SitesBLAST
Comparing WP_020173493.1 NCBI__GCF_000385335.1:WP_020173493.1 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)
54% identity, 96% coverage: 6:398/408 of query aligns to 10:406/406 of P9WGB5
- K219 (= K215) 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)
43% identity, 93% coverage: 17:397/408 of query aligns to 10:392/396 of 4omaA
- active site: R59 (= R65), Y112 (≠ F118), D184 (= D190), K209 (= K215)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G93), I88 (≠ M94), Y112 (≠ F118), D184 (= D190), S206 (= S212), T208 (= T214), K209 (= K215), V337 (≠ N342), S338 (≠ N343), R373 (= R378)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
43% identity, 93% coverage: 17:397/408 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)
43% identity, 93% coverage: 17:397/408 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)
43% identity, 93% coverage: 17:397/408 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)
43% identity, 93% coverage: 17:397/408 of query aligns to 9:391/395 of 5m3zA
- active site: R58 (= R65), Y111 (≠ F118), D183 (= D190), K208 (= K215)
- binding norleucine: Y111 (≠ F118), H113 (≠ S120), K208 (= K215), V336 (≠ N342), S337 (≠ N343)
- binding pyridoxal-5'-phosphate: G86 (= G93), I87 (≠ M94), Y111 (≠ F118), E154 (= E161), D183 (= D190), T185 (≠ V192), S205 (= S212), T207 (= T214), K208 (= K215)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G93), I87 (≠ M94), Y111 (≠ F118), D183 (= D190), S205 (= S212), T207 (= T214), K208 (= K215), V336 (≠ N342), S337 (≠ N343), R372 (= R378)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
43% identity, 93% coverage: 17:397/408 of query aligns to 10:392/396 of 6egrA
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
43% identity, 93% coverage: 17:397/408 of query aligns to 10:392/396 of 4hf8A
- active site: R59 (= R65), Y112 (≠ F118), D184 (= D190), K209 (= K215)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G93), I88 (≠ M94), Y112 (≠ F118), E155 (= E161), N159 (= N165), D184 (= D190), S206 (= S212), K209 (= K215), S338 (≠ N343), R373 (= R378)
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
40% identity, 96% coverage: 11:402/408 of query aligns to 4:399/399 of 5dx5A
- active site: R59 (= R65), Y112 (≠ F118), D186 (= D190), K211 (= K215)
- binding pyridoxal-5'-phosphate: Y57 (= Y63), R59 (= R65), S86 (= S92), G87 (= G93), M88 (= M94), Y112 (≠ F118), D186 (= D190), F189 (= F193), S208 (= S212), T210 (= T214), K211 (= K215)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
43% identity, 93% coverage: 17:397/408 of query aligns to 10:381/386 of 3mkjA
- active site: Y101 (≠ F118), D173 (= D190), K198 (= K215)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G93), I77 (≠ M94), Y101 (≠ F118), E144 (= E161), D173 (= D190), F176 (= F193), S195 (= S212), T197 (= T214), K198 (= K215)
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
43% identity, 93% coverage: 21:401/408 of query aligns to 19:393/393 of 5x30C
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
43% identity, 93% coverage: 21:401/408 of query aligns to 18:392/392 of 5x2xA
- active site: R55 (= R65), Y108 (≠ F118), D180 (= D190), K205 (= K215)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y63), R55 (= R65), G83 (= G93), M84 (= M94), Y108 (≠ F118), N155 (= N165), D180 (= D190), S202 (= S212), T204 (= T214), K205 (= K215), V333 (≠ N342), S334 (≠ N343), R369 (= R378)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
43% identity, 93% coverage: 21:401/408 of query aligns to 18:392/392 of 5x2wA
