SitesBLAST
Comparing Ac3H11_549 FitnessBrowser__acidovorax_3H11:Ac3H11_549 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)
2ctzA Crystal structure of o-acetyl homoserine sulfhydrylase from thermus thermophilus hb8
54% identity, 93% coverage: 32:455/458 of query aligns to 1:420/421 of 2ctzA
- active site: R54 (= R85), Y107 (= Y138), D180 (= D210), K206 (= K235)
- binding pyridoxal-5'-phosphate: S81 (= S112), G82 (= G113), H83 (≠ M114), Q86 (≠ I117), Y107 (= Y138), D180 (= D210), T182 (= T212), S203 (= S232), T205 (= T234), K206 (= K235)
Q5SK88 O-acetyl-L-homoserine sulfhydrylase 1; OAH-sulfhydrylase 1; EC 2.5.1.- from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
54% identity, 93% coverage: 32:455/458 of query aligns to 1:420/421 of Q5SK88
- K206 (= K235) modified: N6-(pyridoxal phosphate)lysine
7kb1C Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
55% identity, 92% coverage: 36:455/458 of query aligns to 9:423/428 of 7kb1C
- binding pyridoxal-5'-phosphate: Y57 (= Y83), R59 (= R85)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: G87 (= G113), Q88 (≠ M114), Y112 (= Y138), N160 (= N185), D185 (= D210), S206 (= S232), T208 (= T234), K209 (= K235), N369 (= N401), I370 (= I402), R404 (= R436)
7kb1A Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
55% identity, 92% coverage: 36:455/458 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 (= Y83), R59 (= R85), G87 (= G113), Q88 (≠ M114), Y112 (= Y138), N160 (= N185), D185 (= D210), S206 (= S232), T208 (= T234), K209 (= K235), N369 (= N401), I370 (= I402), R404 (= R436)
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, 92% coverage: 34:456/458 of query aligns to 8:427/429 of O13326
- G411 (= G440) mutation to D: Impairs homocysteine synthase activity.
8erbK Crystal structure of fub7 in complex with vinylglycine ketimine (see paper)
54% identity, 93% coverage: 31:455/458 of query aligns to 3:424/429 of 8erbK
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y55 (= Y83), R57 (= R85), G85 (= G113), Q86 (≠ M114), Q89 (≠ I117), Y110 (= Y138), N157 (= N185), D182 (= D210), S205 (= S232), T207 (= T234), K208 (= K235), T385 (= T416), R405 (= R436)
8erjB Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
54% identity, 93% coverage: 31:455/458 of query aligns to 2:423/428 of 8erjB
- binding (2S)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]but-3-enoic acid: G84 (= G113), Q85 (≠ M114), Q88 (≠ I117), Y109 (= Y138), D181 (= D210), S204 (= S232), K207 (= K235), A368 (≠ V400), N369 (= N401), T384 (= T416), R404 (= R436)
8erjA Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
54% identity, 93% coverage: 31:455/458 of query aligns to 2:423/428 of 8erjA
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: S83 (= S112), G84 (= G113), Q85 (≠ M114), Q88 (≠ I117), Y109 (= Y138), N156 (= N185), D181 (= D210), S204 (= S232), T206 (= T234), K207 (= K235), R404 (= R436)
8wkoA Crystal structure of o-acetylhomoserine sulfhydrylase from lactobacillus plantarum in the closed form
52% identity, 93% coverage: 34:458/458 of query aligns to 9:425/425 of 8wkoA
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: G87 (= G113), S88 (≠ M114), Y112 (= Y138), E155 (= E181), D184 (= D210), T186 (= T212), S206 (= S232), A207 (≠ L233), T208 (= T234), F209 (≠ Y236), G212 (= G239), M217 (≠ V244), V369 (≠ I402), A370 (≠ G403)
- binding proline: H213 (= H240), Q284 (= Q313), S288 (≠ T317)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
42% identity, 92% coverage: 36:455/458 of query aligns to 10:392/396 of 4hf8A
- active site: R59 (= R85), Y112 (= Y138), D184 (= D210), K209 (= K235)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G113), I88 (≠ M114), Y112 (= Y138), E155 (= E181), N159 (= N185), D184 (= D210), S206 (= S232), K209 (= K235), S338 (≠ N401), R373 (= R436)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
