SitesBLAST
Comparing WP_012590055.1 NCBI__GCF_000021745.1:WP_012590055.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
56% identity, 94% coverage: 14:395/406 of query aligns to 20:405/406 of P9WGB5
- K219 (= K213) 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)
44% identity, 94% coverage: 15:395/406 of query aligns to 10:392/396 of 4omaA
- active site: R59 (= R63), Y112 (≠ F116), D184 (= D188), K209 (= K213)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G91), I88 (≠ M92), Y112 (≠ F116), D184 (= D188), S206 (= S210), T208 (= T212), K209 (= K213), V337 (≠ S340), S338 (≠ N341), R373 (= R376)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
44% identity, 94% coverage: 15:395/406 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)
44% identity, 94% coverage: 15:395/406 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)
44% identity, 94% coverage: 15:395/406 of query aligns to 10:392/396 of 3jw9A
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
44% identity, 94% coverage: 15:395/406 of query aligns to 10:392/396 of 6egrA
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
44% identity, 94% coverage: 15:395/406 of query aligns to 9:391/395 of 5m3zA
- active site: R58 (= R63), Y111 (≠ F116), D183 (= D188), K208 (= K213)
- binding norleucine: Y111 (≠ F116), H113 (≠ A118), K208 (= K213), V336 (≠ S340), S337 (≠ N341)
- binding pyridoxal-5'-phosphate: G86 (= G91), I87 (≠ M92), Y111 (≠ F116), E154 (= E159), D183 (= D188), T185 (≠ V190), S205 (= S210), T207 (= T212), K208 (= K213)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G91), I87 (≠ M92), Y111 (≠ F116), D183 (= D188), S205 (= S210), T207 (= T212), K208 (= K213), V336 (≠ S340), S337 (≠ N341), R372 (= R376)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
44% identity, 94% coverage: 15:395/406 of query aligns to 10:392/396 of 4hf8A
- active site: R59 (= R63), Y112 (≠ F116), D184 (= D188), K209 (= K213)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G91), I88 (≠ M92), Y112 (≠ F116), E155 (= E159), N159 (= N163), D184 (= D188), S206 (= S210), K209 (= K213), S338 (≠ N341), R373 (= R376)
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
42% identity, 97% coverage: 9:400/406 of query aligns to 4:399/399 of 5dx5A
- active site: R59 (= R63), Y112 (≠ F116), D186 (= D188), K211 (= K213)
- binding pyridoxal-5'-phosphate: Y57 (= Y61), R59 (= R63), S86 (≠ T90), G87 (= G91), M88 (= M92), Y112 (≠ F116), D186 (= D188), F189 (= F191), S208 (= S210), T210 (= T212), K211 (= K213)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
42% identity, 94% coverage: 15:395/406 of query aligns to 10:381/386 of 3mkjA
- active site: Y101 (≠ F116), D173 (= D188), K198 (= K213)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G91), I77 (≠ M92), Y101 (≠ F116), E144 (= E159), D173 (= D188), F176 (= F191), S195 (= S210), T197 (= T212), K198 (= K213)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
44% identity, 93% coverage: 19:397/406 of query aligns to 24:396/398 of 1pg8A
- active site: R61 (= R63), Y114 (≠ F116), D186 (= D188), K211 (= K213)
- binding pyridoxal-5'-phosphate: Y59 (= Y61), R61 (= R63), S88 (≠ T90), G89 (= G91), M90 (= M92), Y114 (≠ F116), D186 (= D188), S208 (= S210), T210 (= T212), K211 (= K213)
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)
44% identity, 93% coverage: 19:397/406 of query aligns to 24:396/398 of P13254
- YSR 59:61 (= YSR 61:63) binding
- R61 (= R63) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 91:92) binding in other chain
- Y114 (≠ F116) binding
- C116 (≠ A118) 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 210:212) binding in other chain
- K211 (= K213) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ L241) 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 (≠ R242) 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 (= R376) binding
