SitesBLAST
Comparing WP_092995230.1 NCBI__GCF_900102855.1:WP_092995230.1 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)
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)
42% identity, 95% coverage: 14:389/394 of query aligns to 180:560/563 of P55217
- T412 (≠ M241) natural variant: T -> P
- G459 (= G288) 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
1qgnA Cystathionine gamma-synthase from nicotiana tabacum (see paper)
43% identity, 95% coverage: 14:389/394 of query aligns to 15:395/398 of 1qgnA
- active site: R63 (= R59), Y116 (= Y111), D189 (= D183), K214 (= K208)
- binding pyridoxal-5'-phosphate: Y61 (= Y57), R63 (= R59), S90 (= S87), G91 (= G88), M92 (= M89), Y116 (= Y111), D189 (= D183), S211 (= S205), T213 (= T207), K214 (= K208), F342 (≠ L336)
1i48A Cystathionine gamma-synthase in complex with the inhibitor ctcpo (see paper)
43% identity, 95% coverage: 14:389/394 of query aligns to 13:393/396 of 1i48A
- active site: R61 (= R59), Y114 (= Y111), D187 (= D183), K212 (= K208)
- binding carboxymethylthio-3-(3-chlorophenyl)-1,2,4-oxadiazol: Y114 (= Y111), R115 (≠ G112), A337 (= A333), P338 (= P334), S339 (= S335), D348 (≠ T344), S354 (≠ T350), R374 (= R370), S376 (= S372)
- binding pyridoxal-5'-phosphate: Y59 (= Y57), R61 (= R59), S88 (= S87), G89 (= G88), M90 (= M89), Y114 (= Y111), D187 (= D183), S209 (= S205), T211 (= T207), K212 (= K208), F340 (≠ L336)
1i43A Cystathionine gamma-synthase in complex with the inhibitor ppca (see paper)
43% identity, 95% coverage: 14:389/394 of query aligns to 13:393/396 of 1i43A
- active site: R61 (= R59), Y114 (= Y111), D187 (= D183), K212 (= K208)
- binding pyridoxal-5'-phosphate: Y59 (= Y57), R61 (= R59), S88 (= S87), G89 (= G88), M90 (= M89), Y114 (= Y111), D187 (= D183), S209 (= S205), T211 (= T207), K212 (= K208), F340 (≠ L336)
- binding 3-(phosphonomethyl)pyridine-2-carboxylic acid: E58 (≠ L56), Y62 (= Y60), Y114 (= Y111), K212 (= K208), P338 (= P334), S354 (≠ T350), R374 (= R370)
1i41A Cystathionine gamma-synthase in complex with the inhibitor appa (see paper)
43% identity, 95% coverage: 14:389/394 of query aligns to 13:393/396 of 1i41A
- active site: R61 (= R59), Y114 (= Y111), D187 (= D183), K212 (= K208)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-imino]-5-phosphono-pent-3-enoic acid: E58 (≠ L56), Y59 (= Y57), R61 (= R59), Y62 (= Y60), G89 (= G88), M90 (= M89), Y114 (= Y111), E158 (= E154), D187 (= D183), T189 (= T185), S209 (= S205), T211 (= T207), K212 (= K208), P338 (= P334), S339 (= S335), R374 (= R370)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
40% identity, 97% coverage: 7:389/394 of query aligns to 3:389/394 of 1e5eA
- active site: R55 (= R59), Y108 (= Y111), D181 (= D183), K206 (= K208)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y57), R55 (= R59), G83 (= G88), M84 (= M89), Y108 (= Y111), N155 (= N158), D181 (= D183), S203 (= S205), T205 (= T207), K206 (= K208), S335 (= S335), T350 (= T350), R370 (= R370)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
40% identity, 97% coverage: 7:389/394 of query aligns to 3:389/393 of 1e5fA
- active site: R55 (= R59), Y108 (= Y111), D181 (= D183), K206 (= K208)
- binding pyridoxal-5'-phosphate: Y53 (= Y57), R55 (= R59), G83 (= G88), M84 (= M89), Y108 (= Y111), D181 (= D183), S203 (= S205), K206 (= K208)
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
42% identity, 97% coverage: 7:390/394 of query aligns to 1:371/373 of 4l0oH
- active site: R40 (= R59), Y92 (= Y111), D164 (= D183), K189 (= K208)
- binding pyridoxal-5'-phosphate: Y38 (= Y57), R40 (= R59), S67 (= S87), G68 (= G88), L69 (≠ M89), Y92 (= Y111), D164 (= D183), S186 (= S205), T188 (= T207), K189 (= K208)
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
41% identity, 98% coverage: 7:391/394 of query aligns to 6:396/399 of 5dx5A
- active site: R59 (= R59), Y112 (= Y111), D186 (= D183), K211 (= K208)
- binding pyridoxal-5'-phosphate: Y57 (= Y57), R59 (= R59), S86 (= S87), G87 (= G88), M88 (= M89), Y112 (= Y111), D186 (= D183), F189 (= F186), S208 (= S205), T210 (= T207), K211 (= K208)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
41% identity, 98% coverage: 9:393/394 of query aligns to 9:397/397 of 3vk3A
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
41% identity, 98% coverage: 9:393/394 of query aligns to 10:398/398 of 1pg8A
- active site: R61 (= R59), Y114 (= Y111), D186 (= D183), K211 (= K208)
