SitesBLAST
Comparing Pf6N2E2_5896 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_5896 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)
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
34% identity, 96% coverage: 1:365/381 of query aligns to 1:370/373 of 4l0oH
- active site: R40 (= R40), Y92 (= Y92), D164 (= D165), K189 (= K190)
- binding pyridoxal-5'-phosphate: Y38 (= Y38), R40 (= R40), S67 (≠ T67), G68 (= G68), L69 (≠ M69), Y92 (= Y92), D164 (= D165), S186 (= S187), T188 (= T189), K189 (= K190)
7d7oB Crystal structure of cystathionine gamma-lyase from bacillus cereus atcc 14579 (see paper)
33% identity, 96% coverage: 1:365/381 of query aligns to 1:376/377 of 7d7oB
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
34% identity, 96% coverage: 4:367/381 of query aligns to 5:390/392 of 5x2xA
- active site: R55 (= R40), Y108 (= Y92), D180 (= D165), K205 (= K190)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y38), R55 (= R40), G83 (= G68), M84 (= M69), Y108 (= Y92), N155 (= N138), D180 (= D165), S202 (= S187), T204 (= T189), K205 (= K190), V333 (≠ T310), S334 (≠ G311), R369 (= R346)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
34% identity, 96% coverage: 4:367/381 of query aligns to 5:390/392 of 5x2wA
- active site: R55 (= R40), Y108 (= Y92), D180 (= D165), K205 (= K190)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y38), R55 (= R40), S82 (≠ T67), G83 (= G68), M84 (= M69), Y108 (= Y92), D180 (= D165), S202 (= S187), K205 (= K190), V333 (≠ T310), S334 (≠ G311), R369 (= R346)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
34% identity, 96% coverage: 4:367/381 of query aligns to 11:396/398 of 1pg8A
- active site: R61 (= R40), Y114 (= Y92), D186 (= D165), K211 (= K190)
- binding pyridoxal-5'-phosphate: Y59 (= Y38), R61 (= R40), S88 (≠ T67), G89 (= G68), M90 (= M69), Y114 (= Y92), D186 (= D165), S208 (= S187), T210 (= T189), K211 (= K190)
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)
34% identity, 96% coverage: 4:367/381 of query aligns to 11:396/398 of P13254
- YSR 59:61 (= YSR 38:40) binding
- R61 (= R40) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 68:69) binding in other chain
- Y114 (= Y92) binding
- C116 (= C94) 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 187:189) binding in other chain
- K211 (= K190) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R218) 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 (≠ F219) 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 (= R346) binding
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
34% identity, 96% coverage: 1:366/381 of query aligns to 6:395/399 of 5dx5A
- active site: R59 (= R40), Y112 (= Y92), D186 (= D165), K211 (= K190)
- binding pyridoxal-5'-phosphate: Y57 (= Y38), R59 (= R40), S86 (≠ T67), G87 (= G68), M88 (= M69), Y112 (= Y92), D186 (= D165), F189 (≠ W168), S208 (= S187), T210 (= T189), K211 (= K190)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
34% identity, 96% coverage: 4:367/381 of query aligns to 10:395/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
34% identity, 96% coverage: 4:367/381 of query aligns to 6:391/393 of 5x30C
7mcyH Crystal structure of staphylococcus aureus cystathionine gamma lyase, holoenzyme with bound nl3 (see paper)
33% identity, 91% coverage: 22:368/381 of query aligns to 23:380/380 of 7mcyH
Sites not aligning to the query:
7mcuH Crystal structure of staphylococcus aureus cystathionine gamma lyase, holoenzyme with bound nl2 (see paper)
33% identity, 91% coverage: 22:368/381 of query aligns to 23:380/380 of 7mcuH
Sites not aligning to the query:
7mctH Crystal structure of staphylococcus aureus cystathionine gamma lyase, holoenzyme with bound nl1 (see paper)
33% identity, 91% coverage: 22:368/381 of query aligns to 23:380/380 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)
33% identity, 91% coverage: 22:368/381 of query aligns to 23:380/380 of 7mcqA
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Y45 (= Y38), R47 (= R40), S74 (≠ T67), G75 (= G68), V76 (≠ M69), Y99 (= Y92), D171 (= D165), S193 (= S187), T195 (= T189), K196 (= K190), E322 (≠ T310), S323 (≠ G311)
7mcbH Crystal structure of staphylococcus aureus cystathionine gamma lyase holoenzyme (see paper)
