SitesBLAST
Comparing WP_012709060.1 NCBI__GCF_000018545.1:WP_012709060.1 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)
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
37% identity, 94% coverage: 21:388/390 of query aligns to 12:393/393 of 5x30C
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
37% identity, 96% coverage: 15:388/390 of query aligns to 8:392/392 of 5x2xA
- active site: R55 (= R59), Y108 (= Y112), 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 (= G87), M84 (= M88), Y108 (= Y112), N155 (≠ S158), D180 (= D183), S202 (= S205), T204 (≠ S207), K205 (= K208), V333 (= V329), S334 (= S330), R369 (= R365)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
37% identity, 96% coverage: 15:388/390 of query aligns to 8:392/392 of 5x2wA
- active site: R55 (= R59), Y108 (= Y112), 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 (= S86), G83 (= G87), M84 (= M88), Y108 (= Y112), D180 (= D183), S202 (= S205), K205 (= K208), V333 (= V329), S334 (= S330), R369 (= R365)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
37% identity, 94% coverage: 21:388/390 of query aligns to 16:397/397 of 3vk3A
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
37% identity, 94% coverage: 21:388/390 of query aligns to 17:398/398 of 1pg8A
- active site: R61 (= R59), Y114 (= Y112), D186 (= D183), K211 (= K208)
- binding pyridoxal-5'-phosphate: Y59 (= Y57), R61 (= R59), S88 (= S86), G89 (= G87), M90 (= M88), Y114 (= Y112), D186 (= D183), S208 (= S205), T210 (≠ S207), 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)
37% identity, 94% coverage: 21:388/390 of query aligns to 17:398/398 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 87:88) binding in other chain
- Y114 (= Y112) binding substrate
- C116 (≠ D114) 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 (≠ SAS 205:207) binding in other chain
- K211 (= K208) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ P237) 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 (≠ Y238) 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 (= R365) binding substrate
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
38% identity, 92% coverage: 25:383/390 of query aligns to 20:369/373 of 4l0oH
- active site: R40 (= R59), Y92 (= Y112), D164 (= D183), K189 (= K208)
- binding pyridoxal-5'-phosphate: Y38 (= Y57), R40 (= R59), S67 (= S86), G68 (= G87), L69 (≠ M88), Y92 (= Y112), D164 (= D183), S186 (= S205), T188 (≠ S207), K189 (= K208)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
37% identity, 93% coverage: 25:388/390 of query aligns to 25:396/396 of 4omaA
- active site: R59 (= R59), Y112 (= Y112), 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 (= G87), I88 (≠ M88), Y112 (= Y112), D184 (= D183), S206 (= S205), T208 (≠ S207), K209 (= K208), V337 (= V329), S338 (= S330), R373 (= R365)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
37% identity, 93% coverage: 25:388/390 of query aligns to 25:396/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
37% identity, 93% coverage: 25:388/390 of query aligns to 25:396/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
37% identity, 93% coverage: 25:388/390 of query aligns to 25:396/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
37% identity, 93% coverage: 25:388/390 of query aligns to 24:395/395 of 5m3zA
- active site: R58 (= R59), Y111 (= Y112), D183 (= D183), K208 (= K208)
- binding norleucine: Y111 (= Y112), H113 (≠ D114), K208 (= K208), V336 (= V329), S337 (= S330)
- binding pyridoxal-5'-phosphate: G86 (= G87), I87 (≠ M88), Y111 (= Y112), E154 (= E154), D183 (= D183), T185 (≠ S185), S205 (= S205), T207 (≠ S207), K208 (= K208)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G87), I87 (≠ M88), Y111 (= Y112), D183 (= D183), S205 (= S205), T207 (≠ S207), K208 (= K208), V336 (= V329), S337 (= S330), R372 (= R365)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
37% identity, 93% coverage: 25:388/390 of query aligns to 25:396/396 of 6egrA
4iyoD Crystal structure of cystathionine gamma lyase from xanthomonas oryzae pv. Oryzae (xometc) in complex with e-site serine, a-site serine, a- site external aldimine structure with aminoacrylate and a-site iminopropionate intermediates (see paper)
