SitesBLAST
Comparing Ac3H11_34 FitnessBrowser__acidovorax_3H11:Ac3H11_34 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)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
67% identity, 89% coverage: 12:398/434 of query aligns to 9:394/398 of 1pg8A
- active site: R61 (= R64), Y114 (= Y117), D186 (= D189), K211 (= K214)
- binding pyridoxal-5'-phosphate: Y59 (= Y62), R61 (= R64), S88 (= S91), G89 (= G92), M90 (= M93), Y114 (= Y117), D186 (= D189), S208 (= S211), T210 (= T213), K211 (= K214)
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)
67% identity, 89% coverage: 12:398/434 of query aligns to 9:394/398 of P13254
- YSR 59:61 (≠ YTR 62:64) binding
- R61 (= R64) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 92:93) binding in other chain
- Y114 (= Y117) binding
- C116 (= C119) 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 (≠ SMT 211:213) binding in other chain
- K211 (= K214) modified: N6-(pyridoxal phosphate)lysine
- K240 (= K244) 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 (= D245) 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 (= R379) binding
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
67% identity, 89% coverage: 12:398/434 of query aligns to 3:388/392 of 5x2xA
- active site: R55 (= R64), Y108 (= Y117), D180 (= D189), K205 (= K214)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y62), R55 (= R64), G83 (= G92), M84 (= M93), Y108 (= Y117), N155 (= N164), D180 (= D189), S202 (= S211), T204 (= T213), K205 (= K214), V333 (= V343), S334 (= S344), R369 (= R379)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
67% identity, 89% coverage: 12:398/434 of query aligns to 3:388/392 of 5x2wA
- active site: R55 (= R64), Y108 (= Y117), D180 (= D189), K205 (= K214)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y62), R55 (= R64), S82 (= S91), G83 (= G92), M84 (= M93), Y108 (= Y117), D180 (= D189), S202 (= S211), K205 (= K214), V333 (= V343), S334 (= S344), R369 (= R379)
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
67% identity, 89% coverage: 12:398/434 of query aligns to 4:389/393 of 5x30C
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
67% identity, 89% coverage: 12:398/434 of query aligns to 8:393/397 of 3vk3A
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
53% identity, 90% coverage: 12:400/434 of query aligns to 7:396/399 of 5dx5A
- active site: R59 (= R64), Y112 (= Y117), D186 (= D189), K211 (= K214)
- binding pyridoxal-5'-phosphate: Y57 (= Y62), R59 (= R64), S86 (= S91), G87 (= G92), M88 (= M93), Y112 (= Y117), D186 (= D189), F189 (≠ Y192), S208 (= S211), T210 (= T213), K211 (= K214)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
49% identity, 89% coverage: 12:398/434 of query aligns to 7:392/396 of 6egrA
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
49% identity, 89% coverage: 12:398/434 of query aligns to 7:392/396 of 4hf8A
- active site: R59 (= R64), Y112 (= Y117), D184 (= D189), K209 (= K214)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G92), I88 (≠ M93), Y112 (= Y117), E155 (= E160), N159 (= N164), D184 (= D189), S206 (= S211), K209 (= K214), S338 (= S344), R373 (= R379)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
49% identity, 89% coverage: 12:398/434 of query aligns to 7:392/396 of 4omaA
- active site: R59 (= R64), Y112 (= Y117), D184 (= D189), K209 (= K214)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G92), I88 (≠ M93), Y112 (= Y117), D184 (= D189), S206 (= S211), T208 (= T213), K209 (= K214), V337 (= V343), S338 (= S344), R373 (= R379)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
49% identity, 89% coverage: 12:398/434 of query aligns to 7:392/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
49% identity, 89% coverage: 12:398/434 of query aligns to 7:392/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
