SitesBLAST
Comparing WP_083536388.1 NCBI__GCF_001579945.1:WP_083536388.1 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)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
42% identity, 88% coverage: 40:403/412 of query aligns to 28:394/398 of 1pg8A
- active site: R61 (= R73), Y114 (= Y126), D186 (= D199), K211 (= K222)
- binding pyridoxal-5'-phosphate: Y59 (= Y71), R61 (= R73), S88 (= S100), G89 (= G101), M90 (≠ V102), Y114 (= Y126), D186 (= D199), S208 (= S219), T210 (= T221), K211 (= K222)
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)
42% identity, 88% coverage: 40:403/412 of query aligns to 28:394/398 of P13254
- YSR 59:61 (= YSR 71:73) binding
- R61 (= R73) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (≠ GV 101:102) binding in other chain
- Y114 (= Y126) binding
- C116 (≠ P128) 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 219:221) binding in other chain
- K211 (= K222) modified: N6-(pyridoxal phosphate)lysine
- K240 (vs. gap) 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 (vs. gap) 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 (= R384) binding
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
42% identity, 88% coverage: 40:403/412 of query aligns to 27:393/397 of 3vk3A
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
42% identity, 88% coverage: 40:403/412 of query aligns to 22:388/392 of 5x2xA
- active site: R55 (= R73), Y108 (= Y126), D180 (= D199), K205 (= K222)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y71), R55 (= R73), G83 (= G101), M84 (≠ V102), Y108 (= Y126), N155 (= N174), D180 (= D199), S202 (= S219), T204 (= T221), K205 (= K222), V333 (≠ A348), S334 (= S349), R369 (= R384)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
42% identity, 88% coverage: 40:403/412 of query aligns to 22:388/392 of 5x2wA
- active site: R55 (= R73), Y108 (= Y126), D180 (= D199), K205 (= K222)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y71), R55 (= R73), S82 (= S100), G83 (= G101), M84 (≠ V102), Y108 (= Y126), D180 (= D199), S202 (= S219), K205 (= K222), V333 (≠ A348), S334 (= S349), R369 (= R384)
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
42% identity, 88% coverage: 40:403/412 of query aligns to 23:389/393 of 5x30C
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
38% identity, 89% coverage: 40:406/412 of query aligns to 26:395/396 of 4omaA
- active site: R59 (= R73), Y112 (= Y126), D184 (= D199), K209 (= K222)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G101), I88 (≠ V102), Y112 (= Y126), D184 (= D199), S206 (= S219), T208 (= T221), K209 (= K222), V337 (≠ A348), S338 (= S349), R373 (= R384)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
38% identity, 89% coverage: 40:406/412 of query aligns to 26:395/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
38% identity, 89% coverage: 40:406/412 of query aligns to 26:395/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
38% identity, 89% coverage: 40:406/412 of query aligns to 26:395/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
38% identity, 89% coverage: 40:406/412 of query aligns to 25:394/395 of 5m3zA
- active site: R58 (= R73), Y111 (= Y126), D183 (= D199), K208 (= K222)
- binding norleucine: Y111 (= Y126), H113 (≠ P128), K208 (= K222), V336 (≠ A348), S337 (= S349)
- binding pyridoxal-5'-phosphate: G86 (= G101), I87 (≠ V102), Y111 (= Y126), E154 (= E170), D183 (= D199), T185 (= T201), S205 (= S219), T207 (= T221), K208 (= K222)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G101), I87 (≠ V102), Y111 (= Y126), D183 (= D199), S205 (= S219), T207 (= T221), K208 (= K222), V336 (≠ A348), S337 (= S349), R372 (= R384)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
38% identity, 89% coverage: 40:406/412 of query aligns to 26:395/396 of 6egrA
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
38% identity, 89% coverage: 40:406/412 of query aligns to 26:395/396 of 4hf8A
