SitesBLAST
Comparing WP_012102027.1 NCBI__GCF_000016505.1:WP_012102027.1 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)
P0DXC4 Canavanine gamma-lyase; CangammaL; EC 4.4.1.43 from Pseudomonas canavaninivorans (see paper)
54% identity, 97% coverage: 11:390/393 of query aligns to 15:398/400 of P0DXC4
- K213 (= K209) mutation to A: Loss of activity.
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
41% identity, 98% coverage: 3:389/393 of query aligns to 2:394/396 of 6egrA
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
41% identity, 98% coverage: 3:389/393 of query aligns to 2:394/396 of 4omaA
- active site: R59 (= R58), Y112 (= Y111), D184 (= D184), K209 (= K209)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G86), I88 (≠ V87), Y112 (= Y111), D184 (= D184), S206 (= S206), T208 (= T208), K209 (= K209), V337 (= V336), S338 (= S337), R373 (= R368)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
41% identity, 98% coverage: 3:389/393 of query aligns to 2:394/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
41% identity, 98% coverage: 3:389/393 of query aligns to 2:394/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
41% identity, 98% coverage: 3:389/393 of query aligns to 2:394/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
41% identity, 98% coverage: 3:389/393 of query aligns to 1:393/395 of 5m3zA
- active site: R58 (= R58), Y111 (= Y111), D183 (= D184), K208 (= K209)
- binding norleucine: Y111 (= Y111), H113 (≠ A113), K208 (= K209), V336 (= V336), S337 (= S337)
- binding pyridoxal-5'-phosphate: G86 (= G86), I87 (≠ V87), Y111 (= Y111), E154 (= E155), D183 (= D184), T185 (= T186), S205 (= S206), T207 (= T208), K208 (= K209)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G86), I87 (≠ V87), Y111 (= Y111), D183 (= D184), S205 (= S206), T207 (= T208), K208 (= K209), V336 (= V336), S337 (= S337), R372 (= R368)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
41% identity, 98% coverage: 3:389/393 of query aligns to 2:394/396 of 4hf8A
- active site: R59 (= R58), Y112 (= Y111), D184 (= D184), K209 (= K209)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G86), I88 (≠ V87), Y112 (= Y111), E155 (= E155), N159 (= N159), D184 (= D184), S206 (= S206), K209 (= K209), S338 (= S337), R373 (= R368)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
41% identity, 98% coverage: 3:389/393 of query aligns to 2:383/386 of 3mkjA
- active site: Y101 (= Y111), D173 (= D184), K198 (= K209)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G86), I77 (≠ V87), Y101 (= Y111), E144 (= E155), D173 (= D184), F176 (= F187), S195 (= S206), T197 (= T208), K198 (= K209)
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
42% identity, 97% coverage: 7:387/393 of query aligns to 6:394/399 of 5dx5A
- active site: R59 (= R58), Y112 (= Y111), D186 (= D184), K211 (= K209)
- binding pyridoxal-5'-phosphate: Y57 (= Y56), R59 (= R58), S86 (= S85), G87 (= G86), M88 (≠ V87), Y112 (= Y111), D186 (= D184), F189 (= F187), S208 (= S206), T210 (= T208), K211 (= K209)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
37% identity, 97% coverage: 9:388/393 of query aligns to 10:395/398 of 1pg8A
- active site: R61 (= R58), Y114 (= Y111), D186 (= D184), K211 (= K209)
- binding pyridoxal-5'-phosphate: Y59 (= Y56), R61 (= R58), S88 (= S85), G89 (= G86), M90 (≠ V87), Y114 (= Y111), D186 (= D184), S208 (= S206), T210 (= T208), K211 (= K209)
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, 97% coverage: 9:388/393 of query aligns to 10:395/398 of P13254
- YSR 59:61 (≠ YTR 56:58) binding pyridoxal 5'-phosphate
- R61 (= R58) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (≠ GV 86:87) binding in other chain
