SitesBLAST
Comparing WP_006745821.1 NCBI__GCF_000227685.2:WP_006745821.1 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)
P9WGB5 O-succinylhomoserine sulfhydrylase; OSH sulfhydrylase; OSHS sulfhydrylase; EC 2.5.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
45% identity, 98% coverage: 6:393/397 of query aligns to 14:405/406 of P9WGB5
- K219 (= K211) modified: N6-(pyridoxal phosphate)lysine
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
43% identity, 92% coverage: 32:397/397 of query aligns to 30:398/399 of 5dx5A
- active site: R59 (= R61), Y112 (≠ F114), D186 (= D186), K211 (= K211)
- binding pyridoxal-5'-phosphate: Y57 (= Y59), R59 (= R61), S86 (= S88), G87 (= G89), M88 (= M90), Y112 (≠ F114), D186 (= D186), F189 (= F189), S208 (= S208), T210 (= T210), K211 (= K211)
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
41% identity, 98% coverage: 5:395/397 of query aligns to 1:393/395 of 5m3zA
- active site: R58 (= R61), Y111 (≠ F114), D183 (= D186), K208 (= K211)
- binding norleucine: Y111 (≠ F114), H113 (≠ T116), K208 (= K211), V336 (≠ A338), S337 (≠ N339)
- binding pyridoxal-5'-phosphate: G86 (= G89), I87 (≠ M90), Y111 (≠ F114), E154 (= E157), D183 (= D186), T185 (≠ C188), S205 (= S208), T207 (= T210), K208 (= K211)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G89), I87 (≠ M90), Y111 (≠ F114), D183 (= D186), S205 (= S208), T207 (= T210), K208 (= K211), V336 (≠ A338), S337 (≠ N339), R372 (= R374)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
41% identity, 98% coverage: 5:395/397 of query aligns to 2:394/396 of 4omaA
- active site: R59 (= R61), Y112 (≠ F114), D184 (= D186), K209 (= K211)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G89), I88 (≠ M90), Y112 (≠ F114), D184 (= D186), S206 (= S208), T208 (= T210), K209 (= K211), V337 (≠ A338), S338 (≠ N339), R373 (= R374)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
41% identity, 98% coverage: 5:395/397 of query aligns to 2:394/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
41% identity, 98% coverage: 5:395/397 of query aligns to 2:394/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
41% identity, 98% coverage: 5:395/397 of query aligns to 2:394/396 of 3jw9A
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
41% identity, 98% coverage: 5:395/397 of query aligns to 2:394/396 of 6egrA
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
41% identity, 98% coverage: 5:395/397 of query aligns to 2:394/396 of 4hf8A
- active site: R59 (= R61), Y112 (≠ F114), D184 (= D186), K209 (= K211)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G89), I88 (≠ M90), Y112 (≠ F114), E155 (= E157), N159 (= N161), D184 (= D186), S206 (= S208), K209 (= K211), S338 (≠ N339), R373 (= R374)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
40% identity, 98% coverage: 5:395/397 of query aligns to 2:383/386 of 3mkjA
- active site: Y101 (≠ F114), D173 (= D186), K198 (= K211)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G89), I77 (≠ M90), Y101 (≠ F114), E144 (= E157), D173 (= D186), F176 (= F189), S195 (= S208), T197 (= T210), K198 (= K211)
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
42% identity, 95% coverage: 15:393/397 of query aligns to 5:388/392 of 5x2xA
- active site: R55 (= R61), Y108 (≠ F114), D180 (= D186), K205 (= K211)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y59), R55 (= R61), G83 (= G89), M84 (= M90), Y108 (≠ F114), N155 (= N161), D180 (= D186), S202 (= S208), T204 (= T210), K205 (= K211), V333 (≠ A338), S334 (≠ N339), R369 (= R374)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
42% identity, 95% coverage: 15:393/397 of query aligns to 5:388/392 of 5x2wA
- active site: R55 (= R61), Y108 (≠ F114), D180 (= D186), K205 (= K211)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y59), R55 (= R61), S82 (= S88), G83 (= G89), M84 (= M90), Y108 (≠ F114), D180 (= D186), S202 (= S208), K205 (= K211), V333 (≠ A338), S334 (≠ N339), R369 (= R374)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