42% identity, 92% coverage: 36:455/458 of query aligns to 10:392/396 of 4omaA
- active site: R59 (= R85), Y112 (= Y138), D184 (= D210), K209 (= K235)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G113), I88 (≠ M114), Y112 (= Y138), D184 (= D210), S206 (= S232), T208 (= T234), K209 (= K235), V337 (= V400), S338 (≠ N401), R373 (= R436)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
42% identity, 92% coverage: 36:455/458 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)
42% identity, 92% coverage: 36:455/458 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)
42% identity, 92% coverage: 36:455/458 of query aligns to 10:392/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
42% identity, 92% coverage: 36:455/458 of query aligns to 9:391/395 of 5m3zA
- active site: R58 (= R85), Y111 (= Y138), D183 (= D210), K208 (= K235)
- binding norleucine: Y111 (= Y138), H113 (≠ G140), K208 (= K235), V336 (= V400), S337 (≠ N401)
- binding pyridoxal-5'-phosphate: G86 (= G113), I87 (≠ M114), Y111 (= Y138), E154 (= E181), D183 (= D210), T185 (= T212), S205 (= S232), T207 (= T234), K208 (= K235)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G113), I87 (≠ M114), Y111 (= Y138), D183 (= D210), S205 (= S232), T207 (= T234), K208 (= K235), V336 (= V400), S337 (≠ N401), R372 (= R436)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
42% identity, 92% coverage: 36:455/458 of query aligns to 10:392/396 of 6egrA
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
43% identity, 92% coverage: 36:457/458 of query aligns to 12:396/398 of 1pg8A
- active site: R61 (= R85), Y114 (= Y138), D186 (= D210), K211 (= K235)
- binding pyridoxal-5'-phosphate: Y59 (= Y83), R61 (= R85), S88 (= S112), G89 (= G113), M90 (= M114), Y114 (= Y138), D186 (= D210), S208 (= S232), T210 (= T234), K211 (= K235)
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)
43% identity, 92% coverage: 36:457/458 of query aligns to 12:396/398 of P13254
- YSR 59:61 (≠ YTR 83:85) binding
- R61 (= R85) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 113:114) binding in other chain
- Y114 (= Y138) binding
- C116 (≠ G140) 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 (≠ SLT 232:234) binding in other chain
- K211 (= K235) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R297) 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 (≠ N298) 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 (= R436) binding
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
43% identity, 92% coverage: 36:457/458 of query aligns to 11:395/397 of 3vk3A
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
43% identity, 92% coverage: 36:457/458 of query aligns to 6:390/392 of 5x2xA
- active site: R55 (= R85), Y108 (= Y138), D180 (= D210), K205 (= K235)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y83), R55 (= R85), G83 (= G113), M84 (= M114), Y108 (= Y138), N155 (= N185), D180 (= D210), S202 (= S232), T204 (= T234), K205 (= K235), V333 (= V400), S334 (≠ N401), R369 (= R436)
Query Sequence
>Ac3H11_549 FitnessBrowser__acidovorax_3H11:Ac3H11_549
MARAIGTSRNAQPWVEADCPTPFPSTKETSFMKIETLAVHAGYSPDPTTKAVAVPIYQTV
AYAFDSAQHGADLFDLKVPGNIYTRIMNPTTDVLEKRVAALEGGIAALAVASGMAAITYA
IQTIAEAGDNIVSASTLYGGTYNLFAHTLPQQGITTRFADPRDPASFAQHIDARTKAIFI
ESIGNPLGNVTDIAAIAKVAHDHGVPLIVDNTVPSPYLLRPIEHGADIVVHSLTKYLGGH
GNSVGGAIVDSGKFPWAEHKARFPRLNEPDVSYHGVVYTEALGPAAFIGRARVVPLRNTG
AALSPQSAFLILQGIETLALRMDRICDNTLALAKYLQSHPKVEWVRYAGLPDHPDHALVQ
RQSGGKASGILSFGLKSTDADPRAAGARFLDALQLFTRLVNIGDAKSLATHPASTTHRQL
NPEELAKAGVSESMVRLSVGIEHIDDLRADLVQALDAV
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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