SitesBLAST
Comparing WP_013089932.1 NCBI__GCF_000092885.1:WP_013089932.1 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)
50% identity, 95% coverage: 6:427/445 of query aligns to 7:428/428 of 7kb1C
- binding pyridoxal-5'-phosphate: Y57 (= Y55), R59 (= R57)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: G87 (= G85), Q88 (= Q86), Y112 (= Y110), N160 (= N157), D185 (= D182), S206 (= S204), T208 (= T206), K209 (= K207), N369 (= N368), I370 (≠ V369), R404 (= R403)
7kb1A Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
50% identity, 95% coverage: 6:427/445 of query aligns to 7:428/428 of 7kb1A
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y57 (= Y55), R59 (= R57), G87 (= G85), Q88 (= Q86), Y112 (= Y110), N160 (= N157), D185 (= D182), S206 (= S204), T208 (= T206), K209 (= K207), N369 (= N368), I370 (≠ V369), R404 (= R403)
8wkoA Crystal structure of o-acetylhomoserine sulfhydrylase from lactobacillus plantarum in the closed form (see paper)
50% identity, 94% coverage: 6:422/445 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 (= G85), S88 (≠ Q86), Y112 (= Y110), E155 (= E153), D184 (= D182), T186 (= T184), S206 (= S204), A207 (= A205), T208 (= T206), F209 (= F208), G212 (= G211), M217 (≠ I216), V369 (= V369), A370 (≠ G370)
- binding proline: H213 (= H212), Q284 (= Q284), S288 (≠ T288)
8erjB Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
50% identity, 95% coverage: 4:425/445 of query aligns to 3:426/428 of 8erjB
- binding (2S)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]but-3-enoic acid: G84 (= G85), Q85 (= Q86), Q88 (≠ L89), Y109 (= Y110), D181 (= D182), S204 (= S204), K207 (= K207), A368 (= A367), N369 (= N368), T384 (= T383), R404 (= R403)
8erjA Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
50% identity, 95% coverage: 4:425/445 of query aligns to 3:426/428 of 8erjA
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: S83 (= S84), G84 (= G85), Q85 (= Q86), Q88 (≠ L89), Y109 (= Y110), N156 (= N157), D181 (= D182), S204 (= S204), T206 (= T206), K207 (= K207), R404 (= R403)
8erbK Crystal structure of fub7 in complex with vinylglycine ketimine (see paper)
50% identity, 95% coverage: 4:425/445 of query aligns to 4:427/429 of 8erbK
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y55 (= Y55), R57 (= R57), G85 (= G85), Q86 (= Q86), Q89 (≠ L89), Y110 (= Y110), N157 (= N157), D182 (= D182), S205 (= S204), T207 (= T206), K208 (= K207), T385 (= T383), R405 (= R403)
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)
49% identity, 96% coverage: 1:425/445 of query aligns to 3:429/429 of O13326
- G411 (= G407) mutation to D: Impairs homocysteine synthase activity.
2ctzA Crystal structure of o-acetyl homoserine sulfhydrylase from thermus thermophilus hb8
48% identity, 94% coverage: 5:422/445 of query aligns to 2:420/421 of 2ctzA
- active site: R54 (= R57), Y107 (= Y110), D180 (= D182), K206 (= K207)
- binding pyridoxal-5'-phosphate: S81 (= S84), G82 (= G85), H83 (≠ Q86), Q86 (≠ L89), Y107 (= Y110), D180 (= D182), T182 (= T184), S203 (= S204), T205 (= T206), K206 (= K207)
Q5SK88 O-acetyl-L-homoserine sulfhydrylase 1; OAH-sulfhydrylase 1; EC 2.5.1.- from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
48% identity, 94% coverage: 5:422/445 of query aligns to 2:420/421 of Q5SK88
- K206 (= K207) modified: N6-(pyridoxal phosphate)lysine
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
39% identity, 94% coverage: 6:425/445 of query aligns to 8:395/396 of 4omaA
- active site: R59 (= R57), Y112 (= Y110), D184 (= D182), K209 (= K207)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G85), I88 (≠ Q86), Y112 (= Y110), D184 (= D182), S206 (= S204), T208 (= T206), K209 (= K207), V337 (≠ A367), S338 (≠ N368), R373 (= R403)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
39% identity, 94% coverage: 6:425/445 of query aligns to 8:395/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
