SitesBLAST
Comparing WP_011372397.1 NCBI__GCF_000012965.1:WP_011372397.1 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)
8wkoA Crystal structure of o-acetylhomoserine sulfhydrylase from lactobacillus plantarum in the closed form (see paper)
46% identity, 99% coverage: 3:419/421 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 (= G81), S88 (≠ M82), Y112 (= Y106), E155 (= E149), D184 (= D178), T186 (= T180), S206 (= S200), A207 (= A201), T208 (≠ S202), F209 (≠ Y204), G212 (= G207), M217 (≠ I212), V369 (≠ I366), A370 (≠ G367)
- binding proline: H213 (≠ Q208), Q284 (= Q281), S288 (≠ T285)
7kb1C Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
47% identity, 99% coverage: 5:419/421 of query aligns to 9:423/428 of 7kb1C
- binding pyridoxal-5'-phosphate: Y57 (= Y51), R59 (= R53)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: G87 (= G81), Q88 (≠ M82), Y112 (= Y106), N160 (= N153), D185 (= D178), S206 (= S200), T208 (≠ S202), K209 (= K203), N369 (= N365), I370 (= I366), R404 (= R400)
7kb1A Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
47% identity, 99% coverage: 5:419/421 of query aligns to 9:423/428 of 7kb1A
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y57 (= Y51), R59 (= R53), G87 (= G81), Q88 (≠ M82), Y112 (= Y106), N160 (= N153), D185 (= D178), S206 (= S200), T208 (≠ S202), K209 (= K203), N369 (= N365), I370 (= I366), R404 (= R400)
8erjB Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
46% identity, 100% coverage: 2:420/421 of query aligns to 4:424/428 of 8erjB
- binding (2S)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]but-3-enoic acid: G84 (= G81), Q85 (≠ M82), Q88 (≠ T85), Y109 (= Y106), D181 (= D178), S204 (= S200), K207 (= K203), A368 (≠ V364), N369 (= N365), T384 (= T380), R404 (= R400)
8erjA Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
46% identity, 100% coverage: 2:420/421 of query aligns to 4:424/428 of 8erjA
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: S83 (= S80), G84 (= G81), Q85 (≠ M82), Q88 (≠ T85), Y109 (= Y106), N156 (= N153), D181 (= D178), S204 (= S200), T206 (≠ S202), K207 (= K203), R404 (= R400)
8erbK Crystal structure of fub7 in complex with vinylglycine ketimine (see paper)
46% identity, 100% coverage: 2:420/421 of query aligns to 5:425/429 of 8erbK
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y55 (= Y51), R57 (= R53), G85 (= G81), Q86 (≠ M82), Q89 (≠ T85), Y110 (= Y106), N157 (= N153), D182 (= D178), S205 (= S200), T207 (≠ S202), K208 (= K203), T385 (= T380), R405 (= R400)
2ctzA Crystal structure of o-acetyl homoserine sulfhydrylase from thermus thermophilus hb8
42% identity, 100% coverage: 1:419/421 of query aligns to 1:420/421 of 2ctzA
- active site: R54 (= R53), Y107 (= Y106), D180 (= D178), K206 (= K203)
- binding pyridoxal-5'-phosphate: S81 (= S80), G82 (= G81), H83 (≠ M82), Q86 (≠ T85), Y107 (= Y106), D180 (= D178), T182 (= T180), S203 (= S200), T205 (≠ S202), K206 (= K203)
Q5SK88 O-acetyl-L-homoserine sulfhydrylase 1; OAH-sulfhydrylase 1; EC 2.5.1.- from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
42% identity, 100% coverage: 1:419/421 of query aligns to 1:420/421 of Q5SK88
- K206 (= K203) 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)
44% identity, 99% coverage: 3:420/421 of query aligns to 8:427/429 of O13326
- G411 (= G404) mutation to D: Impairs homocysteine synthase activity.