49% identity, 89% coverage: 12:398/434 of query aligns to 7:392/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
49% identity, 89% coverage: 12:398/434 of query aligns to 6:391/395 of 5m3zA
- active site: R58 (= R64), Y111 (= Y117), D183 (= D189), K208 (= K214)
- binding norleucine: Y111 (= Y117), H113 (≠ C119), K208 (= K214), V336 (= V343), S337 (= S344)
- binding pyridoxal-5'-phosphate: G86 (= G92), I87 (≠ M93), Y111 (= Y117), E154 (= E160), D183 (= D189), T185 (= T191), S205 (= S211), T207 (= T213), K208 (= K214)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G92), I87 (≠ M93), Y111 (= Y117), D183 (= D189), S205 (= S211), T207 (= T213), K208 (= K214), V336 (= V343), S337 (= S344), R372 (= R379)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
46% identity, 87% coverage: 23:399/434 of query aligns to 13:390/393 of 1e5fA
- active site: R55 (= R64), Y108 (= Y117), D181 (= D189), K206 (= K214)
- binding pyridoxal-5'-phosphate: Y53 (= Y62), R55 (= R64), G83 (= G92), M84 (= M93), Y108 (= Y117), D181 (= D189), S203 (= S211), K206 (= K214)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
46% identity, 87% coverage: 23:399/434 of query aligns to 13:390/394 of 1e5eA
- active site: R55 (= R64), Y108 (= Y117), D181 (= D189), K206 (= K214)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y62), R55 (= R64), G83 (= G92), M84 (= M93), Y108 (= Y117), N155 (= N164), D181 (= D189), S203 (= S211), T205 (= T213), K206 (= K214), S335 (= S344), T350 (= T359), R370 (= R379)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
47% identity, 89% coverage: 12:398/434 of query aligns to 7:381/386 of 3mkjA
- active site: Y101 (= Y117), D173 (= D189), K198 (= K214)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G92), I77 (≠ M93), Y101 (= Y117), E144 (= E160), D173 (= D189), F176 (≠ Y192), S195 (= S211), T197 (= T213), K198 (= K214)
7kb1C Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
40% identity, 89% coverage: 12:398/434 of query aligns to 6:423/428 of 7kb1C
- binding pyridoxal-5'-phosphate: Y57 (= Y62), R59 (= R64)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: G87 (= G92), Q88 (≠ M93), Y112 (= Y117), N160 (= N164), D185 (= D189), S206 (= S211), T208 (= T213), K209 (= K214), N369 (≠ S344), I370 (≠ L345), R404 (= R379)
7kb1A Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
40% identity, 89% coverage: 12:398/434 of query aligns to 6:423/428 of 7kb1A
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y57 (= Y62), R59 (= R64), G87 (= G92), Q88 (≠ M93), Y112 (= Y117), N160 (= N164), D185 (= D189), S206 (= S211), T208 (= T213), K209 (= K214), N369 (≠ S344), I370 (≠ L345), R404 (= R379)
3aeoA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 containing methionine alpha, beta-enamine-pyridoxamine- 5'-phosphate
41% identity, 85% coverage: 34:400/434 of query aligns to 23:386/387 of 3aeoA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y51 (= Y62), R53 (= R64), G81 (= G92), M82 (= M93), Y106 (= Y117), E149 (= E160), N153 (= N164), D178 (= D189), S200 (= S211), S202 (≠ T213), K203 (= K214), V329 (= V343), S330 (= S344), T345 (= T359), R365 (= R379)
Query Sequence
>Ac3H11_34 FitnessBrowser__acidovorax_3H11:Ac3H11_34
MTRTTDRSPATGFSTRAIHHGYNPADHQGALVPPIHTSATYAFPDVAYGARCFAGQEPGY
FYTRIANPTLALLEGRLAALEEGAGAVVFGSGMGAITATLWSMLEPGDEILADLTLYGCT
FSFLHHGLGRFGVTVRHVDMTDPARVAEALTAKTRVLYLETPANPNMRLVDIAAVSALAH
AQGAKVVVDNTYCTPYLQQPLLLGADVSVHSMTKYLGGHGDLTAGAAVFADAELAQRVRL
YGLKDMTGAVMSAQDAHLVMRGLKTLALRMDRHCQSAQKVAEFIAAHPAAAAVHYPGLPS
FAQHALAKQQMRQMGGMIAFELRGGLQAGVRFMDALQLVTRAVSLGDAETLAQHPASMTH
STYTPEQRAAHGIAEGLVRLSVGLEDLDDLLADIGQALDLAHAMDLSAGISAGIHAGLSP
ERVAAAEPSCSAPA
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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