- active site: R59 (= R73), Y112 (= Y126), D184 (= D199), K209 (= K222)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G101), I88 (≠ V102), Y112 (= Y126), E155 (= E170), N159 (= N174), D184 (= D199), S206 (= S219), K209 (= K222), S338 (= S349), R373 (= R384)
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
38% identity, 88% coverage: 40:403/412 of query aligns to 26:394/399 of 5dx5A
- active site: R59 (= R73), Y112 (= Y126), D186 (= D199), K211 (= K222)
- binding pyridoxal-5'-phosphate: Y57 (= Y71), R59 (= R73), S86 (= S100), G87 (= G101), M88 (≠ V102), Y112 (= Y126), D186 (= D199), F189 (= F202), S208 (= S219), T210 (= T221), K211 (= K222)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
38% identity, 89% coverage: 40:406/412 of query aligns to 26:384/386 of 3mkjA
- active site: Y101 (= Y126), D173 (= D199), K198 (= K222)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G101), I77 (≠ V102), Y101 (= Y126), E144 (= E170), D173 (= D199), F176 (= F202), S195 (= S219), T197 (= T221), K198 (= K222)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
36% identity, 88% coverage: 41:403/412 of query aligns to 23:389/394 of 1e5eA
- active site: R55 (= R73), Y108 (= Y126), D181 (= D199), K206 (= K222)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y71), R55 (= R73), G83 (= G101), M84 (≠ V102), Y108 (= Y126), N155 (= N174), D181 (= D199), S203 (= S219), T205 (= T221), K206 (= K222), S335 (= S349), T350 (≠ W364), R370 (= R384)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
36% identity, 88% coverage: 41:403/412 of query aligns to 23:389/393 of 1e5fA
- active site: R55 (= R73), Y108 (= Y126), D181 (= D199), K206 (= K222)
- binding pyridoxal-5'-phosphate: Y53 (= Y71), R55 (= R73), G83 (= G101), M84 (≠ V102), Y108 (= Y126), D181 (= D199), S203 (= S219), K206 (= K222)
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)
38% identity, 88% coverage: 40:403/412 of query aligns to 22:380/384 of 4iyoD
- active site: R47 (= R73), Y99 (= Y126), D172 (= D199), K197 (= K222)
- binding serine: Y45 (= Y71), T48 (≠ V74), Y99 (= Y126), Y99 (= Y126), R104 (≠ Y131), K197 (= K222), N227 (≠ I250), E325 (≠ A348), S326 (= S349), T341 (≠ W364), R361 (= R384)
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, 88% coverage: 43:403/412 of query aligns to 25:380/381 of 4iyoB
- active site: R47 (= R73), Y99 (= Y126), D172 (= D199), K197 (= K222)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y71), R47 (= R73)
- binding amino-acrylate: Y99 (= Y126), K197 (= K222), S326 (= S349), T341 (≠ W364), R361 (= R384)
- binding pyruvic acid: Q221 (≠ A244), F224 (≠ T247)
- binding serine: Y45 (= Y71), T48 (≠ V74), Y99 (= Y126), R104 (≠ Y131), N227 (≠ I250), E325 (≠ A348)
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, 88% coverage: 43:403/412 of query aligns to 25:380/381 of 4iy7B
- active site: R47 (= R73), Y99 (= Y126), D172 (= D199), K197 (= K222)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y71), R47 (= R73)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: G75 (= G101), M76 (≠ V102), Y99 (= Y126), E143 (= E170), N147 (= N174), D172 (= D199), S194 (= S219), K197 (= K222), S326 (= S349), L327 (= L350), T341 (≠ W364), R361 (= R384)
- binding pyruvic acid: Q221 (≠ A244), F224 (≠ T247)
- binding serine: Y45 (= Y71), T48 (≠ V74), Y99 (= Y126), R104 (≠ Y131), N227 (≠ I250), E325 (≠ A348)
Query Sequence
>WP_083536388.1 NCBI__GCF_001579945.1:WP_083536388.1
MQGADGCPAQKPRDWSRPMKNSTRLNHPPIVAVATDNRPLVAPIYQSVKFTFDDVVQTQR
HSRGEREGFAYSRVSNPTLQQLELTLAQLQGRDACLLTASGVAAVNLAMLSLCKQGDHVV
SFAELYQPTRYMIRRLLGRYGVSHTILSLEDIEGIEQLLASTPTRLVMFESPSNPVLKIA
DIGRITAAARAHGALTVMDNTFAGFHNHGQFDIDVYVHSLTKYAGGHGDVMGGAVIARQE
LIDAMRTDFIVMGATLDPHAAFLIQRGMKTYALRYERQCDNASKVARWLASQPGVARVRY
PGLAAHPQYALARAQMHDFGTVVTVDLEGGETAVNRFSEALRLFTISASLGSTESLVQPG
RLMWPSDLDAIQRQWAEITAATMRLSIGIEDVEDLLEDMRQALHQAGRAAPV
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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