33% identity, 91% coverage: 22:368/381 of query aligns to 23:380/380 of 7mcbH
Sites not aligning to the query:
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
31% identity, 97% coverage: 1:370/381 of query aligns to 3:394/394 of 1e5eA
- active site: R55 (= R40), Y108 (= Y92), D181 (= D165), K206 (= K190)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y38), R55 (= R40), G83 (= G68), M84 (= M69), Y108 (= Y92), N155 (= N138), D181 (= D165), S203 (= S187), T205 (= T189), K206 (= K190), S335 (≠ G311), T350 (≠ S326), R370 (= R346)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
31% identity, 97% coverage: 1:368/381 of query aligns to 3:392/393 of 1e5fA
- active site: R55 (= R40), Y108 (= Y92), D181 (= D165), K206 (= K190)
- binding pyridoxal-5'-phosphate: Y53 (= Y38), R55 (= R40), G83 (= G68), M84 (= M69), Y108 (= Y92), D181 (= D165), S203 (= S187), K206 (= K190)
8j6nA Crystal structure of cystathionine gamma-lyase in complex with compound 1 (see paper)
34% identity, 96% coverage: 4:367/381 of query aligns to 10:387/390 of 8j6nA
- binding [6-methyl-4-[(~{E})-(oxamoylhydrazinylidene)methyl]-5-oxidanyl-pyridin-3-yl]methyl dihydrogen phosphate: Y51 (= Y38), R53 (= R40), G81 (= G68), L82 (≠ M69), Y105 (= Y92), E148 (= E134), N152 (= N138), D178 (= D165), S200 (= S187), T202 (= T189), K203 (= K190), E330 (≠ T310), S331 (≠ G311), T346 (≠ S326), R366 (= R346)
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)
36% identity, 90% coverage: 23:365/381 of query aligns to 25:380/381 of 4iyoB
- active site: R47 (= R40), Y99 (= Y92), D172 (= D165), K197 (= K190)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y38), R47 (= R40)
- binding amino-acrylate: Y99 (= Y92), K197 (= K190), S326 (≠ G311), T341 (≠ S326), R361 (= R346)
- binding pyruvic acid: Q221 (≠ N212), F224 (≠ L214)
- binding serine: Y45 (= Y38), T48 (≠ K41), Y99 (= Y92), R104 (≠ K97), N227 (≠ G217), E325 (≠ T310)
4iy7B Crystal structure of cystathionine gamma lyase (xometc) from xanthomonas oryzae pv. Oryzae in complex with e-site serine, a-site external aldimine structure with serine and a-site external aldimine structure with aminoacrylate intermediates (see paper)
36% identity, 90% coverage: 23:365/381 of query aligns to 25:380/381 of 4iy7B
- active site: R47 (= R40), Y99 (= Y92), D172 (= D165), K197 (= K190)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y38), R47 (= R40)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: G75 (= G68), M76 (= M69), Y99 (= Y92), E143 (= E134), N147 (= N138), D172 (= D165), S194 (= S187), K197 (= K190), S326 (≠ G311), L327 (≠ M312), T341 (≠ S326), R361 (= R346)
- binding pyruvic acid: Q221 (≠ N212), F224 (≠ L214)
- binding serine: Y45 (= Y38), T48 (≠ K41), Y99 (= Y92), R104 (≠ K97), N227 (≠ G217), E325 (≠ T310)
4iy7A Crystal structure of cystathionine gamma lyase (xometc) from xanthomonas oryzae pv. Oryzae in complex with e-site serine, a-site external aldimine structure with serine and a-site external aldimine structure with aminoacrylate intermediates (see paper)
36% identity, 90% coverage: 23:365/381 of query aligns to 25:380/381 of 4iy7A
- active site: R47 (= R40), Y99 (= Y92), D172 (= D165), K197 (= K190)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: G75 (= G68), M76 (= M69), Y99 (= Y92), E143 (= E134), N147 (= N138), D172 (= D165), S194 (= S187), K197 (= K190), S326 (≠ G311), L327 (≠ M312), T341 (≠ S326), R361 (= R346)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: Y45 (= Y38), R47 (= R40)
- binding serine: Y45 (= Y38), T48 (≠ K41), Y99 (= Y92), R104 (≠ K97), N227 (≠ G217), E325 (≠ T310)
Query Sequence
>Pf6N2E2_5896 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_5896
MKVSTEILHIKVDDRDARPSVTPIYQCSAFSADSAFFYSRKANPNVSELEQVVASLEGSE
YALAYSTGMSAIYMVLELLKPGASLVINKYIYGCSYKLFQRYAARIGAHLTILDLTTQDG
LNALPANVDMVIFETPTNPFLKDIDIHAVSRAVKQNNPQALVVVDNTWATPIFQKPLNFG
ADISLYSATKYFSGHSDVMGGLVLVNSEMIYNRLLEGRFYSGTILTPNSAWLLRRSMQTF
NLRMEKHSQTTASMLNYLRELPFIEHVYYPRVDGKQLTGYGGIVFVDIRPDLVPFYKTFT
STLKWFGTGTGMACVTSMVAQPFSGSHASMTDQEKADMGIEKGLVRLCFGLEDLDDLKED
LLQAFEAMERMVDQESSLDPA
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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