SitesBLAST
Comparing AO356_15115 FitnessBrowser__pseudo5_N2C3_1:AO356_15115 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)
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
40% identity, 94% coverage: 10:402/417 of query aligns to 3:399/399 of 5dx5A
- active site: R59 (= R66), Y112 (= Y119), D186 (= D191), K211 (= K216)
- binding pyridoxal-5'-phosphate: Y57 (= Y64), R59 (= R66), S86 (= S93), G87 (= G94), M88 (= M95), Y112 (= Y119), D186 (= D191), F189 (= F194), S208 (= S213), T210 (= T215), K211 (= K216)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
39% identity, 89% coverage: 27:397/417 of query aligns to 16:389/394 of 1e5eA
- active site: R55 (= R66), Y108 (= Y119), D181 (= D191), K206 (= K216)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y64), R55 (= R66), G83 (= G94), M84 (= M95), Y108 (= Y119), N155 (= N166), D181 (= D191), S203 (= S213), T205 (= T215), K206 (= K216), S335 (≠ N343), T350 (≠ S358), R370 (= R378)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
39% identity, 89% coverage: 27:397/417 of query aligns to 16:389/393 of 1e5fA
- active site: R55 (= R66), Y108 (= Y119), D181 (= D191), K206 (= K216)
- binding pyridoxal-5'-phosphate: Y53 (= Y64), R55 (= R66), G83 (= G94), M84 (= M95), Y108 (= Y119), D181 (= D191), S203 (= S213), K206 (= K216)
7d7oB Crystal structure of cystathionine gamma-lyase from bacillus cereus atcc 14579 (see paper)
41% identity, 88% coverage: 32:398/417 of query aligns to 20:377/377 of 7d7oB
P55217 Cystathionine gamma-synthase 1, chloroplastic; AtCGS1; METHIONINE OVERACCUMULATION 1; O-succinylhomoserine (thiol)-lyase; EC 2.5.1.48 from Arabidopsis thaliana (Mouse-ear cress) (see 4 papers)
40% identity, 92% coverage: 16:397/417 of query aligns to 176:560/563 of P55217
- T412 (≠ S249) natural variant: T -> P
- G459 (= G296) natural variant: G -> A
Sites not aligning to the query:
- 8 natural variant: C -> S
- 55 natural variant: A -> G
- 77 R→H: In mto1-4; over-accumulation of soluble methionine.
- 78 R→K: In mto1-7; over-accumulation of soluble methionine.
- 81 S→N: In mto1-2; over-accumulation of soluble methionine.
- 84 G→D: In mto1-3 and mto1-5; over-accumulation of soluble methionine.; G→S: In mto1-1; over-accumulation of soluble methionine.
- 86 A→V: In mto1-6; over-accumulation of soluble methionine.
- 91 natural variant: A -> G
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
40% identity, 92% coverage: 14:397/417 of query aligns to 8:393/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
40% identity, 92% coverage: 14:397/417 of query aligns to 4:389/393 of 5x30C
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
36% identity, 92% coverage: 14:397/417 of query aligns to 7:392/396 of 6egrA
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
36% identity, 92% coverage: 14:397/417 of query aligns to 7:392/396 of 4omaA
- active site: R59 (= R66), Y112 (= Y119), D184 (= D191), K209 (= K216)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G94), I88 (≠ M95), Y112 (= Y119), D184 (= D191), S206 (= S213), T208 (= T215), K209 (= K216), V337 (≠ G342), S338 (≠ N343), R373 (= R378)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
36% identity, 92% coverage: 14:397/417 of query aligns to 7:392/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
36% identity, 92% coverage: 14:397/417 of query aligns to 7:392/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
36% identity, 92% coverage: 14:397/417 of query aligns to 7:392/396 of 3jw9A
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
40% identity, 92% coverage: 14:397/417 of query aligns to 9:394/398 of 1pg8A
- active site: R61 (= R66), Y114 (= Y119), D186 (= D191), K211 (= K216)
- binding pyridoxal-5'-phosphate: Y59 (= Y64), R61 (= R66), S88 (= S93), G89 (= G94), M90 (= M95), Y114 (= Y119), D186 (= D191), S208 (= S213), T210 (= T215), K211 (= K216)
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)
40% identity, 92% coverage: 14:397/417 of query aligns to 9:394/398 of P13254
