SitesBLAST
Comparing WP_106717709.1 NCBI__GCF_003010935.1:WP_106717709.1 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)
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
39% identity, 92% coverage: 29:390/395 of query aligns to 19:370/373 of 4l0oH
- active site: R40 (= R64), Y92 (= Y117), D164 (= D188), K189 (= K213)
- binding pyridoxal-5'-phosphate: Y38 (= Y62), R40 (= R64), S67 (= S91), G68 (= G92), L69 (≠ M93), Y92 (= Y117), D164 (= D188), S186 (= S210), T188 (≠ S212), K189 (= K213)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
35% identity, 96% coverage: 10:390/395 of query aligns to 1:389/393 of 1e5fA
- active site: R55 (= R64), Y108 (= Y117), D181 (= D188), K206 (= K213)
- binding pyridoxal-5'-phosphate: Y53 (= Y62), R55 (= R64), G83 (= G92), M84 (= M93), Y108 (= Y117), D181 (= D188), S203 (= S210), K206 (= K213)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
35% identity, 96% coverage: 10:390/395 of query aligns to 1:389/394 of 1e5eA
- active site: R55 (= R64), Y108 (= Y117), D181 (= D188), K206 (= K213)
- 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 (≠ S163), D181 (= D188), S203 (= S210), T205 (≠ S212), K206 (= K213), S335 (= S336), T350 (≠ S350), R370 (= R371)
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
36% identity, 92% coverage: 28:390/395 of query aligns to 20:389/393 of 5x30C
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
36% identity, 92% coverage: 28:390/395 of query aligns to 19:388/392 of 5x2xA
- active site: R55 (= R64), Y108 (= Y117), 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 (= Y62), R55 (= R64), G83 (= G92), M84 (= M93), Y108 (= Y117), N155 (≠ S163), D180 (= D188), S202 (= S210), T204 (≠ S212), K205 (= K213), V333 (= V335), S334 (= S336), R369 (= R371)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
36% identity, 92% coverage: 28:390/395 of query aligns to 19:388/392 of 5x2wA
- active site: R55 (= R64), Y108 (= Y117), 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 (= Y62), R55 (= R64), S82 (= S91), G83 (= G92), M84 (= M93), Y108 (= Y117), D180 (= D188), S202 (= S210), K205 (= K213), V333 (= V335), S334 (= S336), R369 (= R371)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
36% identity, 92% coverage: 28:390/395 of query aligns to 24:393/397 of 3vk3A
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
36% identity, 92% coverage: 28:390/395 of query aligns to 25:394/398 of 1pg8A
- active site: R61 (= R64), Y114 (= Y117), D186 (= D188), K211 (= K213)
- binding pyridoxal-5'-phosphate: Y59 (= Y62), R61 (= R64), S88 (= S91), G89 (= G92), M90 (= M93), Y114 (= Y117), D186 (= D188), S208 (= S210), T210 (≠ S212), 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)
36% identity, 92% coverage: 28:390/395 of query aligns to 25:394/398 of P13254
- YSR 59:61 (= YSR 62:64) binding pyridoxal 5'-phosphate
- 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 substrate
- C116 (≠ D119) 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 (≠ SAS 210:212) binding in other chain
- K211 (= K213) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ S242) 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 (≠ Y243) 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 (= R371) binding substrate
7mcyH Crystal structure of staphylococcus aureus cystathionine gamma lyase, holoenzyme with bound nl3 (see paper)
37% identity, 92% coverage: 29:390/395 of query aligns to 19:377/380 of 7mcyH
Sites not aligning to the query:
7mcuH Crystal structure of staphylococcus aureus cystathionine gamma lyase, holoenzyme with bound nl2 (see paper)
37% identity, 92% coverage: 29:390/395 of query aligns to 19:377/380 of 7mcuH
Sites not aligning to the query:
7mctH Crystal structure of staphylococcus aureus cystathionine gamma lyase, holoenzyme with bound nl1 (see paper)
37% identity, 92% coverage: 29:390/395 of query aligns to 19:377/380 of 7mctH
Sites not aligning to the query:
7mcqA Crystal structure of staphylococcus aureus cystathionine gamma lyase, aoaa-bound enzyme in dimeric form (see paper)
37% identity, 92% coverage: 29:390/395 of query aligns to 19:377/380 of 7mcqA
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Y45 (= Y62), R47 (= R64), S74 (= S91), G75 (= G92), V76 (≠ M93), Y99 (= Y117), D171 (= D188), S193 (= S210), T195 (≠ S212), K196 (= K213), E322 (≠ V335), S323 (= S336)
7mcbH Crystal structure of staphylococcus aureus cystathionine gamma lyase holoenzyme (see paper)
37% identity, 92% coverage: 29:390/395 of query aligns to 19:377/380 of 7mcbH
Sites not aligning to the query:
3aeoA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 containing methionine alpha, beta-enamine-pyridoxamine- 5'-phosphate
37% identity, 91% coverage: 34:392/395 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 (= E159), N153 (≠ S163), D178 (= D188), S200 (= S210), S202 (= S212), K203 (= K213), V329 (= V335), S330 (= S336), T345 (≠ S350), R365 (= R371)
3aelA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 containing methionine imine-pyridoxamine-5'-phosphate and alpha-amino-alpha, beta-butenoic acid-pyridoxal-5'-phosphate
37% identity, 91% coverage: 34:392/395 of query aligns to 23:386/387 of 3aelA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]-4-(methylsulfanyl)butanoic acid: Y51 (= Y62), R53 (= R64)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: G81 (= G92), M82 (= M93), Y106 (= Y117), E149 (= E159), N153 (≠ S163), D178 (= D188), T180 (≠ S190), S200 (= S210), S202 (= S212), K203 (= K213), S330 (= S336), T345 (≠ S350), R365 (= R371)
3aejC Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 tetramer containing michaelis complex and methionine- pyridoxal-5'-phosphate
37% identity, 91% coverage: 34:392/395 of query aligns to 23:386/387 of 3aejC
- active site: R53 (= R64), Y106 (= Y117), D178 (= D188), K203 (= K213)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: F42 (= F53), Y51 (= Y62), R53 (= R64)
- binding methionine: Y106 (= Y117), K203 (= K213), S330 (= S336), L331 (≠ W337), T345 (≠ S350), R365 (= R371)
3aejA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 tetramer containing michaelis complex and methionine- pyridoxal-5'-phosphate
37% identity, 91% coverage: 34:392/395 of query aligns to 23:386/387 of 3aejA
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: Y51 (= Y62), R53 (= R64), G81 (= G92), M82 (= M93), Y106 (= Y117), E149 (= E159), N153 (≠ S163), D178 (= D188), S200 (= S210), S202 (= S212), K203 (= K213), S330 (= S336), L331 (≠ W337), T345 (≠ S350), R365 (= R371)
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)
37% identity, 91% coverage: 30:390/395 of query aligns to 194:560/563 of P55217
- T412 (≠ K247) natural variant: T -> P
- G459 (≠ V294) 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
1i48A Cystathionine gamma-synthase in complex with the inhibitor ctcpo (see paper)
37% identity, 91% coverage: 30:390/395 of query aligns to 27:393/396 of 1i48A
- active site: R61 (= R64), Y114 (= Y117), D187 (= D188), K212 (= K213)
- binding carboxymethylthio-3-(3-chlorophenyl)-1,2,4-oxadiazol: Y114 (= Y117), R115 (≠ G118), A337 (≠ G334), P338 (≠ V335), S339 (= S336), D348 (vs. gap), S354 (= S350), R374 (= R371), S376 (≠ H373)
- binding pyridoxal-5'-phosphate: Y59 (= Y62), R61 (= R64), S88 (= S91), G89 (= G92), M90 (= M93), Y114 (= Y117), D187 (= D188), S209 (= S210), T211 (≠ S212), K212 (= K213), F340 (≠ W337)
Query Sequence
>WP_106717709.1 NCBI__GCF_003010935.1:WP_106717709.1
MSDNPYFHDQDMMAQAATLLAHDEPFPGGSVVPPIYQTSLFTFENYAAMADAFAGRKRQP
MYSRGDNPTVMEFESKIAALEGAEAARAFSSGMGAISAMVLAFVGAGDRIVAVRNCYGDA
YRLFERLLPHLGIRVDYVDGSDPDAVASALPGAKLLYLESPSSMMFELQDIAHYAKLAKQ
HGIVTTIDNSWATPLFQKPISHGIDLVMHSASKYLGGHSDTVAGVVAGSREMIERINGRT
YSYLGAKLSPFEAWLLLRGLRTLTLRLPHHMKSGLTIAERLMAHGNVERVMHPVYSNHPG
KATLTGYSGLFSFEVTDDIDVPAFVDALKLFRIGVSWGGHESLVVPALASLQQTPDANSI
GRFGVSPRTIRLHVGLESVEELWADLVNALTIAKR
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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