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
44% identity, 93% coverage: 19:397/406 of query aligns to 18:390/392 of 5x2xA
- active site: R55 (= R63), Y108 (≠ F116), D180 (= D188), K205 (= K213)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y61), R55 (= R63), G83 (= G91), M84 (= M92), Y108 (≠ F116), N155 (= N163), D180 (= D188), S202 (= S210), T204 (= T212), K205 (= K213), V333 (≠ S340), S334 (≠ N341), R369 (= R376)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
44% identity, 93% coverage: 19:397/406 of query aligns to 18:390/392 of 5x2wA
- active site: R55 (= R63), Y108 (≠ F116), D180 (= D188), K205 (= K213)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y61), R55 (= R63), S82 (≠ T90), G83 (= G91), M84 (= M92), Y108 (≠ F116), D180 (= D188), S202 (= S210), K205 (= K213), V333 (≠ S340), S334 (≠ N341), R369 (= R376)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
44% identity, 93% coverage: 19:397/406 of query aligns to 23:395/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
44% identity, 93% coverage: 19:397/406 of query aligns to 19:391/393 of 5x30C
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
38% identity, 96% coverage: 11:400/406 of query aligns to 3:394/394 of 1e5eA
- active site: R55 (= R63), Y108 (≠ F116), D181 (= D188), K206 (= K213)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y61), R55 (= R63), G83 (= G91), M84 (= M92), Y108 (≠ F116), N155 (= N163), D181 (= D188), S203 (= S210), T205 (= T212), K206 (= K213), S335 (≠ N341), T350 (= T356), R370 (= R376)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
37% identity, 96% coverage: 11:398/406 of query aligns to 3:392/393 of 1e5fA
- active site: R55 (= R63), Y108 (≠ F116), D181 (= D188), K206 (= K213)
- binding pyridoxal-5'-phosphate: Y53 (= Y61), R55 (= R63), G83 (= G91), M84 (= M92), Y108 (≠ F116), D181 (= D188), S203 (= S210), K206 (= K213)
P55217 Cystathionine gamma-synthase 1, chloroplastic; AtCGS1; METHIONINE OVERACCUMULATION 1; O-succinylhomoserine (thiol)-lyase; EC 2.5.1.48 from Arabidopsis thaliana (Mouse-ear cress) (see 4 papers)
40% identity, 84% coverage: 59:398/406 of query aligns to 224:563/563 of P55217
- T412 (≠ A247) natural variant: T -> P
- G459 (= G294) natural variant: G -> A
Sites not aligning to the query:
- 8 natural variant: C -> S
- 55 natural variant: A -> G
- 77 R→H: In mto1-4; over-accumulation of soluble methionine.
- 78 R→K: In mto1-7; over-accumulation of soluble methionine.
- 81 S→N: In mto1-2; over-accumulation of soluble methionine.
- 84 G→D: In mto1-3 and mto1-5; over-accumulation of soluble methionine.; G→S: In mto1-1; over-accumulation of soluble methionine.
- 86 A→V: In mto1-6; over-accumulation of soluble methionine.
- 91 natural variant: A -> G
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)
42% identity, 95% coverage: 11:395/406 of query aligns to 2:380/384 of 4iyoD
- active site: R47 (= R63), Y99 (≠ F116), D172 (= D188), K197 (= K213)
- binding serine: Y45 (= Y61), T48 (≠ Y64), Y99 (≠ F116), Y99 (≠ F116), R104 (≠ Y121), K197 (= K213), N227 (≠ R242), E325 (≠ S340), S326 (≠ N341), T341 (= T356), R361 (= R376)
Query Sequence
>WP_012590055.1 NCBI__GCF_000021745.1:WP_012590055.1
MTDSFGGSKPLRPATLLVHGGGVRTPFGETSEALFLTQGYVFASMEACAARFAGEEPGFV
YSRYGNPTVAMFEGRMALLEGAEAARATATGMAAVTASVMSQVRAGDHVVAARALFGACR
YIVEDHLPRYGVASTLVDGDDLDQWRAAVRLETKVFFLESPTNPCLDVYDIAAIAKIAHD
AGAILVVDNVFATPMLQKPLTLGADLVVYSATKHIDGGGRCLGGVILGAKALVEGDLQQF
LRQTGPALSPFNAWVLLKALETLAIRVERQTKSAARIADFLSEQPAVAFVRYPGRADHPH
ADIARRQMSGGGTLVAFEIVGGKPAAFAFGRALKLIKISSNLGDAKSLITHPATTTHHRL
PPEARAALGVSEGLVRLSVGLEDEEDLIDDLKAALDALQRQDIAAE
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