SitesBLAST
Comparing RR42_RS14320 FitnessBrowser__Cup4G11:RR42_RS14320 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)
51% identity, 99% coverage: 5:399/401 of query aligns to 13:405/406 of P9WGB5
- K219 (= K212) 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)
49% identity, 91% coverage: 30:395/401 of query aligns to 27:388/396 of 4omaA
- active site: R59 (= R62), Y112 (≠ F115), D184 (= D187), K209 (= K212)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G90), I88 (≠ M91), Y112 (≠ F115), D184 (= D187), S206 (= S209), T208 (= T211), K209 (= K212), V337 (≠ G344), S338 (≠ N345), R373 (= R380)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
49% identity, 91% coverage: 30:395/401 of query aligns to 27:388/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
49% identity, 91% coverage: 30:395/401 of query aligns to 27:388/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
49% identity, 91% coverage: 30:395/401 of query aligns to 27:388/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
49% identity, 91% coverage: 30:395/401 of query aligns to 26:387/395 of 5m3zA
- active site: R58 (= R62), Y111 (≠ F115), D183 (= D187), K208 (= K212)
- binding norleucine: Y111 (≠ F115), H113 (≠ S117), K208 (= K212), V336 (≠ G344), S337 (≠ N345)
- binding pyridoxal-5'-phosphate: G86 (= G90), I87 (≠ M91), Y111 (≠ F115), E154 (= E158), D183 (= D187), T185 (≠ C189), S205 (= S209), T207 (= T211), K208 (= K212)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G90), I87 (≠ M91), Y111 (≠ F115), D183 (= D187), S205 (= S209), T207 (= T211), K208 (= K212), V336 (≠ G344), S337 (≠ N345), R372 (= R380)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
49% identity, 91% coverage: 30:395/401 of query aligns to 27:388/396 of 4hf8A
- active site: R59 (= R62), Y112 (≠ F115), D184 (= D187), K209 (= K212)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G90), I88 (≠ M91), Y112 (≠ F115), E155 (= E158), N159 (= N162), D184 (= D187), S206 (= S209), K209 (= K212), S338 (≠ N345), R373 (= R380)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
48% identity, 91% coverage: 30:395/401 of query aligns to 27:388/396 of 6egrA
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
47% identity, 91% coverage: 30:395/401 of query aligns to 27:377/386 of 3mkjA
- active site: Y101 (≠ F115), D173 (= D187), K198 (= K212)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G90), I77 (≠ M91), Y101 (≠ F115), E144 (= E158), D173 (= D187), F176 (= F190), S195 (= S209), T197 (= T211), K198 (= K212)
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
41% identity, 98% coverage: 7:399/401 of query aligns to 3:394/399 of 5dx5A
- active site: R59 (= R62), Y112 (≠ F115), D186 (= D187), K211 (= K212)
- binding pyridoxal-5'-phosphate: Y57 (= Y60), R59 (= R62), S86 (= S89), G87 (= G90), M88 (= M91), Y112 (≠ F115), D186 (= D187), F189 (= F190), S208 (= S209), T210 (= T211), K211 (= K212)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
37% identity, 96% coverage: 14:399/401 of query aligns to 7:389/393 of 1e5fA
- active site: R55 (= R62), Y108 (≠ F115), D181 (= D187), K206 (= K212)
- binding pyridoxal-5'-phosphate: Y53 (= Y60), R55 (= R62), G83 (= G90), M84 (= M91), Y108 (≠ F115), D181 (= D187), S203 (= S209), K206 (= K212)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
37% identity, 96% coverage: 14:399/401 of query aligns to 7:389/394 of 1e5eA
- active site: R55 (= R62), Y108 (≠ F115), D181 (= D187), K206 (= K212)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y60), R55 (= R62), G83 (= G90), M84 (= M91), Y108 (≠ F115), N155 (= N162), D181 (= D187), S203 (= S209), T205 (= T211), K206 (= K212), S335 (≠ N345), T350 (= T360), R370 (= R380)