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
39% identity, 99% coverage: 5:421/421 of query aligns to 11:395/397 of 3vk3A
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
39% identity, 99% coverage: 5:421/421 of query aligns to 12:396/398 of 1pg8A
- active site: R61 (= R53), Y114 (= Y106), D186 (= D178), K211 (= K203)
- binding pyridoxal-5'-phosphate: Y59 (= Y51), R61 (= R53), S88 (= S80), G89 (= G81), M90 (= M82), Y114 (= Y106), D186 (= D178), S208 (= S200), T210 (≠ S202), K211 (= K203)
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)
39% identity, 99% coverage: 5:421/421 of query aligns to 12:396/398 of P13254
- YSR 59:61 (≠ YTR 51:53) binding pyridoxal 5'-phosphate
- R61 (= R53) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 81:82) binding in other chain
- Y114 (= Y106) binding substrate
- C116 (≠ G108) 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 200:202) binding in other chain
- K211 (= K203) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ P253) 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 (≠ P254) 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 (= R400) binding substrate
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
39% identity, 99% coverage: 5:421/421 of query aligns to 6:390/392 of 5x2xA
- active site: R55 (= R53), Y108 (= Y106), D180 (= D178), K205 (= K203)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y51), R55 (= R53), G83 (= G81), M84 (= M82), Y108 (= Y106), N155 (= N153), D180 (= D178), S202 (= S200), T204 (≠ S202), K205 (= K203), V333 (= V364), S334 (≠ N365), R369 (= R400)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
39% identity, 99% coverage: 5:421/421 of query aligns to 6:390/392 of 5x2wA
- active site: R55 (= R53), Y108 (= Y106), D180 (= D178), K205 (= K203)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y51), R55 (= R53), S82 (= S80), G83 (= G81), M84 (= M82), Y108 (= Y106), D180 (= D178), S202 (= S200), K205 (= K203), V333 (= V364), S334 (≠ N365), R369 (= R400)
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
39% identity, 99% coverage: 5:421/421 of query aligns to 7:391/393 of 5x30C
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
37% identity, 99% coverage: 5:420/421 of query aligns to 10:393/396 of 4hf8A
- active site: R59 (= R53), Y112 (= Y106), D184 (= D178), K209 (= K203)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G81), I88 (≠ M82), Y112 (= Y106), E155 (= E149), N159 (= N153), D184 (= D178), S206 (= S200), K209 (= K203), S338 (≠ N365), R373 (= R400)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
37% identity, 99% coverage: 5:419/421 of query aligns to 10:392/396 of 4omaA
- active site: R59 (= R53), Y112 (= Y106), D184 (= D178), K209 (= K203)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G81), I88 (≠ M82), Y112 (= Y106), D184 (= D178), S206 (= S200), T208 (≠ S202), K209 (= K203), V337 (= V364), S338 (≠ N365), R373 (= R400)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
37% identity, 99% coverage: 5:419/421 of query aligns to 10:392/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
37% identity, 99% coverage: 5:419/421 of query aligns to 10:392/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
37% identity, 99% coverage: 5:419/421 of query aligns to 10:392/396 of 3jw9A
Query Sequence
>WP_011372397.1 NCBI__GCF_000012965.1:WP_011372397.1
MDLQTRALHEGYTKDSQGTMAVPIYQTTAYEFNSVEHAADLFSLKQLGNIYTRLNNPTTD
VFEKRFASLEGGEAALATSSGMSATFFAIVNATAAGENIVCAKQLYGGSLTLNTHTLKRF
GIEARYFDVHDMSSLESLIDDKTRVIFFESLTNPSIDVADIEAITKIADKYGILSVVDNT
VATPVLCRPFEFGADIVVHSASKYTTGQGLAIGGILVERKNLVEKLRSNPRYEHFNNPDP
SYHGLIYVNIGLPPFTLRARLSLSRDLGAVLSPFNSWLFIQGIETLSLRMKEHSKNALAL
AEFLESHPKVKKVNYPGLKSNANYKNAQKYFDGGECSGLLSFEVASLQEATKIVDATKLY
SLVVNIGDSKSIITHPASTTHQQLNEQELIACGVPSGLIRISCGLESIKDLIDDMKQALE
A
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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