SitesBLAST
Comparing WP_013841856.1 NCBI__GCF_000215085.1:WP_013841856.1 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)
63% identity, 99% coverage: 4:425/427 of query aligns to 3:424/428 of 7kb1C
- binding pyridoxal-5'-phosphate: Y57 (= Y57), R59 (= R59)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: G87 (= G87), Q88 (≠ H88), Y112 (= Y112), N160 (= N159), D185 (= D184), S206 (= S206), T208 (= T208), K209 (= K209), N369 (= N370), I370 (≠ V371), R404 (= R405)
7kb1A Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
63% identity, 99% coverage: 4:425/427 of query aligns to 3:424/428 of 7kb1A
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y57 (= Y57), R59 (= R59), G87 (= G87), Q88 (≠ H88), Y112 (= Y112), N160 (= N159), D185 (= D184), S206 (= S206), T208 (= T208), K209 (= K209), N369 (= N370), I370 (≠ V371), R404 (= R405)
8wkoA Crystal structure of o-acetylhomoserine sulfhydrylase from lactobacillus plantarum in the closed form (see paper)
57% identity, 98% coverage: 8:424/427 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 (= G87), S88 (≠ H88), Y112 (= Y112), E155 (= E155), D184 (= D184), T186 (= T186), S206 (= S206), A207 (≠ T207), T208 (= T208), F209 (= F210), G212 (= G213), M217 (≠ I218), V369 (= V371), A370 (≠ G372)
- binding proline: H213 (= H214), Q284 (= Q286), S288 (≠ T290)
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)
56% identity, 98% coverage: 8:425/427 of query aligns to 8:427/429 of O13326
- G411 (= G409) mutation to D: Impairs homocysteine synthase activity.
2ctzA Crystal structure of o-acetyl homoserine sulfhydrylase from thermus thermophilus hb8
55% identity, 98% coverage: 8:424/427 of query aligns to 3:420/421 of 2ctzA
- active site: R54 (= R59), Y107 (= Y112), D180 (= D184), K206 (= K209)
- binding pyridoxal-5'-phosphate: S81 (= S86), G82 (= G87), H83 (= H88), Q86 (≠ I91), Y107 (= Y112), D180 (= D184), T182 (= T186), S203 (= S206), T205 (= T208), K206 (= K209)
Q5SK88 O-acetyl-L-homoserine sulfhydrylase 1; OAH-sulfhydrylase 1; EC 2.5.1.- from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
55% identity, 98% coverage: 8:424/427 of query aligns to 3:420/421 of Q5SK88
- K206 (= K209) modified: N6-(pyridoxal phosphate)lysine
8erbK Crystal structure of fub7 in complex with vinylglycine ketimine (see paper)
52% identity, 98% coverage: 8:425/427 of query aligns to 6:425/429 of 8erbK
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y55 (= Y57), R57 (= R59), G85 (= G87), Q86 (≠ H88), Q89 (≠ I91), Y110 (= Y112), N157 (= N159), D182 (= D184), S205 (= S206), T207 (= T208), K208 (= K209), T385 (= T385), R405 (= R405)
8erjB Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
52% identity, 98% coverage: 8:425/427 of query aligns to 5:424/428 of 8erjB
- binding (2S)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]but-3-enoic acid: G84 (= G87), Q85 (≠ H88), Q88 (≠ I91), Y109 (= Y112), D181 (= D184), S204 (= S206), K207 (= K209), A368 (= A369), N369 (= N370), T384 (= T385), R404 (= R405)
8erjA Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
52% identity, 98% coverage: 8:425/427 of query aligns to 5:424/428 of 8erjA
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: S83 (= S86), G84 (= G87), Q85 (≠ H88), Q88 (≠ I91), Y109 (= Y112), N156 (= N159), D181 (= D184), S204 (= S206), T206 (= T208), K207 (= K209), R404 (= R405)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
44% identity, 99% coverage: 4:425/427 of query aligns to 4:393/396 of 4omaA
- active site: R59 (= R59), Y112 (= Y112), D184 (= D184), K209 (= K209)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G87), I88 (≠ H88), Y112 (= Y112), D184 (= D184), S206 (= S206), T208 (= T208), K209 (= K209), V337 (≠ A369), S338 (≠ N370), R373 (= R405)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
