SitesBLAST
Comparing WP_013836024.1 NCBI__GCF_000214825.1:WP_013836024.1 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)
7kb1C Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
54% identity, 99% coverage: 5:425/426 of query aligns to 9:427/428 of 7kb1C
- binding pyridoxal-5'-phosphate: Y57 (= Y52), R59 (= R54)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: G87 (= G82), Q88 (≠ M83), Y112 (= Y107), N160 (= N155), D185 (= D180), S206 (= S202), T208 (= T204), K209 (= K205), N369 (= N367), I370 (= I368), R404 (= R402)
7kb1A Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
54% identity, 99% coverage: 5:425/426 of query aligns to 9:427/428 of 7kb1A
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y57 (= Y52), R59 (= R54), G87 (= G82), Q88 (≠ M83), Y112 (= Y107), N160 (= N155), D185 (= D180), S206 (= S202), T208 (= T204), K209 (= K205), N369 (= N367), I370 (= I368), R404 (= R402)
2ctzA Crystal structure of o-acetyl homoserine sulfhydrylase from thermus thermophilus hb8
50% identity, 99% coverage: 1:421/426 of query aligns to 1:420/421 of 2ctzA
- active site: R54 (= R54), Y107 (= Y107), D180 (= D180), K206 (= K205)
- binding pyridoxal-5'-phosphate: S81 (= S81), G82 (= G82), H83 (≠ M83), Q86 (≠ I86), Y107 (= Y107), D180 (= D180), T182 (= T182), S203 (= S202), T205 (= T204), K206 (= K205)
Q5SK88 O-acetyl-L-homoserine sulfhydrylase 1; OAH-sulfhydrylase 1; EC 2.5.1.- from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
50% identity, 99% coverage: 1:421/426 of query aligns to 1:420/421 of Q5SK88
- K206 (= K205) modified: N6-(pyridoxal phosphate)lysine
O13326 Homocysteine synthase; O-acetylhomoserine sulfhydrylase; OAH SHL; OAH sulfhydrylase; EC 2.5.1.49 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
53% identity, 98% coverage: 3:421/426 of query aligns to 8:426/429 of O13326
- G411 (= G406) mutation to D: Impairs homocysteine synthase activity.
8erjB Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
52% identity, 99% coverage: 2:421/426 of query aligns to 4:423/428 of 8erjB
- binding (2S)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]but-3-enoic acid: G84 (= G82), Q85 (≠ M83), Q88 (≠ I86), Y109 (= Y107), D181 (= D180), S204 (= S202), K207 (= K205), A368 (≠ V366), N369 (= N367), T384 (= T382), R404 (= R402)
8erjA Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
52% identity, 99% coverage: 2:421/426 of query aligns to 4:423/428 of 8erjA
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: S83 (= S81), G84 (= G82), Q85 (≠ M83), Q88 (≠ I86), Y109 (= Y107), N156 (= N155), D181 (= D180), S204 (= S202), T206 (= T204), K207 (= K205), R404 (= R402)
8erbK Crystal structure of fub7 in complex with vinylglycine ketimine (see paper)
52% identity, 99% coverage: 2:421/426 of query aligns to 5:424/429 of 8erbK
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y55 (= Y52), R57 (= R54), G85 (= G82), Q86 (≠ M83), Q89 (≠ I86), Y110 (= Y107), N157 (= N155), D182 (= D180), S205 (= S202), T207 (= T204), K208 (= K205), T385 (= T382), R405 (= R402)
8wkoA Crystal structure of o-acetylhomoserine sulfhydrylase from lactobacillus plantarum in the closed form (see paper)
47% identity, 98% coverage: 3:421/426 of query aligns to 9:422/425 of 8wkoA
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: G87 (= G82), S88 (≠ M83), Y112 (= Y107), E155 (= E151), D184 (= D180), T186 (= T182), S206 (= S202), A207 (= A203), T208 (= T204), F209 (≠ Y206), G212 (= G209), M217 (≠ I214), V369 (≠ I368), A370 (≠ G369)
- binding proline: H213 (= H210), Q284 (= Q283), S288 (≠ T287)
8ovhA Crystal structure of o-acetyl-l-homoserine sulfhydrolase from saccharomyces cerevisiae in complex with pyridoxal-5'-phosphate (see paper)
45% identity, 98% coverage: 3:421/426 of query aligns to 5:391/400 of 8ovhA
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
38% identity, 98% coverage: 3:421/426 of query aligns to 8:392/396 of 4hf8A