- active site: R55 (= R65), Y108 (≠ F118), D180 (= D190), K205 (= K215)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y63), R55 (= R65), S82 (= S92), G83 (= G93), M84 (= M94), Y108 (≠ F118), D180 (= D190), S202 (= S212), K205 (= K215), V333 (≠ N342), S334 (≠ N343), R369 (= R378)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
43% identity, 93% coverage: 21:401/408 of query aligns to 23:397/397 of 3vk3A
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
43% identity, 93% coverage: 21:401/408 of query aligns to 24:398/398 of 1pg8A
- active site: R61 (= R65), Y114 (≠ F118), D186 (= D190), K211 (= K215)
- binding pyridoxal-5'-phosphate: Y59 (= Y63), R61 (= R65), S88 (= S92), G89 (= G93), M90 (= M94), Y114 (≠ F118), D186 (= D190), S208 (= S212), T210 (= T214), K211 (= K215)
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, 93% coverage: 21:401/408 of query aligns to 24:398/398 of P13254
- YSR 59:61 (= YSR 63:65) binding pyridoxal 5'-phosphate
- R61 (= R65) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 93:94) binding in other chain
- Y114 (≠ F118) binding substrate
- C116 (≠ S120) 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 212:214) binding in other chain
- K211 (= K215) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ L243) 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 (≠ R244) 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 (= R378) binding substrate
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
34% identity, 96% coverage: 13:402/408 of query aligns to 3:394/394 of 1e5eA
- active site: R55 (= R65), Y108 (≠ F118), D181 (= D190), K206 (= K215)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y63), R55 (= R65), G83 (= G93), M84 (= M94), Y108 (≠ F118), N155 (= N165), D181 (= D190), S203 (= S212), T205 (= T214), K206 (= K215), S335 (≠ N343), T350 (= T358), R370 (= R378)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
34% identity, 95% coverage: 13:400/408 of query aligns to 3:392/393 of 1e5fA
- active site: R55 (= R65), Y108 (≠ F118), D181 (= D190), K206 (= K215)
- binding pyridoxal-5'-phosphate: Y53 (= Y63), R55 (= R65), G83 (= G93), M84 (= M94), Y108 (≠ F118), D181 (= D190), S203 (= S212), K206 (= K215)
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)
41% identity, 95% coverage: 12:397/408 of query aligns to 1:380/384 of 4iyoD
- active site: R47 (= R65), Y99 (≠ F118), D172 (= D190), K197 (= K215)
- binding serine: Y45 (= Y63), T48 (≠ Y66), Y99 (≠ F118), Y99 (≠ F118), R104 (≠ Y123), K197 (= K215), N227 (≠ Q245), E325 (≠ N342), S326 (≠ N343), T341 (= T358), R361 (= R378)
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)
41% identity, 95% coverage: 12:397/408 of query aligns to 1:380/381 of 4iyoB
- active site: R47 (= R65), Y99 (≠ F118), D172 (= D190), K197 (= K215)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y63), R47 (= R65)
- binding amino-acrylate: Y99 (≠ F118), K197 (= K215), S326 (≠ N343), T341 (= T358), R361 (= R378)
- binding pyruvic acid: Q221 (≠ L239), F224 (= F242)
- binding serine: Y45 (= Y63), T48 (≠ Y66), Y99 (≠ F118), R104 (≠ Y123), N227 (≠ Q245), E325 (≠ N342)
Query Sequence
>WP_020173493.1 NCBI__GCF_000385335.1:WP_020173493.1
MTDFKPKPAAKALRPATQLVHGGTTRSPFGETSEALFLTQGFVYASAEAAEARFKGEDPG
FVYSRYANPTVAMFEERMALLEGAEAARATASGMAAVTAALMGQVKAGDHVIAARALFGS
CLYIVEDLLPRYGVETTLVDGADLSQWKAAVRPQTKVLFLESPTNPCLEVYDIRAIAEIA
HAHGATLVVDNVFATPLLQKPMALGADCVVYSATKHIDGQGRCLGGVILASKAFIEANLH
NFLRQTGPALSPFNAWVLLKSLETLPLRINQQMQSAARIADFLSDAPQISRVLYPGRDDH
PQAEIVRRQMSGGGTMVAFETAGGKASAFAFANALSIIKISNNLGDAKSLITHPATTTHQ
RLTPETRAGLGISDGMLRLSVGLEDVEDLLDDLREALSAVARPHLAAE
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