44% identity, 99% coverage: 4:425/427 of query aligns to 4:393/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
44% identity, 99% coverage: 4:425/427 of query aligns to 4:393/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
44% identity, 99% coverage: 4:425/427 of query aligns to 4:393/396 of 3jw9A
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
44% identity, 99% coverage: 4:425/427 of query aligns to 4:393/396 of 4hf8A
- active site: R59 (= R59), Y112 (= Y112), D184 (= D184), K209 (= K209)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G87), I88 (≠ H88), Y112 (= Y112), E155 (= E155), N159 (= N159), D184 (= D184), S206 (= S206), K209 (= K209), S338 (≠ N370), R373 (= R405)
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
44% identity, 99% coverage: 4:425/427 of query aligns to 3:392/395 of 5m3zA
- active site: R58 (= R59), Y111 (= Y112), D183 (= D184), K208 (= K209)
- binding norleucine: Y111 (= Y112), H113 (≠ G114), K208 (= K209), V336 (≠ A369), S337 (≠ N370)
- binding pyridoxal-5'-phosphate: G86 (= G87), I87 (≠ H88), Y111 (= Y112), E154 (= E155), D183 (= D184), T185 (= T186), S205 (= S206), T207 (= T208), K208 (= K209)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G87), I87 (≠ H88), Y111 (= Y112), D183 (= D184), S205 (= S206), T207 (= T208), K208 (= K209), V336 (≠ A369), S337 (≠ N370), R372 (= R405)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
44% identity, 99% coverage: 4:425/427 of query aligns to 4:393/396 of 6egrA
8ovhA Crystal structure of o-acetyl-l-homoserine sulfhydrolase from saccharomyces cerevisiae in complex with pyridoxal-5'-phosphate (see paper)
48% identity, 98% coverage: 8:425/427 of query aligns to 5:392/400 of 8ovhA
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
42% identity, 99% coverage: 4:425/427 of query aligns to 4:382/386 of 3mkjA
- active site: Y101 (= Y112), D173 (= D184), K198 (= K209)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G87), I77 (≠ H88), Y101 (= Y112), E144 (= E155), D173 (= D184), F176 (= F187), S195 (= S206), T197 (= T208), K198 (= K209)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
39% identity, 98% coverage: 7:426/427 of query aligns to 9:396/398 of 1pg8A
- active site: R61 (= R59), Y114 (= Y112), D186 (= D184), K211 (= K209)
- binding pyridoxal-5'-phosphate: Y59 (= Y57), R61 (= R59), S88 (= S86), G89 (= G87), M90 (≠ H88), Y114 (= Y112), D186 (= D184), S208 (= S206), T210 (= T208), K211 (= K209)
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, 98% coverage: 7:426/427 of query aligns to 9:396/398 of P13254
- YSR 59:61 (≠ YTR 57:59) binding pyridoxal 5'-phosphate
- R61 (= R59) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (≠ GH 87:88) binding in other chain
- Y114 (= Y112) binding substrate
- C116 (≠ G114) 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 (≠ STT 206:208) binding in other chain
- K211 (= K209) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R270) 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 (= D271) 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 (= R405) binding substrate
Query Sequence
>WP_013841856.1 NCBI__GCF_000215085.1:WP_013841856.1
MTERKLGFETLALHAGHQPDRETLSRAVPIYQTSSYVFRDSEHAANLFSLKEEGHIYTRI
DNPTTDVLEKRLAALEGGVGALAMASGHAAIVAAILNIASAGDEIVSSTNLYGGTVNLFT
HTFARLGIKVVFVNPEDPENFRKAITEKTKALFAETIGNPRCDVLDLEAVGKIAHQAEIP
LIVDSTFTTPYLCRPFDYGADIVVHSTTKFIGGHGTSIGGVIIDSGKFDWSQNDKFPGLN
QPDPSYHDITYTKEMGAAAYIAKARTQLLRDLGACVSPFNAFLLLQGIETLALRMERHVS
NAQRVAEFLQQHSLVNWVSYPGIKGHPSYELAQKYLPKGAGAILTFGIKGGLEAGRRFID
SLQIFSHLANVGDAKSLVIHPASTTHSQLSEEALKQAGVSPDLIRISVGLESIGDLLEDL
DQALKAQ
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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