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
40% identity, 92% coverage: 33:400/401 of query aligns to 27:390/393 of 5x30C
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
40% identity, 92% coverage: 33:400/401 of query aligns to 26:389/392 of 5x2xA
- active site: R55 (= R62), Y108 (≠ F115), D180 (= D187), K205 (= K212)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y60), R55 (= R62), G83 (= G90), M84 (= M91), Y108 (≠ F115), N155 (= N162), D180 (= D187), S202 (= S209), T204 (= T211), K205 (= K212), V333 (≠ G344), S334 (≠ N345), R369 (= R380)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
40% identity, 92% coverage: 33:400/401 of query aligns to 26:389/392 of 5x2wA
- active site: R55 (= R62), Y108 (≠ F115), D180 (= D187), K205 (= K212)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y60), R55 (= R62), S82 (= S89), G83 (= G90), M84 (= M91), Y108 (≠ F115), D180 (= D187), S202 (= S209), K205 (= K212), V333 (≠ G344), S334 (≠ N345), R369 (= R380)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
40% identity, 92% coverage: 33:400/401 of query aligns to 32:395/398 of 1pg8A
- active site: R61 (= R62), Y114 (≠ F115), D186 (= D187), K211 (= K212)
- binding pyridoxal-5'-phosphate: Y59 (= Y60), R61 (= R62), S88 (= S89), G89 (= G90), M90 (= M91), Y114 (≠ F115), D186 (= D187), S208 (= S209), T210 (= T211), K211 (= K212)
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)
40% identity, 92% coverage: 33:400/401 of query aligns to 32:395/398 of P13254
- YSR 59:61 (= YSR 60:62) binding
- R61 (= R62) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 90:91) binding in other chain
- Y114 (≠ F115) binding
- C116 (≠ S117) 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 209:211) binding in other chain
- K211 (= K212) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ V240) 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 (≠ R241) 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 (= R380) binding
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
40% identity, 92% coverage: 33:400/401 of query aligns to 31:394/397 of 3vk3A
3aeoA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 containing methionine alpha, beta-enamine-pyridoxamine- 5'-phosphate
37% identity, 93% coverage: 29:400/401 of query aligns to 20:385/387 of 3aeoA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y51 (= Y60), R53 (= R62), G81 (= G90), M82 (= M91), Y106 (≠ F115), E149 (= E158), N153 (= N162), D178 (= D187), S200 (= S209), S202 (≠ T211), K203 (= K212), V329 (≠ G344), S330 (≠ N345), T345 (= T360), R365 (= R380)
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, 93% coverage: 29:400/401 of query aligns to 20:385/387 of 3aelA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]-4-(methylsulfanyl)butanoic acid: Y51 (= Y60), R53 (= R62)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: G81 (= G90), M82 (= M91), Y106 (≠ F115), E149 (= E158), N153 (= N162), D178 (= D187), T180 (≠ C189), S200 (= S209), S202 (≠ T211), K203 (= K212), S330 (≠ N345), T345 (= T360), R365 (= R380)
Query Sequence
>RR42_RS14320 FitnessBrowser__Cup4G11:RR42_RS14320
MNEPLPLDSLGIDTLGVRAGTMRSEFMEHSEAMYLTSSFCFNSAAEAAERFANSESGFTY
SRFTNPTVAMFQSRLAALEGAEACMATASGMSAIMSIVMSAMQAGDHLVSSRAIFGSTMT
LFSNIFAKFGVETTFVDGTDLAAWRAAVKPNTKLFFLETPSNPLTEVADIAAVADIAHNA
GALLVVDNCFCSPALQQPMKFGADIVVHSATKHIDGQGRVLGGAVLGSHDFIMGKVFPFV
RTAGPTLSAFNAWVLLKGMETLAIRMERHSQSALALAEFLESHPAVARVYHPALKSHPQY
EVAQRQQSGGGAIVSFELKGDTPEQQRANAWRVIDNTRVCSITGNLGDTRTTVTHPYTTT
HGRVSPQAKAAAGISEGLIRLAVGLESVADLKADLLRGLQG
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