SitesBLAST
Comparing 351915 FitnessBrowser__Btheta:351915 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
60% identity, 99% coverage: 4:428/428 of query aligns to 5:425/425 of 8wkoA
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: G87 (= G88), S88 (≠ A89), Y112 (= Y113), E155 (= E156), D184 (= D185), T186 (= T187), S206 (= S207), A207 (= A208), T208 (= T209), F209 (= F211), G212 (= G214), M217 (≠ L219), V369 (= V372), A370 (= A373)
- binding proline: H213 (= H215), Q284 (= Q287), S288 (≠ T291)
7kb1C Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
56% identity, 100% coverage: 2:427/428 of query aligns to 1:425/428 of 7kb1C
- binding pyridoxal-5'-phosphate: Y57 (= Y58), R59 (= R60)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: G87 (= G88), Q88 (≠ A89), Y112 (= Y113), N160 (= N160), D185 (= D185), S206 (= S207), T208 (= T209), K209 (= K210), N369 (= N371), I370 (≠ V372), R404 (= R406)
7kb1A Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
56% identity, 100% coverage: 2:427/428 of query aligns to 1:425/428 of 7kb1A
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y57 (= Y58), R59 (= R60), G87 (= G88), Q88 (≠ A89), Y112 (= Y113), N160 (= N160), D185 (= D185), S206 (= S207), T208 (= T209), K209 (= K210), N369 (= N371), I370 (≠ V372), R404 (= R406)
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)
51% identity, 99% coverage: 1:425/428 of query aligns to 1:426/429 of O13326
- G411 (= G410) mutation to D: Impairs homocysteine synthase activity.
8erbK Crystal structure of fub7 in complex with vinylglycine ketimine (see paper)
49% identity, 98% coverage: 7:427/428 of query aligns to 5:426/429 of 8erbK
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y55 (= Y58), R57 (= R60), G85 (= G88), Q86 (≠ A89), Q89 (≠ I92), Y110 (= Y113), N157 (= N160), D182 (= D185), S205 (= S207), T207 (= T209), K208 (= K210), T385 (= T386), R405 (= R406)
8erjB Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
49% identity, 98% coverage: 7:427/428 of query aligns to 4:425/428 of 8erjB
- binding (2S)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]but-3-enoic acid: G84 (= G88), Q85 (≠ A89), Q88 (≠ I92), Y109 (= Y113), D181 (= D185), S204 (= S207), K207 (= K210), A368 (= A370), N369 (= N371), T384 (= T386), R404 (= R406)
8erjA Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
49% identity, 98% coverage: 7:427/428 of query aligns to 4:425/428 of 8erjA
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: S83 (= S87), G84 (= G88), Q85 (≠ A89), Q88 (≠ I92), Y109 (= Y113), N156 (= N160), D181 (= D185), S204 (= S207), T206 (= T209), K207 (= K210), R404 (= R406)
2ctzA Crystal structure of o-acetyl homoserine sulfhydrylase from thermus thermophilus hb8
48% identity, 98% coverage: 6:426/428 of query aligns to 1:421/421 of 2ctzA
- active site: R54 (= R60), Y107 (= Y113), D180 (= D185), K206 (= K210)
- binding pyridoxal-5'-phosphate: S81 (= S87), G82 (= G88), H83 (≠ A89), Q86 (≠ I92), Y107 (= Y113), D180 (= D185), T182 (= T187), S203 (= S207), T205 (= T209), K206 (= K210)
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, 98% coverage: 6:426/428 of query aligns to 1:421/421 of Q5SK88
- K206 (= K210) 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)
42% identity, 98% coverage: 8:427/428 of query aligns to 8:394/396 of 4omaA
- active site: R59 (= R60), Y112 (= Y113), D184 (= D185), K209 (= K210)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G88), I88 (≠ A89), Y112 (= Y113), D184 (= D185), S206 (= S207), T208 (= T209), K209 (= K210), V337 (≠ A370), S338 (≠ N371), R373 (= R406)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