- Y114 (= Y111) binding substrate
- C116 (≠ A113) 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 206:208) binding in other chain
- K211 (= K209) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ V238) 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 (≠ N239) 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 (= R368) binding substrate
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
37% identity, 97% coverage: 9:388/393 of query aligns to 4:389/392 of 5x2xA
- active site: R55 (= R58), Y108 (= Y111), D180 (= D184), K205 (= K209)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y56), R55 (= R58), G83 (= G86), M84 (≠ V87), Y108 (= Y111), N155 (= N159), D180 (= D184), S202 (= S206), T204 (= T208), K205 (= K209), V333 (= V336), S334 (= S337), R369 (= R368)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
37% identity, 97% coverage: 9:388/393 of query aligns to 4:389/392 of 5x2wA
- active site: R55 (= R58), Y108 (= Y111), D180 (= D184), K205 (= K209)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y56), R55 (= R58), S82 (= S85), G83 (= G86), M84 (≠ V87), Y108 (= Y111), D180 (= D184), S202 (= S206), K205 (= K209), V333 (= V336), S334 (= S337), R369 (= R368)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
37% identity, 97% coverage: 9:388/393 of query aligns to 9:394/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
37% identity, 97% coverage: 9:388/393 of query aligns to 5:390/393 of 5x30C
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
41% identity, 96% coverage: 11:387/393 of query aligns to 7:389/393 of 1e5fA
- active site: R55 (= R58), Y108 (= Y111), D181 (= D184), K206 (= K209)
- binding pyridoxal-5'-phosphate: Y53 (= Y56), R55 (= R58), G83 (= G86), M84 (≠ V87), Y108 (= Y111), D181 (= D184), S203 (= S206), K206 (= K209)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
41% identity, 96% coverage: 11:387/393 of query aligns to 7:389/394 of 1e5eA
- active site: R55 (= R58), Y108 (= Y111), D181 (= D184), K206 (= K209)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y56), R55 (= R58), G83 (= G86), M84 (≠ V87), Y108 (= Y111), N155 (= N159), D181 (= D184), S203 (= S206), T205 (= T208), K206 (= K209), S335 (= S337), T350 (≠ R354), R370 (= R368)
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
40% identity, 96% coverage: 11:389/393 of query aligns to 5:372/373 of 4l0oH
- active site: R40 (= R58), Y92 (= Y111), D164 (= D184), K189 (= K209)
- binding pyridoxal-5'-phosphate: Y38 (= Y56), R40 (= R58), S67 (= S85), G68 (= G86), L69 (≠ V87), Y92 (= Y111), D164 (= D184), S186 (= S206), T188 (= T208), K189 (= K209)
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)
38% identity, 97% coverage: 7:387/393 of query aligns to 2:380/381 of 4iyoB
- active site: R47 (= R58), Y99 (= Y111), D172 (= D184), K197 (= K209)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y56), R47 (= R58)
- binding amino-acrylate: Y99 (= Y111), K197 (= K209), S326 (= S337), T341 (≠ R354), R361 (= R368)
- binding pyruvic acid: Q221 (≠ I232), F224 (≠ E235)
- binding serine: Y45 (= Y56), T48 (≠ N59), Y99 (= Y111), R104 (= R116), N227 (≠ V238), E325 (≠ V336)
Query Sequence
>WP_012102027.1 NCBI__GCF_000016505.1:WP_012102027.1
MIDDNNIDFITKCIHVGNGIDKETGAIRRPITMANCYRLPEDASSINWSDADQLLYTRNT
SANQVYLQEKLASLEGGEDCVVLASGVSALAGVFFSFLNKESHVICSNVSYIAVYRLLNE
YLPDKYGIQTSFVDTSNLEEIKKAIRPNTKLIHIETPGNPTTKISDIEEISKIVKSIGAL
LSVDSTFASPFLQRPLQLGADLVIHSLTKYINGHGDAMGGAVIGKKELIDKIKREAMVNL
GGTISPFNAWLIMRGVVTLPLRMKQHSDTALEVAEFLESNPVVKFVAYPGLESHPQHNIA
KKQMNMYSGIIAFALKADVDTHNKFINSLKLITQAVSLGHDESLIVYTGPNDERINFYPE
QFREGYIRFSIGLESASDIIADLKQALKKCGLQ
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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