SitesBLAST
Comparing Ac3H11_4146 FitnessBrowser__acidovorax_3H11:Ac3H11_4146 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)
8sadA Crystal structure of cystathionine beta lyase from klebsiella aerogenes, plp/malonate complex (c2 form)
36% identity, 97% coverage: 8:407/412 of query aligns to 6:396/398 of 8sadA
- binding magnesium ion: A359 (≠ G369), R362 (= R374), A365 (≠ P377)
- binding pyridoxal-5'-phosphate: C88 (≠ S89), G89 (= G90), A90 (≠ L91), Y114 (= Y115), D188 (= D187), A210 (= A215), T212 (= T217), K213 (= K218), M222 (≠ L227), W343 (= W356)
8u99A Crystal structure of cystathionine beta lyase from klebsiella aerogenes (plp-serine adduct)
37% identity, 91% coverage: 33:407/412 of query aligns to 24:389/391 of 8u99A
- binding pyridoxal-5'-phosphate: C81 (≠ S89), G82 (= G90), A83 (≠ L91), Y107 (= Y115), D181 (= D187), T205 (= T217), K206 (= K218), M215 (≠ L227), W336 (= W356)
- binding serine: Y107 (= Y115), K206 (= K218), Y334 (= Y354), S335 (= S355), W336 (= W356), R368 (= R386)
8u98A Crystal structure of cystathionine beta lyase from klebsiella aerogenes (plp-glycine adduct)
37% identity, 91% coverage: 33:407/412 of query aligns to 24:389/391 of 8u98A
- binding glycine: Y107 (= Y115), K206 (= K218), Y334 (= Y354), S335 (= S355), W336 (= W356), R368 (= R386)
- binding pyridoxal-5'-phosphate: Y52 (= Y60), R54 (≠ L62), C81 (≠ S89), G82 (= G90), A83 (≠ L91), Y107 (= Y115), D181 (= D187), A203 (= A215), T205 (= T217), K206 (= K218), M215 (≠ L227), W336 (= W356)
8sa9A Crystal structure of cystathionine beta lyase from klebsiella aerogenes, plp-oxamate adduct (c2 form)
37% identity, 91% coverage: 33:407/412 of query aligns to 24:389/391 of 8sa9A
- binding pyridoxal-5'-phosphate: C81 (≠ S89), G82 (= G90), A83 (≠ L91), Y107 (= Y115), D181 (= D187), A203 (= A215), T205 (= T217), K206 (= K218), M215 (≠ L227), W336 (= W356)
- binding [({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino](oxo)acetic acid: C81 (≠ S89), G82 (= G90), A83 (≠ L91), Y107 (= Y115), D181 (= D187), A203 (= A215), T205 (= T217), K206 (= K218), M215 (≠ L227), S335 (= S355), W336 (= W356), R368 (= R386)
8sabA Crystal structure of cystathionine beta lyase from klebsiella aerogenes, plp adduct with alanine (c2 form)
37% identity, 91% coverage: 33:407/412 of query aligns to 25:390/392 of 8sabA
- binding lysine: L330 (= L349), E341 (≠ M360)
- binding pyridoxal-5'-phosphate: C82 (≠ S89), G83 (= G90), A84 (≠ L91), Y108 (= Y115), D182 (= D187), A204 (= A215), T206 (= T217), K207 (= K218), M216 (≠ L227), W337 (= W356)
- binding alanyl-pyridoxal-5'-phosphate: C82 (≠ S89), G83 (= G90), A84 (≠ L91), Y108 (= Y115), D182 (= D187), A204 (= A215), T206 (= T217), K207 (= K218), M216 (≠ L227), Y335 (= Y354), S336 (= S355), W337 (= W356), R369 (= R386)
Sites not aligning to the query:
P06721 Cystathionine beta-lyase MetC; CBL; CL; Beta-cystathionase MetC; Cysteine desulfhydrase MetC; CD; Cysteine lyase MetC; Cysteine-S-conjugate beta-lyase MetC; EC 4.4.1.13; EC 4.4.1.28 from Escherichia coli (strain K12) (see 2 papers)
34% identity, 97% coverage: 8:407/412 of query aligns to 3:393/395 of P06721
- K210 (= K218) modified: N6-(pyridoxal phosphate)lysine
2gqnA Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-nitro-benzamide (see paper)
34% identity, 96% coverage: 11:407/412 of query aligns to 2:389/391 of 2gqnA
- active site: R54 (≠ L62), Y107 (= Y115), D181 (= D187), K206 (= K218)