- active site: R59 (= R54), Y112 (= Y107), D184 (= D180), K209 (= K205)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G82), I88 (≠ M83), Y112 (= Y107), E155 (= E151), N159 (= N155), D184 (= D180), S206 (= S202), K209 (= K205), S338 (≠ N367), R373 (= R402)
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
41% identity, 99% coverage: 5:424/426 of query aligns to 6:391/392 of 5x2xA
- active site: R55 (= R54), Y108 (= Y107), D180 (= D180), K205 (= K205)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y52), R55 (= R54), G83 (= G82), M84 (= M83), Y108 (= Y107), N155 (= N155), D180 (= D180), S202 (= S202), T204 (= T204), K205 (= K205), V333 (= V366), S334 (≠ N367), R369 (= R402)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
41% identity, 99% coverage: 5:424/426 of query aligns to 6:391/392 of 5x2wA
- active site: R55 (= R54), Y108 (= Y107), D180 (= D180), K205 (= K205)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y52), R55 (= R54), S82 (= S81), G83 (= G82), M84 (= M83), Y108 (= Y107), D180 (= D180), S202 (= S202), K205 (= K205), V333 (= V366), S334 (≠ N367), R369 (= R402)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
41% identity, 99% coverage: 5:424/426 of query aligns to 12:397/398 of 1pg8A
- active site: R61 (= R54), Y114 (= Y107), D186 (= D180), K211 (= K205)
- binding pyridoxal-5'-phosphate: Y59 (= Y52), R61 (= R54), S88 (= S81), G89 (= G82), M90 (= M83), Y114 (= Y107), D186 (= D180), S208 (= S202), T210 (= T204), K211 (= K205)
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, 99% coverage: 5:424/426 of query aligns to 12:397/398 of P13254
- YSR 59:61 (= YSR 52:54) binding pyridoxal 5'-phosphate
- R61 (= R54) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 82:83) binding in other chain
- Y114 (= Y107) binding substrate
- C116 (≠ G109) 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 202:204) binding in other chain
- K211 (= K205) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R267) 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 (≠ N268) 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 (= R402) binding substrate
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
41% identity, 99% coverage: 5:424/426 of query aligns to 11:396/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
41% identity, 99% coverage: 5:424/426 of query aligns to 7:392/393 of 5x30C
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
38% identity, 98% coverage: 3:421/426 of query aligns to 7:391/395 of 5m3zA
- active site: R58 (= R54), Y111 (= Y107), D183 (= D180), K208 (= K205)
- binding norleucine: Y111 (= Y107), H113 (≠ G109), K208 (= K205), V336 (= V366), S337 (≠ N367)
- binding pyridoxal-5'-phosphate: G86 (= G82), I87 (≠ M83), Y111 (= Y107), E154 (= E151), D183 (= D180), T185 (= T182), S205 (= S202), T207 (= T204), K208 (= K205)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G82), I87 (≠ M83), Y111 (= Y107), D183 (= D180), S205 (= S202), T207 (= T204), K208 (= K205), V336 (= V366), S337 (≠ N367), R372 (= R402)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
38% identity, 98% coverage: 3:421/426 of query aligns to 8:392/396 of 4omaA
- active site: R59 (= R54), Y112 (= Y107), D184 (= D180), K209 (= K205)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G82), I88 (≠ M83), Y112 (= Y107), D184 (= D180), S206 (= S202), T208 (= T204), K209 (= K205), V337 (= V366), S338 (≠ N367), R373 (= R402)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
38% identity, 98% coverage: 3:421/426 of query aligns to 8:392/396 of 3jwbA
Query Sequence
>WP_013836024.1 NCBI__GCF_000214825.1:WP_013836024.1
MKLETIALHGGYKPEDTTKSVAVPIYQTTSFAFDDAQHAADLFDLKVAGNIYSRIMNPTN
AVLETRIAAMEGGIAGLAVSSGMAAITYTIQTLAEAGDNILSTGELYGGSYNLFAHTLPR
QGLEVRFFNKDAPDQDIAQLIDANTKLLYCETVGNPSGGIADIERLAKLAHQHGIPLVVD
STVATPALWRPIEQGADIVIHSATKYIGGHGTTIGGVIVDSGKFPWAEHAERFPLLNTPD
VSYHGVTYTQDFGAAAFIARARVVPLRNMGAALSPMNAFQLMQGLETLALRMERVCENAH
KVAEFLEEQPLVSWVNYAGLASHKDHQLAQKYMQGKASGILSFGLKSGREGTRKFYDALQ
MILRLVNIGDAKSCASIPAETTHRQLNDVELKAAGVSPDMVRLSIGIEHIDDILADIDQA
LMASKA
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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