 (= G147), L144 (= L149), N326 (= N313), F342 (= F329)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y56), G60 (= G63), G142 (= G147), N193 (= N198), N326 (= N313), F342 (= F329)
2o7dA Tyrosine ammonia-lyase from rhodobacter sphaeroides, complexed with caffeate (see paper)
34% identity, 94% coverage: 12:484/502 of query aligns to 11:502/515 of 2o7dA
- active site: Y54 (= Y56), G61 (= G63), L84 (≠ H86), N195 (= N198), Y292 (= Y280), R295 (= R283), F342 (= F329), Q428 (≠ E413)
- binding caffeic acid: G61 (= G63), H83 (≠ S85), L84 (≠ H86), Y292 (= Y280), R295 (= R283), N424 (≠ S409), N427 (≠ Q412), Q428 (≠ E413)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
34% identity, 94% coverage: 12:484/502 of query aligns to 11:502/515 of 2o7eA
- active site: Y54 (= Y56), G61 (= G63), L84 (≠ H86), N195 (= N198), Y292 (= Y280), R295 (= R283), F342 (= F329), Q428 (≠ E413)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y56), G143 (= G147), L145 (= L149), N195 (= N198), Y292 (= Y280), R295 (= R283), N325 (= N313), F342 (= F329)
6s7qA Crystal structure of ergothioneine degrading enzyme ergothionase from treponema denticola in complex with desmethyl-ergothioneine sulfonic acid (see paper)
30% identity, 98% coverage: 7:496/502 of query aligns to 5:494/497 of 6s7qA
- active site: Y53 (= Y56), G60 (= G63), D275 (= D278), A324 (≠ G327)
- binding (2~{S})-2-(dimethylamino)-3-(2-sulfo-1~{H}-imidazol-4-yl)propanoic acid: Y53 (= Y56), V59 (≠ F62), G60 (= G63), S194 (≠ N198), F326 (= F329), T380 (≠ I382), K383 (≠ Y385), E411 (= E413)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
32% identity, 90% coverage: 7:459/502 of query aligns to 28:498/567 of Q3M5Z3
- L108 (≠ H86) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (= A145) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S146) modified: 2,3-didehydroalanine (Ser)
- G169 (= G147) 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)
31% identity, 90% coverage: 2:451/502 of query aligns to 23:490/569 of B2J528
- A167 (= A145) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S146) modified: 2,3-didehydroalanine (Ser)
- G169 (= G147) 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)
31% identity, 90% coverage: 7:459/502 of query aligns to 4:472/537 of 5ltmB
- active site: F54 (≠ Y56), G61 (= G63), L84 (≠ H86), N197 (= N198), Y288 (= Y280), R291 (= R283), F337 (= F329), Q426 (≠ E413)
- binding hydrocinnamic acid: F60 (= F62), A143 (= A145), L145 (= L149), Y288 (= Y280), R291 (= R283)
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)
30% identity, 84% coverage: 30:452/502 of query aligns to 55:498/698 of Q6GZ04
- Y80 (= Y56) mutation to F: Abolishes enzyme activity.
- L104 (= L82) mutation to A: Decreases enzyme activity.
- Q319 (= Q277) binding (E)-cinnamate
- R325 (= R283) binding (E)-cinnamate
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)
30% identity, 84% coverage: 30:452/502 of query aligns to 55:498/687 of Q68G84
- Y80 (= Y56) active site, Proton donor/acceptor; mutation Y->A,F: Abolishes enzyme activity.
- A175 (= A145) modified: Crosslink with 177, 5-imidazolinone (Ala-Gly)
- S176 (= S146) modified: 2,3-didehydroalanine (Ser)
- G177 (= G147) modified: Crosslink with 175, 5-imidazolinone (Ala-Gly)
- N231 (= N198) binding (E)-cinnamate; 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 (= Q277) binding (E)-cinnamate; 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 (= Y280) 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 (= R283) binding (E)-cinnamate; 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 (= N313) binding (E)-cinnamate; mutation to X: Abolishes enzyme activity; when associated with X-231.
- F371 (= F329) mutation to X: Abolishes enzyme activity; when associated with X-322.
- N458 (≠ Q412) binding (E)-cinnamate
4c5sC Structural investigations into the stereochemistry and activity of a phenylalanine-2,3-aminomutase from taxus chinensis (see paper)
30% identity, 85% coverage: 26:452/502 of query aligns to 42:480/642 of 4c5sC
- active site: A71 (≠ Y56), G78 (= G63), L99 (≠ H86), N213 (= N198), Y304 (= Y280), R307 (= R283), F353 (= F329), Q441 (≠ E413)
- binding (3S)-3-amino-2,2-difluoro-3-phenylpropanoic acid: G78 (= G63), G159 (= G147), L161 (= L149), N213 (= N198), Y304 (= Y280), R307 (= R283), N337 (= N313), F353 (= F329), E437 (≠ S409)
Query Sequence
>WP_035134897.1 NCBI__GCF_000769915.1:WP_035134897.1
METIHYISSELLSIEVVNEIITQGKKLELSEEARLNIEKCRTYLDEKMKSHSDPIYGINT
GFGSLYNVKISNENLSKLQENLVKSHACGTGEEVPQEIVKIMLLLKIQSLSYGHSGVQLE
TVQRLIDFYNNDILPVVYNQGSLGASGDLAPLAHLSLPLLGEGEVNMDGFRQPASKVLEK
IGWKPIVLKSKEGLALLNGTQFMSSYGVYVLLKSIKYSYLADVIGAISLEGFDGRIEPFN
ELIHMVRPHKGQIVTAQRFNQLLEDSEIIAHPKQHVQDPYSFRCIPQVHGATKDTIDYVK
KVFRTEINSVTDNPNIFIDSDQIISGGNFHGQPLALTLDFLGIALSELGSISERRTYQLI
SGLRGLPPFLVANPGLNSGFMIPQYTAASIVSQNKQLCTPASADSIVSSNGQEDHVSMGA
NAATKALRIIENLERILAIELMNASQAIEFRRPLKSSDFIEMFLKSYREEVPLVEDDRIL
HYDIENTIAFLNNMQIDETVID
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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