39% identity, 92% coverage: 25:384/390 of query aligns to 21:380/384 of 4iyoD
- active site: R47 (= R59), Y99 (= Y112), D172 (= D183), K197 (= K208)
- binding serine: Y45 (= Y57), T48 (≠ G60), Y99 (= Y112), Y99 (= Y112), R104 (= R117), K197 (= K208), N227 (≠ P237), E325 (≠ V329), S326 (= S330), T341 (≠ L345), R361 (= R365)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
37% identity, 93% coverage: 25:388/390 of query aligns to 25:396/396 of 4hf8A
- active site: R59 (= R59), Y112 (= Y112), D184 (= D183), K209 (= K208)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G87), I88 (≠ M88), Y112 (= Y112), E155 (= E154), N159 (≠ S158), D184 (= D183), S206 (= S205), K209 (= K208), S338 (= S330), R373 (= R365)
4iyoB Crystal structure of cystathionine gamma lyase from xanthomonas oryzae pv. Oryzae (xometc) in complex with e-site serine, a-site serine, a- site external aldimine structure with aminoacrylate and a-site iminopropionate intermediates (see paper)
39% identity, 92% coverage: 25:384/390 of query aligns to 21:380/381 of 4iyoB
- active site: R47 (= R59), Y99 (= Y112), D172 (= D183), K197 (= K208)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y57), R47 (= R59)
- binding amino-acrylate: Y99 (= Y112), K197 (= K208), S326 (= S330), T341 (≠ L345), R361 (= R365)
- binding pyruvic acid: Q221 (≠ I231), F224 (≠ E234)
- binding serine: Y45 (= Y57), T48 (≠ G60), Y99 (= Y112), R104 (= R117), N227 (≠ P237), E325 (≠ V329)
4iy7B Crystal structure of cystathionine gamma lyase (xometc) from xanthomonas oryzae pv. Oryzae in complex with e-site serine, a-site external aldimine structure with serine and a-site external aldimine structure with aminoacrylate intermediates (see paper)
39% identity, 92% coverage: 25:384/390 of query aligns to 21:380/381 of 4iy7B
- active site: R47 (= R59), Y99 (= Y112), D172 (= D183), K197 (= K208)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y57), R47 (= R59)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: G75 (= G87), M76 (= M88), Y99 (= Y112), E143 (= E154), N147 (≠ S158), D172 (= D183), S194 (= S205), K197 (= K208), S326 (= S330), L327 (≠ W331), T341 (≠ L345), R361 (= R365)
- binding pyruvic acid: Q221 (≠ I231), F224 (≠ E234)
- binding serine: Y45 (= Y57), T48 (≠ G60), Y99 (= Y112), R104 (= R117), N227 (≠ P237), E325 (≠ V329)
4iy7A Crystal structure of cystathionine gamma lyase (xometc) from xanthomonas oryzae pv. Oryzae in complex with e-site serine, a-site external aldimine structure with serine and a-site external aldimine structure with aminoacrylate intermediates (see paper)
39% identity, 92% coverage: 25:384/390 of query aligns to 21:380/381 of 4iy7A
- active site: R47 (= R59), Y99 (= Y112), D172 (= D183), K197 (= K208)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: G75 (= G87), M76 (= M88), Y99 (= Y112), E143 (= E154), N147 (≠ S158), D172 (= D183), S194 (= S205), K197 (= K208), S326 (= S330), L327 (≠ W331), T341 (≠ L345), R361 (= R365)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: Y45 (= Y57), R47 (= R59)
- binding serine: Y45 (= Y57), T48 (≠ G60), Y99 (= Y112), R104 (= R117), N227 (≠ P237), E325 (≠ V329)
4ixzA Native structure of cystathionine gamma lyase (xometc) from xanthomonas oryzae pv. Oryzae at ph 9.0 (see paper)
39% identity, 92% coverage: 25:384/390 of query aligns to 21:380/381 of 4ixzA
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
35% identity, 96% coverage: 12:386/390 of query aligns to 8:391/393 of 1e5fA
- active site: R55 (= R59), Y108 (= Y112), D181 (= D183), K206 (= K208)
- binding pyridoxal-5'-phosphate: Y53 (= Y57), R55 (= R59), G83 (= G87), M84 (= M88), Y108 (= Y112), D181 (= D183), S203 (= S205), K206 (= K208)
Query Sequence
>WP_012709060.1 NCBI__GCF_000018545.1:WP_012709060.1
MNDGLDPFDRASLIAVHDEGHAFDAVVPPIVQTSLFTFKDYDEMIASYRGERVRPIYTRG
LNPTVRLFEEMLAKLEGAGDAIGFASGMSAISSTVLSFVEPGDRIVAVKHLYPDAFRLFG
THLKRMRIEVTYVDGRDEEEVAKALPGAKLFYMESPTSWVMDTHDVAALAALAKAQGIVT
VIDNSWASPVFQQPISLGVDLVIHSASKYLGGHSDVVAGVVAGSTELIGRIRSEAYPYLG
GKLSPFDAWLLIRGLRTLPIRMKAHERSALALARRLQDHPLVETVCHPGLGNHLPPGLLG
TSGLFSFIVRDGVDVRRFADHLQFFKLGVSWGGHESLIVPGEVVLAQKAQPNSAAAFGIS
PRSVRLHVGLEGTEALWSDLEAAIDAASSG
Or try a new SitesBLAST search
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