- YSR 59:61 (= YSR 64:66) binding
- R61 (= R66) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 94:95) binding in other chain
- Y114 (= Y119) binding
- C116 (≠ G121) 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 (= SAT 213:215) binding in other chain
- K211 (= K216) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R243) 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 (≠ E244) 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 (= R378) binding
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
36% identity, 92% coverage: 14:397/417 of query aligns to 6:391/395 of 5m3zA
- active site: R58 (= R66), Y111 (= Y119), D183 (= D191), K208 (= K216)
- binding norleucine: Y111 (= Y119), H113 (≠ G121), K208 (= K216), V336 (≠ G342), S337 (≠ N343)
- binding pyridoxal-5'-phosphate: G86 (= G94), I87 (≠ M95), Y111 (= Y119), E154 (= E162), D183 (= D191), T185 (= T193), S205 (= S213), T207 (= T215), K208 (= K216)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G94), I87 (≠ M95), Y111 (= Y119), D183 (= D191), S205 (= S213), T207 (= T215), K208 (= K216), V336 (≠ G342), S337 (≠ N343), R372 (= R378)
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
40% identity, 92% coverage: 14:397/417 of query aligns to 3:388/392 of 5x2xA
- active site: R55 (= R66), Y108 (= Y119), D180 (= D191), K205 (= K216)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y64), R55 (= R66), G83 (= G94), M84 (= M95), Y108 (= Y119), N155 (= N166), D180 (= D191), S202 (= S213), T204 (= T215), K205 (= K216), V333 (≠ G342), S334 (≠ N343), R369 (= R378)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
40% identity, 92% coverage: 14:397/417 of query aligns to 3:388/392 of 5x2wA
- active site: R55 (= R66), Y108 (= Y119), D180 (= D191), K205 (= K216)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y64), R55 (= R66), S82 (= S93), G83 (= G94), M84 (= M95), Y108 (= Y119), D180 (= D191), S202 (= S213), K205 (= K216), V333 (≠ G342), S334 (≠ N343), R369 (= R378)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
36% identity, 92% coverage: 14:397/417 of query aligns to 7:392/396 of 4hf8A
- active site: R59 (= R66), Y112 (= Y119), D184 (= D191), K209 (= K216)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G94), I88 (≠ M95), Y112 (= Y119), E155 (= E162), N159 (= N166), D184 (= D191), S206 (= S213), K209 (= K216), S338 (≠ N343), R373 (= R378)
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
41% identity, 92% coverage: 17:398/417 of query aligns to 5:371/373 of 4l0oH
- active site: R40 (= R66), Y92 (= Y119), D164 (= D191), K189 (= K216)
- binding pyridoxal-5'-phosphate: Y38 (= Y64), R40 (= R66), S67 (= S93), G68 (= G94), L69 (≠ M95), Y92 (= Y119), D164 (= D191), S186 (= S213), T188 (= T215), K189 (= K216)
1i48A Cystathionine gamma-synthase in complex with the inhibitor ctcpo (see paper)
40% identity, 92% coverage: 16:397/417 of query aligns to 9:393/396 of 1i48A
- active site: R61 (= R66), Y114 (= Y119), D187 (= D191), K212 (= K216)
- binding carboxymethylthio-3-(3-chlorophenyl)-1,2,4-oxadiazol: Y114 (= Y119), R115 (≠ G120), A337 (= A341), P338 (≠ G342), S339 (≠ N343), D348 (≠ G352), S354 (= S358), R374 (= R378), S376 (= S380)
- binding pyridoxal-5'-phosphate: Y59 (= Y64), R61 (= R66), S88 (= S93), G89 (= G94), M90 (= M95), Y114 (= Y119), D187 (= D191), S209 (= S213), T211 (= T215), K212 (= K216), F340 (≠ L344)
Query Sequence
>AO356_15115 FitnessBrowser__pseudo5_N2C3_1:AO356_15115
MNNKPDSTGLDNAGAGTRAVWGGEQVRHPYNATQTPIVASAAYGYDDIDVWYDVALGKAP
GFIYSRMSNPTVETLEAKIRELEMAESAVAFSSGMAAISSVLYTFLAHGDRVVSTKDSYG
GTNKIFEEFLPRTGVAVTLCETFDHDDIEREIAKGCQVLYLETPTNPTLKILDIPRLVAA
AKRVGAVVVADNTFATPLNQSPLALGVDVVIHSATKFLSGHGDVLGGLVCGREALMAKVR
HYREINGASLDPFSAYLIIRGMKTLALRMRQQQHSARALAEFLCTEPLVESVNYPGLPSH
PNHAVACAQMSGFGAIVSFVLAGGMDTVKLLLPRLRFAHCAGNLGAVETIYGPARTTSHV
ENTLEERQALGISEGLVRVSVGIEDTDDLLDDLKQAFAFVKKTLDPQLNEVLTETAT
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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