42% identity, 98% coverage: 8:427/428 of query aligns to 8:394/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
42% identity, 98% coverage: 8:427/428 of query aligns to 8:394/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
42% identity, 98% coverage: 8:427/428 of query aligns to 8:394/396 of 3jw9A
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
42% identity, 98% coverage: 8:427/428 of query aligns to 8:394/396 of 4hf8A
- active site: R59 (= R60), Y112 (= Y113), D184 (= D185), K209 (= K210)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G88), I88 (≠ A89), Y112 (= Y113), E155 (= E156), N159 (= N160), D184 (= D185), S206 (= S207), K209 (= K210), S338 (≠ N371), R373 (= R406)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
42% identity, 98% coverage: 8:427/428 of query aligns to 8:394/396 of 6egrA
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
42% identity, 98% coverage: 8:427/428 of query aligns to 7:393/395 of 5m3zA
- active site: R58 (= R60), Y111 (= Y113), D183 (= D185), K208 (= K210)
- binding norleucine: Y111 (= Y113), H113 (≠ G115), K208 (= K210), V336 (≠ A370), S337 (≠ N371)
- binding pyridoxal-5'-phosphate: G86 (= G88), I87 (≠ A89), Y111 (= Y113), E154 (= E156), D183 (= D185), T185 (= T187), S205 (= S207), T207 (= T209), K208 (= K210)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G88), I87 (≠ A89), Y111 (= Y113), D183 (= D185), S205 (= S207), T207 (= T209), K208 (= K210), V336 (≠ A370), S337 (≠ N371), R372 (= R406)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
41% identity, 98% coverage: 8:427/428 of query aligns to 8:383/386 of 3mkjA
- active site: Y101 (= Y113), D173 (= D185), K198 (= K210)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G88), I77 (≠ A89), Y101 (= Y113), E144 (= E156), D173 (= D185), F176 (= F188), S195 (= S207), T197 (= T209), K198 (= K210)
8ovhA Crystal structure of o-acetyl-l-homoserine sulfhydrolase from saccharomyces cerevisiae in complex with pyridoxal-5'-phosphate (see paper)
43% identity, 99% coverage: 7:428/428 of query aligns to 4:394/400 of 8ovhA
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
38% identity, 98% coverage: 8:425/428 of query aligns to 10:394/398 of 1pg8A
- active site: R61 (= R60), Y114 (= Y113), D186 (= D185), K211 (= K210)
- binding pyridoxal-5'-phosphate: Y59 (= Y58), R61 (= R60), S88 (= S87), G89 (= G88), M90 (≠ A89), Y114 (= Y113), D186 (= D185), S208 (= S207), T210 (= T209), K211 (= K210)
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)
38% identity, 98% coverage: 8:425/428 of query aligns to 10:394/398 of P13254
- YSR 59:61 (≠ YGR 58:60) binding
- R61 (= R60) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (≠ GA 88:89) binding in other chain
- Y114 (= Y113) binding
- C116 (≠ G115) 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 207:209) binding in other chain
- K211 (= K210) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R271) 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 (= D272) 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 (= R406) binding
Query Sequence
>351915 FitnessBrowser__Btheta:351915
MERKNLHFETLQVHVGQEQADPATDARAVPIYQTTSYVFHNSAHAAARFGLQDPGNIYGR
LTNSTQGVFEERVAVLEGGVAGLAVASGAAAITYAFENITRAGDHIVAAKTIYGGSYNLL
AHTLPNYGVTTTFVDPSDLSNFEKAIQENTKAVFIETLGNPNSNIIDIEAVSEIAHRHKI
PLIIDNTFGTPYLIRPIEHGADIVVHSATKFIGGHGSSLGGVIVDSGKFDWVASGKFPQL
TEPDPSYHGVRFVDAAGPAAYVTRIRATLLRDTGATISPFNAFILLQGLETLSLRVERHV
ENALKVVNFLNNHPKVKKVNHPSLSDHPDHALYQRYFPNGAGSIFTFEVKGGQEEAHRFI
DSLEIFSLLANVADVKSLVIHPASTTHSQLNAQELAEQEIYPGTVRLSIGTEHINDLIAD
LEQALAKI
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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