SitesBLAST
Comparing Ac3H11_2452 FitnessBrowser__acidovorax_3H11:Ac3H11_2452 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)
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
36% identity, 98% coverage: 9:415/415 of query aligns to 7:394/395 of 5m3zA
- active site: R58 (= R61), Y111 (≠ F114), D183 (= D185), K208 (= K210)
- binding norleucine: Y111 (≠ F114), H113 (≠ N116), K208 (= K210), V336 (≠ T357), S337 (≠ G358)
- binding pyridoxal-5'-phosphate: G86 (= G89), I87 (≠ M90), Y111 (≠ F114), E154 (= E156), D183 (= D185), T185 (= T187), S205 (= S207), T207 (= T209), K208 (= K210)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G89), I87 (≠ M90), Y111 (≠ F114), D183 (= D185), S205 (= S207), T207 (= T209), K208 (= K210), V336 (≠ T357), S337 (≠ G358), R372 (= R393)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
36% identity, 98% coverage: 9:415/415 of query aligns to 8:395/396 of 4omaA
- active site: R59 (= R61), Y112 (≠ F114), D184 (= D185), K209 (= K210)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G89), I88 (≠ M90), Y112 (≠ F114), D184 (= D185), S206 (= S207), T208 (= T209), K209 (= K210), V337 (≠ T357), S338 (≠ G358), R373 (= R393)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
36% identity, 98% coverage: 9:415/415 of query aligns to 8:395/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
36% identity, 98% coverage: 9:415/415 of query aligns to 8:395/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
36% identity, 98% coverage: 9:415/415 of query aligns to 8:395/396 of 3jw9A
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
36% identity, 98% coverage: 9:415/415 of query aligns to 8:395/396 of 6egrA
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
36% identity, 98% coverage: 9:415/415 of query aligns to 8:395/396 of 4hf8A
- active site: R59 (= R61), Y112 (≠ F114), D184 (= D185), K209 (= K210)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G89), I88 (≠ M90), Y112 (≠ F114), E155 (= E156), N159 (= N160), D184 (= D185), S206 (= S207), K209 (= K210), S338 (≠ G358), R373 (= R393)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
36% identity, 98% coverage: 9:415/415 of query aligns to 8:384/386 of 3mkjA
- active site: Y101 (≠ F114), D173 (= D185), K198 (= K210)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G89), I77 (≠ M90), Y101 (≠ F114), E144 (= E156), D173 (= D185), F176 (≠ V188), S195 (= S207), T197 (= T209), K198 (= K210)
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
34% identity, 98% coverage: 5:412/415 of query aligns to 4:394/399 of 5dx5A
- active site: R59 (= R61), Y112 (≠ F114), D186 (= D185), K211 (= K210)
- binding pyridoxal-5'-phosphate: Y57 (= Y59), R59 (= R61), S86 (= S88), G87 (= G89), M88 (= M90), Y112 (≠ F114), D186 (= D185), F189 (≠ V188), S208 (= S207), T210 (= T209), K211 (= K210)
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
35% identity, 97% coverage: 9:412/415 of query aligns to 5:389/393 of 5x30C
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
35% identity, 97% coverage: 9:412/415 of query aligns to 9:393/397 of 3vk3A
7kb1C Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
34% identity, 92% coverage: 30:412/415 of query aligns to 29:423/428 of 7kb1C
- binding pyridoxal-5'-phosphate: Y57 (= Y59), R59 (= R61)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: G87 (= G89), Q88 (≠ M90), Y112 (≠ F114), N160 (= N160), D185 (= D185), S206 (= S207), T208 (= T209), K209 (= K210), N369 (≠ G358), I370 (≠ L359), R404 (= R393)
7kb1A Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
34% identity, 92% coverage: 30:412/415 of query aligns to 29:423/428 of 7kb1A