- binding (5-hydroxy-6-methyl-4-((2-(2-(2-nitrobenzamido)acetyl)hydrazinyl)methyl)pyridin-3-yl)methyl dihydrogen phosphate: C81 (≠ S89), G82 (= G90), A83 (≠ L91), Y107 (= Y115), E108 (≠ G116), D181 (= D187), A203 (= A215), T205 (= T217), K206 (= K218), M215 (≠ L227), Y334 (= Y354), S335 (= S355), W336 (= W356), R368 (= R386)
2fq6A Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-trifluoromethyl-benzamide (see paper)
34% identity, 96% coverage: 11:407/412 of query aligns to 2:389/391 of 2fq6A
- active site: R54 (≠ L62), Y107 (= Y115), D181 (= D187), K206 (= K218)
- binding phosphoric acid mono-(5-hydroxy-6-methyl-4-{[2-(2-trifluoromethyl-benzoylamino)-acetyl]-hydrazonomethyl}-pyridin-3-ylmethyl)ester: C81 (≠ S89), G82 (= G90), A83 (≠ L91), Y107 (= Y115), P109 (= P117), D181 (= D187), A203 (= A215), T205 (= T217), K206 (= K218), M215 (≠ L227), Y334 (= Y354), S335 (= S355), W336 (= W356), R368 (= R386)
1cl2A Cystathionine beta-lyase (cbl) from escherichia coli in complex with aminoethoxyvinylglycine (see paper)
34% identity, 96% coverage: 11:407/412 of query aligns to 2:389/391 of 1cl2A
- active site: R54 (≠ L62), Y107 (= Y115), D181 (= D187), K206 (= K218)
- binding (2E,3E)-4-(2-aminoethoxy)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: C81 (≠ S89), G82 (= G90), A83 (≠ L91), Y107 (= Y115), D181 (= D187), A203 (= A215), T205 (= T217), K206 (= K218), M215 (≠ L227), Y334 (= Y354), S335 (= S355), W336 (= W356), R368 (= R386)
1cl1B Cystathionine beta-lyase (cbl) from escherichia coli (see paper)
34% identity, 96% coverage: 11:407/412 of query aligns to 3:390/392 of 1cl1B
4itxA P113s mutant of e. Coli cystathionine beta-lyase metc inhibited by reaction with l-ala-p (see paper)
34% identity, 96% coverage: 11:407/412 of query aligns to 2:389/391 of 4itxA
- active site: R54 (≠ L62), Y107 (= Y115), D181 (= D187), K206 (= K218)
- binding {1-[(3-hydroxy-methyl-5-phosphonooxy-methyl-pyridin-4-ylmethyl)-amino]-ethyl}-phosphonic acid: C81 (≠ S89), G82 (= G90), A83 (≠ L91), Y107 (= Y115), D181 (= D187), A203 (= A215), T205 (= T217), K206 (= K218), M215 (≠ L227), Y334 (= Y354), S335 (= S355), W336 (= W356), R368 (= R386)
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
30% identity, 96% coverage: 11:406/412 of query aligns to 5:390/393 of 5x30C
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
30% identity, 96% coverage: 11:406/412 of query aligns to 9:394/397 of 3vk3A
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
30% identity, 96% coverage: 11:406/412 of query aligns to 10:395/398 of 1pg8A
- active site: R61 (≠ L62), Y114 (= Y115), D186 (= D187), K211 (= K218)
- binding pyridoxal-5'-phosphate: Y59 (= Y60), R61 (≠ L62), S88 (= S89), G89 (= G90), M90 (≠ L91), Y114 (= Y115), D186 (= D187), S208 (≠ A215), T210 (= T217), K211 (= K218)
P13254 L-methionine gamma-lyase; MGL; Homocysteine desulfhydrase; L-methioninase; EC 4.4.1.11; EC 4.4.1.2 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
30% identity, 96% coverage: 11:406/412 of query aligns to 10:395/398 of P13254
- YSR 59:61 (≠ YGL 60:62) binding
- R61 (≠ L62) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (≠ GL 90:91) binding in other chain
- Y114 (= Y115) binding
- C116 (≠ P117) mutation to H: Drastic decrease of the catalytic efficiency of the elimination reaction with L-methionine, by 6700-fold, and increases that with L-cysteine by 7-fold, mainly due to changes in kcat. Loss of ability to catalyze replacement reaction between L-methionine and 2-mercaptoethanol.; mutation to S: 9% of wild-type elimination activity against L-methionine.; mutation to T: 40% of wild-type elimination activity against L-methionine.