39% identity, 94% coverage: 6:425/445 of query aligns to 8:395/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
39% identity, 94% coverage: 6:425/445 of query aligns to 8:395/396 of 3jw9A
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
39% identity, 94% coverage: 6:425/445 of query aligns to 8:395/396 of 6egrA
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
39% identity, 94% coverage: 6:425/445 of query aligns to 7:394/395 of 5m3zA
- active site: R58 (= R57), Y111 (= Y110), D183 (= D182), K208 (= K207)
- binding norleucine: Y111 (= Y110), H113 (≠ G112), K208 (= K207), V336 (≠ A367), S337 (≠ N368)
- binding pyridoxal-5'-phosphate: G86 (= G85), I87 (≠ Q86), Y111 (= Y110), E154 (= E153), D183 (= D182), T185 (= T184), S205 (= S204), T207 (= T206), K208 (= K207)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G85), I87 (≠ Q86), Y111 (= Y110), D183 (= D182), S205 (= S204), T207 (= T206), K208 (= K207), V336 (≠ A367), S337 (≠ N368), R372 (= R403)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
39% identity, 94% coverage: 6:425/445 of query aligns to 8:395/396 of 4hf8A
- active site: R59 (= R57), Y112 (= Y110), D184 (= D182), K209 (= K207)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G85), I88 (≠ Q86), Y112 (= Y110), E155 (= E153), N159 (= N157), D184 (= D182), S206 (= S204), K209 (= K207), S338 (≠ N368), R373 (= R403)
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
41% identity, 94% coverage: 6:425/445 of query aligns to 4:391/392 of 5x2xA
- active site: R55 (= R57), Y108 (= Y110), D180 (= D182), K205 (= K207)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y55), R55 (= R57), G83 (= G85), M84 (≠ Q86), Y108 (= Y110), N155 (= N157), D180 (= D182), S202 (= S204), T204 (= T206), K205 (= K207), V333 (≠ A367), S334 (≠ N368), R369 (= R403)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
41% identity, 94% coverage: 6:425/445 of query aligns to 4:391/392 of 5x2wA
- active site: R55 (= R57), Y108 (= Y110), D180 (= D182), K205 (= K207)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y55), R55 (= R57), S82 (= S84), G83 (= G85), M84 (≠ Q86), Y108 (= Y110), D180 (= D182), S202 (= S204), K205 (= K207), V333 (≠ A367), S334 (≠ N368), R369 (= R403)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
41% identity, 94% coverage: 6:425/445 of query aligns to 10:397/398 of 1pg8A
- active site: R61 (= R57), Y114 (= Y110), D186 (= D182), K211 (= K207)
- binding pyridoxal-5'-phosphate: Y59 (= Y55), R61 (= R57), S88 (= S84), G89 (= G85), M90 (≠ Q86), Y114 (= Y110), D186 (= D182), S208 (= S204), T210 (= T206), K211 (= K207)
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, 94% coverage: 6:425/445 of query aligns to 10:397/398 of P13254
- YSR 59:61 (= YSR 55:57) binding pyridoxal 5'-phosphate
- R61 (= R57) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (≠ GQ 85:86) binding in other chain
- Y114 (= Y110) binding substrate
- C116 (≠ G112) 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 204:206) binding in other chain
- K211 (= K207) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R268) 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 (= D269) 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 (= R403) binding substrate
Query Sequence
>WP_013089932.1 NCBI__GCF_000092885.1:WP_013089932.1
MSANRFDTLALHAGAAPDPATGARATPIYQTTSFSFRDSDHAAALFNMERAGHVYSRISN
PTVAVFEERVAALENGAGAIGTASGQAALHLAIATLMGAGSHIVASSALYGGSHNLLHYT
LRRFGIETTFVKPGDLDAWRAALRPNTRLLFGETLGNPGLEVLDIAALAQIARAHRVPLL
VDSTFTTPYLLRPFEHGADFVYHSATKFLGGHGTTIGGVLVDGGRFDFEASGLFLEFTEP
YDGFHGMVFAEESTVAPFLLRARREGLRDFGACLHPQAAWQLLQGIETLPLRMERHVANT
RRVVDFLAGHAAVESVAYPELPTHPDHALAKRLLPRGAGAVFSFNLRGDRAAGRAFIEAL
TLFSHLANVGDARSLVIHPASTTHFRMDAAALAAAGITEGTIRLSIGLEDPDDLIDDLKR
ALKAAQRTAAVAPTATNAPARPESP
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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