SitesBLAST
Comparing WP_041773934.1 NCBI__GCF_000284315.1:WP_041773934.1 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)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
42% identity, 97% coverage: 13:400/402 of query aligns to 5:392/396 of 4hf8A
- active site: R59 (= R66), Y112 (= Y119), D184 (= D194), K209 (= K219)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G94), I88 (≠ M95), Y112 (= Y119), E155 (= E165), N159 (= N169), D184 (= D194), S206 (= S216), K209 (= K219), S338 (= S346), R373 (= R381)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
42% identity, 97% coverage: 13:400/402 of query aligns to 5:392/396 of 4omaA
- active site: R59 (= R66), Y112 (= Y119), D184 (= D194), K209 (= K219)
- 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 (= D194), S206 (= S216), T208 (= T218), K209 (= K219), V337 (= V345), S338 (= S346), R373 (= R381)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
42% identity, 97% coverage: 13:400/402 of query aligns to 5:392/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
42% identity, 97% coverage: 13:400/402 of query aligns to 5:392/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
42% identity, 97% coverage: 13:400/402 of query aligns to 5:392/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
42% identity, 97% coverage: 13:400/402 of query aligns to 4:391/395 of 5m3zA
- active site: R58 (= R66), Y111 (= Y119), D183 (= D194), K208 (= K219)
- binding norleucine: Y111 (= Y119), H113 (≠ G121), K208 (= K219), V336 (= V345), S337 (= S346)
- binding pyridoxal-5'-phosphate: G86 (= G94), I87 (≠ M95), Y111 (= Y119), E154 (= E165), D183 (= D194), T185 (= T196), S205 (= S216), T207 (= T218), K208 (= K219)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G94), I87 (≠ M95), Y111 (= Y119), D183 (= D194), S205 (= S216), T207 (= T218), K208 (= K219), V336 (= V345), S337 (= S346), R372 (= R381)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
42% identity, 97% coverage: 13:400/402 of query aligns to 5:392/396 of 6egrA
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
44% identity, 97% coverage: 14:402/402 of query aligns to 3:391/393 of 5x30C
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
44% identity, 97% coverage: 14:402/402 of query aligns to 7:395/397 of 3vk3A
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
44% identity, 97% coverage: 14:402/402 of query aligns to 2:390/392 of 5x2xA
- active site: R55 (= R66), Y108 (= Y119), D180 (= D194), K205 (= K219)
- 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 (= N169), D180 (= D194), S202 (= S216), T204 (= T218), K205 (= K219), V333 (= V345), S334 (= S346), R369 (= R381)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
44% identity, 97% coverage: 14:402/402 of query aligns to 2:390/392 of 5x2wA
- active site: R55 (= R66), Y108 (= Y119), D180 (= D194), K205 (= K219)
- 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 (= D194), S202 (= S216), K205 (= K219), V333 (= V345), S334 (= S346), R369 (= R381)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
44% identity, 97% coverage: 14:402/402 of query aligns to 8:396/398 of 1pg8A
- active site: R61 (= R66), Y114 (= Y119), D186 (= D194), K211 (= K219)
- binding pyridoxal-5'-phosphate: Y59 (= Y64), R61 (= R66), S88 (= S93), G89 (= G94), M90 (= M95), Y114 (= Y119), D186 (= D194), S208 (= S216), T210 (= T218), K211 (= K219)
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)
44% identity, 97% coverage: 14:402/402 of query aligns to 8:396/398 of P13254
- YSR 59:61 (≠ YGR 64:66) binding pyridoxal 5'-phosphate
- 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 substrate
- 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 216:218) binding in other chain
- K211 (= K219) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ G247) 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 (≠ S248) 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 (= R381) binding substrate
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
43% identity, 98% coverage: 9:401/402 of query aligns to 1:395/399 of 5dx5A
- active site: R59 (= R66), Y112 (= Y119), D186 (= D194), K211 (= K219)
- binding pyridoxal-5'-phosphate: Y57 (= Y64), R59 (= R66), S86 (= S93), G87 (= G94), M88 (= M95), Y112 (= Y119), D186 (= D194), F189 (= F197), S208 (= S216), T210 (= T218), K211 (= K219)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
40% identity, 96% coverage: 16:402/402 of query aligns to 5:391/393 of 1e5fA
- active site: R55 (= R66), Y108 (= Y119), D181 (= D194), K206 (= K219)
- binding pyridoxal-5'-phosphate: Y53 (= Y64), R55 (= R66), G83 (= G94), M84 (= M95), Y108 (= Y119), D181 (= D194), S203 (= S216), K206 (= K219)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
40% identity, 96% coverage: 16:402/402 of query aligns to 5:391/394 of 1e5eA
- active site: R55 (= R66), Y108 (= Y119), D181 (= D194), K206 (= K219)
- 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 (= N169), D181 (= D194), S203 (= S216), T205 (= T218), K206 (= K219), S335 (= S346), T350 (≠ S361), R370 (= R381)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
41% identity, 97% coverage: 13:400/402 of query aligns to 5:381/386 of 3mkjA
- active site: Y101 (= Y119), D173 (= D194), K198 (= K219)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G94), I77 (≠ M95), Y101 (= Y119), E144 (= E165), D173 (= D194), F176 (= F197), S195 (= S216), T197 (= T218), K198 (= K219)
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
42% identity, 96% coverage: 17:400/402 of query aligns to 4:370/373 of 4l0oH
- active site: R40 (= R66), Y92 (= Y119), D164 (= D194), K189 (= K219)
- binding pyridoxal-5'-phosphate: Y38 (= Y64), R40 (= R66), S67 (= S93), G68 (= G94), L69 (≠ M95), Y92 (= Y119), D164 (= D194), S186 (= S216), T188 (= T218), K189 (= K219)
7d7oB Crystal structure of cystathionine gamma-lyase from bacillus cereus atcc 14579 (see paper)
41% identity, 96% coverage: 17:400/402 of query aligns to 4:376/377 of 7d7oB
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)
42% identity, 95% coverage: 18:400/402 of query aligns to 6:380/381 of 4iyoB
- active site: R47 (= R66), Y99 (= Y119), D172 (= D194), K197 (= K219)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y64), R47 (= R66)
- binding amino-acrylate: Y99 (= Y119), K197 (= K219), S326 (= S346), T341 (≠ S361), R361 (= R381)
- binding pyruvic acid: Q221 (≠ R241), F224 (= F244)
- binding serine: Y45 (= Y64), T48 (≠ M67), Y99 (= Y119), R104 (≠ A124), N227 (≠ G247), E325 (≠ V345)
Query Sequence
>WP_041773934.1 NCBI__GCF_000284315.1:WP_041773934.1
MGGKLKNKKNYLTPGPRTKCIHTSGPEDPWRALTPPLYQTSTFTFPDFDQVDRVLKGEEE
GFVYGRMGNPTTERFETLVSELEGGEKTRAFASGMGAISAILIHLTKSRPEMAFPKVLYG
GTRAFIEKYLIPQGCLIHWFDPREEGWGEELSRRLSPKTAAVFAETPSNPVMTVIDLGRL
SGIAKSAGVPLVVDNTFATPILQKPLALGADIVVHSATKYLGGHGDLLGGTVTGNASLME
RLSFEEGSYLGATLSPFHSWLLLRGMKTLPLRMEAHCRGAMNIAEFLSHHPMVKSVHYPG
LPGDPGHKVAALQMKGFGGMLSFSLGDDQKARKVASRLEFFKIAVSLGDPESLIEHPASL
SHRQMSPEGRMALGIDPGFLRVSVGLEDPEDLILDLKRALEA
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