- binding pyridoxal-5'-phosphate: Y59 (= Y57), R61 (= R59), S88 (= S87), G89 (= G88), M90 (= M89), Y114 (= Y111), D186 (= D183), S208 (= S205), T210 (= T207), K211 (= K208)
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)
41% identity, 98% coverage: 9:393/394 of query aligns to 10:398/398 of P13254
- YSR 59:61 (≠ YTR 57:59) binding pyridoxal 5'-phosphate
- R61 (= R59) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 88:89) binding in other chain
- Y114 (= Y111) binding substrate
- C116 (≠ G113) 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 205:207) binding in other chain
- K211 (= K208) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R235) 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 (≠ K236) 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 (= R370) binding substrate
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
41% identity, 98% coverage: 9:393/394 of query aligns to 4:392/392 of 5x2xA
- active site: R55 (= R59), Y108 (= Y111), D180 (= D183), K205 (= K208)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y57), R55 (= R59), G83 (= G88), M84 (= M89), Y108 (= Y111), N155 (= N158), D180 (= D183), S202 (= S205), T204 (= T207), K205 (= K208), V333 (≠ P334), S334 (= S335), R369 (= R370)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
41% identity, 98% coverage: 9:393/394 of query aligns to 4:392/392 of 5x2wA
- active site: R55 (= R59), Y108 (= Y111), D180 (= D183), K205 (= K208)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y57), R55 (= R59), S82 (= S87), G83 (= G88), M84 (= M89), Y108 (= Y111), D180 (= D183), S202 (= S205), K205 (= K208), V333 (≠ P334), S334 (= S335), R369 (= R370)
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
41% identity, 98% coverage: 9:393/394 of query aligns to 5:393/393 of 5x30C
7d7oB Crystal structure of cystathionine gamma-lyase from bacillus cereus atcc 14579 (see paper)
38% identity, 97% coverage: 7:390/394 of query aligns to 1:377/377 of 7d7oB
5x5hA Crystal structure of metb from corynebacterium glutamicum (see paper)
40% identity, 98% coverage: 3:390/394 of query aligns to 2:382/385 of 5x5hA
- active site: R52 (= R59), Y105 (= Y111), D177 (= D183), K202 (= K208)
- binding magnesium ion: F36 (= F36), Q38 (≠ F38), E49 (≠ L56), E69 (= E77), Q187 (= Q193), P188 (= P194), L189 (= L195)
- binding pyridoxal-5'-phosphate: G80 (= G88), M81 (= M89), Y105 (= Y111), D177 (= D183), S199 (= S205), T201 (= T207), K202 (= K208)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
38% identity, 97% coverage: 11:393/394 of query aligns to 10:396/396 of 4hf8A
- active site: R59 (= R59), Y112 (= Y111), D184 (= D183), K209 (= K208)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G88), I88 (≠ M89), Y112 (= Y111), E155 (= E154), N159 (= N158), D184 (= D183), S206 (= S205), K209 (= K208), S338 (= S335), R373 (= R370)
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
38% identity, 97% coverage: 11:393/394 of query aligns to 9:395/395 of 5m3zA
- active site: R58 (= R59), Y111 (= Y111), D183 (= D183), K208 (= K208)
- binding norleucine: Y111 (= Y111), H113 (≠ G113), K208 (= K208), V336 (≠ P334), S337 (= S335)
- binding pyridoxal-5'-phosphate: G86 (= G88), I87 (≠ M89), Y111 (= Y111), E154 (= E154), D183 (= D183), T185 (= T185), S205 (= S205), T207 (= T207), K208 (= K208)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G88), I87 (≠ M89), Y111 (= Y111), D183 (= D183), S205 (= S205), T207 (= T207), K208 (= K208), V336 (≠ P334), S337 (= S335), R372 (= R370)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
38% identity, 97% coverage: 11:393/394 of query aligns to 10:396/396 of 4omaA
- active site: R59 (= R59), Y112 (= Y111), D184 (= D183), K209 (= K208)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G88), I88 (≠ M89), Y112 (= Y111), D184 (= D183), S206 (= S205), T208 (= T207), K209 (= K208), V337 (≠ P334), S338 (= S335), R373 (= R370)
Query Sequence
>WP_092995230.1 NCBI__GCF_900102855.1:WP_092995230.1
MHDKTPMHLATRCVHAGELDDAQGSPHTPLYTTTTFKFASTEAILDVVEGRAAGSLYTRY
GLNPTIQSLEAKLASLEGAEAAFAFCSGMAAETALFLAYGREGVVCIGDAYGGTLELLAD
QLPLFGIDTHLILGSELDRLEDLLAGGARLVFLETPTNPALEVFDLAAIAEKAHAHGALL
AVDNTFASPVNQQPLALGADFAVHSATKYLGGHSDLTAGALMGSQELLAPIFGWRKNLGS
MPAPETCNLLARSLRTLVVRVRQQNASAQAVAEAMQRHPRVRRVLYPGLPDFPGHDLAAK
QMSGFGGMLTIEVDADTEGTAAVVDRLKLFAIAPSLGGAESLVTQPVTTTHHGLSETERE
RRGINGAMVRLSVGLEDAEDLIADLEQALSVASG
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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