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y57 (= Y59), R59 (= R61), G87 (= G89), Q88 (≠ M90), Y112 (≠ F114), N160 (= N160), D185 (= D185), S206 (= S207), T208 (= T209), K209 (= K210), N369 (≠ G358), I370 (≠ L359), R404 (= R393)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
35% identity, 97% coverage: 9:412/415 of query aligns to 10:394/398 of 1pg8A
- active site: R61 (= R61), Y114 (≠ F114), D186 (= D185), K211 (= K210)
- binding pyridoxal-5'-phosphate: Y59 (= Y59), R61 (= R61), S88 (= S88), G89 (= G89), M90 (= M90), Y114 (≠ F114), D186 (= D185), S208 (= S207), T210 (= T209), K211 (= K210)
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)
35% identity, 97% coverage: 9:412/415 of query aligns to 10:394/398 of P13254
- YSR 59:61 (≠ YAR 59:61) binding
- R61 (= R61) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 89:90) binding in other chain
- Y114 (≠ F114) binding
- C116 (≠ N116) 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 (≠ SLT 207:209) binding in other chain
- K211 (= K210) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R260) 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 (= D261) 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 (= R393) binding
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
35% identity, 97% coverage: 9:412/415 of query aligns to 4:388/392 of 5x2xA
- active site: R55 (= R61), Y108 (≠ F114), D180 (= D185), K205 (= K210)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y59), R55 (= R61), G83 (= G89), M84 (= M90), Y108 (≠ F114), N155 (= N160), D180 (= D185), S202 (= S207), T204 (= T209), K205 (= K210), V333 (≠ T357), S334 (≠ G358), R369 (= R393)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
35% identity, 97% coverage: 9:412/415 of query aligns to 4:388/392 of 5x2wA
- active site: R55 (= R61), Y108 (≠ F114), D180 (= D185), K205 (= K210)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y59), R55 (= R61), S82 (= S88), G83 (= G89), M84 (= M90), Y108 (≠ F114), D180 (= D185), S202 (= S207), K205 (= K210), V333 (≠ T357), S334 (≠ G358), R369 (= R393)
O13326 Homocysteine synthase; O-acetylhomoserine sulfhydrylase; OAH SHL; OAH sulfhydrylase; EC 2.5.1.49 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 98% coverage: 5:412/415 of query aligns to 4:426/429 of O13326
- G411 (= G397) mutation to D: Impairs homocysteine synthase activity.
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
33% identity, 97% coverage: 11:413/415 of query aligns to 5:371/373 of 4l0oH
- active site: R40 (= R61), Y92 (≠ F114), D164 (= D185), K189 (= K210)
- binding pyridoxal-5'-phosphate: Y38 (= Y59), R40 (= R61), S67 (= S88), G68 (= G89), L69 (≠ M90), Y92 (≠ F114), D164 (= D185), S186 (= S207), T188 (= T209), K189 (= K210)
8wkoA Crystal structure of o-acetylhomoserine sulfhydrylase from lactobacillus plantarum in the closed form
32% identity, 99% coverage: 2:413/415 of query aligns to 2:423/425 of 8wkoA
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: G87 (= G89), S88 (≠ M90), Y112 (≠ F114), E155 (= E156), D184 (= D185), T186 (= T187), S206 (= S207), A207 (≠ L208), T208 (= T209), F209 (≠ S211), G212 (= G214), M217 (≠ L219), V369 (≠ L359), A370 (= A360)
- binding proline: H213 (≠ L215), Q284 (≠ L276), S288 (≠ T280)
Query Sequence
>Ac3H11_2452 FitnessBrowser__acidovorax_3H11:Ac3H11_2452
MTTPQNQSFTTQIVHADRLGGAEQGAIHQPIHTSVQYGYDKVEDLIAVFQGTAKGGFNYA
RQGTPTTAALEAKITKMERGHGTIVFSSGMAGICAVFLTLLKAGDHLVASQFVFGNTNSV
LGTLADLGVEVTTVDVTDAANVAAALRPNTRMVFVETIANPGTQIPDLEGIGALCKAHGA
LYVVDNTVASPYLFRAATVGAGLVVNSLTKSIGGLGDALGGAITDTGLYDWSRYPNIFAA
YRKGDAKGWGLQQLRKKGLRDMGGTLSSHAAHQLALGAETLALRMDRTSATALALAQWLE
AHPAIARVHYPLLPSHPQHAFAKKHLKAGSWLLSFELRDPDQCLPVCNRLQLPIKATGLA
DTRTLIIPVAHTIFWEAGPAVRASMGIADSMIRLSVGLEEVEDLLADFEQALAGA
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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