42% identity, 96% coverage: 13:393/397 of query aligns to 12:394/398 of 1pg8A
- active site: R61 (= R61), Y114 (≠ F114), D186 (= D186), K211 (= K211)
- binding pyridoxal-5'-phosphate: Y59 (= Y59), R61 (= R61), S88 (= S88), G89 (= G89), M90 (= M90), Y114 (≠ F114), D186 (= D186), S208 (= S208), T210 (= T210), K211 (= K211)
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)
42% identity, 96% coverage: 13:393/397 of query aligns to 12:394/398 of P13254
- YSR 59:61 (= YSR 59:61) binding pyridoxal 5'-phosphate
- R61 (= R61) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 89:90) binding in other chain
- Y114 (≠ F114) binding substrate
- C116 (≠ T116) 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 208:210) binding in other chain
- K211 (= K211) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ L239) 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 (≠ R240) 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 (= R374) binding substrate
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
42% identity, 96% coverage: 13:393/397 of query aligns to 11:393/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
42% identity, 96% coverage: 13:393/397 of query aligns to 7:389/393 of 5x30C
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
35% identity, 97% coverage: 11:397/397 of query aligns to 5:393/393 of 1e5fA
- active site: R55 (= R61), Y108 (≠ F114), D181 (= D186), K206 (= K211)
- binding pyridoxal-5'-phosphate: Y53 (= Y59), R55 (= R61), G83 (= G89), M84 (= M90), Y108 (≠ F114), D181 (= D186), S203 (= S208), K206 (= K211)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
35% identity, 97% coverage: 11:397/397 of query aligns to 5:393/394 of 1e5eA
- active site: R55 (= R61), Y108 (≠ F114), D181 (= D186), K206 (= K211)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y59), R55 (= R61), G83 (= G89), M84 (= M90), Y108 (≠ F114), N155 (= N161), D181 (= D186), S203 (= S208), T205 (= T210), K206 (= K211), S335 (≠ N339), T350 (= T354), R370 (= R374)
4iyoD Crystal structure of cystathionine gamma lyase from xanthomonas oryzae pv. Oryzae (xometc) in complex with e-site serine, a-site serine, a- site external aldimine structure with aminoacrylate and a-site iminopropionate intermediates (see paper)
47% identity, 86% coverage: 52:393/397 of query aligns to 38:380/384 of 4iyoD
- active site: R47 (= R61), Y99 (≠ F114), D172 (= D186), K197 (= K211)
- binding serine: Y45 (= Y59), T48 (≠ F62), Y99 (≠ F114), Y99 (≠ F114), R104 (≠ V119), K197 (= K211), N227 (≠ R240), E325 (≠ A338), S326 (≠ N339), T341 (= T354), R361 (= R374)
4iyoB Crystal structure of cystathionine gamma lyase from xanthomonas oryzae pv. Oryzae (xometc) in complex with e-site serine, a-site serine, a- site external aldimine structure with aminoacrylate and a-site iminopropionate intermediates (see paper)
47% identity, 86% coverage: 52:393/397 of query aligns to 38:380/381 of 4iyoB
- active site: R47 (= R61), Y99 (≠ F114), D172 (= D186), K197 (= K211)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y59), R47 (= R61)
- binding amino-acrylate: Y99 (≠ F114), K197 (= K211), S326 (≠ N339), T341 (= T354), R361 (= R374)
- binding pyruvic acid: Q221 (≠ D234), F224 (≠ G237)
- binding serine: Y45 (= Y59), T48 (≠ F62), Y99 (≠ F114), R104 (≠ V119), N227 (≠ R240), E325 (≠ A338)
Query Sequence
>WP_006745821.1 NCBI__GCF_000227685.2:WP_006745821.1
MQEFDPTEYAPETVAVRAGYRRTAEGEHSEAIFPTSSFVFGSAAEAAARFSGEQPGNIYS
RFTNPTVRTFEQRLAAMEGGEACVATASGMAAILASFMGLLRGGDHVVCSRSVFGTTTVL
LNQYLARFGVEVTYVPLSDLDAWSSATRANTRLYFCETPSNPLGELVDIRALAAIARSRG
VLLAVDNCFCTPALQRPLSLGADLVIHSATKFLDGQGRCMGGAVVGDSERVGKDVYGFLR
SAGPTLAPFNAWVFLKGLETLHLRMRAHSDNALALARWLSAHPAVTAAHYPGLEDHPQHA
LARAQQQGFGGVLSFEVAGGRAAAWSVIDATRMLSITANLGDAKSTITHPATTTHGRLEP
AQREAQGITEGLVRVAVGLEAVADVQADLARGLDRLV
Or try a new SitesBLAST search
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