- SAT 208:210 (≠ ALT 215:217) binding in other chain
- K211 (= K218) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R248) mutation K->D,E: Marked decrease in elimination activity against both L-methionine and DL-homocysteine.; mutation to M: 50% reduction in alpha,gamma-elimination activity against DL-homocysteine, while retaining elimination activity against L-methionine and L-cysteine.
- D241 (vs. gap) mutation D->H,R: 5 to 14-fold reduction in alpha,gamma-elimination activity against L-methionine, while no change in affinity for L-methionine.
- R375 (= R386) binding
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
30% identity, 96% coverage: 11:406/412 of query aligns to 4:389/392 of 5x2xA
- active site: R55 (≠ L62), Y108 (= Y115), D180 (= D187), K205 (= K218)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y60), R55 (≠ L62), G83 (= G90), M84 (≠ L91), Y108 (= Y115), N155 (≠ S162), D180 (= D187), S202 (≠ A215), T204 (= T217), K205 (= K218), V333 (≠ Y354), S334 (= S355), R369 (= R386)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
30% identity, 96% coverage: 11:406/412 of query aligns to 4:389/392 of 5x2wA
- active site: R55 (≠ L62), Y108 (= Y115), D180 (= D187), K205 (= K218)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y60), R55 (≠ L62), S82 (= S89), G83 (= G90), M84 (≠ L91), Y108 (= Y115), D180 (= D187), S202 (≠ A215), K205 (= K218), V333 (≠ Y354), S334 (= S355), R369 (= R386)
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
30% identity, 96% coverage: 11:407/412 of query aligns to 3:372/373 of 4l0oH
- active site: R40 (≠ L62), Y92 (= Y115), D164 (= D187), K189 (= K218)
- binding pyridoxal-5'-phosphate: Y38 (= Y60), R40 (≠ L62), S67 (= S89), G68 (= G90), L69 (= L91), Y92 (= Y115), D164 (= D187), S186 (≠ A215), T188 (= T217), K189 (= K218)
7ba4A Structure of cystathionine gamma-lyase from pseudomonas aeruginosa
32% identity, 96% coverage: 11:407/412 of query aligns to 7:373/377 of 7ba4A
8j6nA Crystal structure of cystathionine gamma-lyase in complex with compound 1 (see paper)
29% identity, 97% coverage: 11:410/412 of query aligns to 9:390/390 of 8j6nA
- binding [6-methyl-4-[(~{E})-(oxamoylhydrazinylidene)methyl]-5-oxidanyl-pyridin-3-yl]methyl dihydrogen phosphate: Y51 (= Y60), R53 (≠ L62), G81 (= G90), L82 (= L91), Y105 (= Y115), E148 (= E158), N152 (≠ S162), D178 (= D187), S200 (≠ A215), T202 (= T217), K203 (= K218), E330 (≠ Y354), S331 (= S355), T346 (≠ S370), R366 (= R386)
Query Sequence
>Ac3H11_4146 FitnessBrowser__acidovorax_3H11:Ac3H11_4146
MAAMKDHDTDLATRIVHHGYLPPAGFEAPQPGVYKASTVIFPNVAAMRSREWKDKSGYTY
GLHGTPTTFILEERLCTLEGGLQCVLVPSGLAAIANVGLALLKPGDEVLIPDNAYGPGKD
FANGELARFGITHVFYDPLDPADLAARITPATRLVWLEAPGSVSMEFPDLCEQVRICRAR
GVTTALDNTWGAGLAFAPFDLTGDGSLGVDISAHALTKYPSGGGDVLMGSVITRDLGLHM
KIKLTHMRLGLGVGVNDVEAVLRALPSIGLRYRAHDEAARVLARWLQQQPAIAQVLHPAL
EGAPGHAHWKALCGAAQGGQGAAAGLFSVMIDARYTQQQVDAFCDGLRLFKLGYSWGGPM
SLVVPYTIGSMRSRPSPQLQPGTLVRFSIGLEAVEDLQRDLQQAMERAFPAA
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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