SitesBLAST
Comparing WP_011814583.1 NCBI__GCF_000015585.1:WP_011814583.1 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)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
45% identity, 97% coverage: 13:396/397 of query aligns to 7:392/396 of 4omaA
- active site: R59 (= R64), Y112 (≠ F117), D184 (= D189), K209 (= K214)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G92), I88 (≠ M93), Y112 (≠ F117), D184 (= D189), S206 (= S211), T208 (= T213), K209 (= K214), V337 (≠ G341), S338 (≠ N342), R373 (= R377)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
45% identity, 97% coverage: 13:396/397 of query aligns to 7:392/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
45% identity, 97% coverage: 13:396/397 of query aligns to 7:392/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
45% identity, 97% coverage: 13:396/397 of query aligns to 7:392/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
45% identity, 97% coverage: 13:396/397 of query aligns to 6:391/395 of 5m3zA
- active site: R58 (= R64), Y111 (≠ F117), D183 (= D189), K208 (= K214)
- binding norleucine: Y111 (≠ F117), H113 (≠ T119), K208 (= K214), V336 (≠ G341), S337 (≠ N342)
- binding pyridoxal-5'-phosphate: G86 (= G92), I87 (≠ M93), Y111 (≠ F117), E154 (= E160), D183 (= D189), T185 (≠ C191), S205 (= S211), T207 (= T213), K208 (= K214)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G92), I87 (≠ M93), Y111 (≠ F117), D183 (= D189), S205 (= S211), T207 (= T213), K208 (= K214), V336 (≠ G341), S337 (≠ N342), R372 (= R377)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
45% identity, 97% coverage: 13:396/397 of query aligns to 7:392/396 of 6egrA
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
44% identity, 97% coverage: 13:396/397 of query aligns to 7:392/396 of 4hf8A
- active site: R59 (= R64), Y112 (≠ F117), D184 (= D189), K209 (= K214)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G92), I88 (≠ M93), Y112 (≠ F117), E155 (= E160), N159 (= N164), D184 (= D189), S206 (= S211), K209 (= K214), S338 (≠ N342), R373 (= R377)
P9WGB5 O-succinylhomoserine sulfhydrylase; OSH sulfhydrylase; OSHS sulfhydrylase; EC 2.5.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
46% identity, 95% coverage: 19:396/397 of query aligns to 24:405/406 of P9WGB5
- K219 (= K214) modified: N6-(pyridoxal phosphate)lysine
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
44% identity, 97% coverage: 13:396/397 of query aligns to 7:394/399 of 5dx5A
- active site: R59 (= R64), Y112 (≠ F117), D186 (= D189), K211 (= K214)
- binding pyridoxal-5'-phosphate: Y57 (= Y62), R59 (= R64), S86 (= S91), G87 (= G92), M88 (= M93), Y112 (≠ F117), D186 (= D189), F189 (= F192), S208 (= S211), T210 (= T213), K211 (= K214)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
44% identity, 97% coverage: 13:396/397 of query aligns to 7:381/386 of 3mkjA
- active site: Y101 (≠ F117), D173 (= D189), K198 (= K214)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G92), I77 (≠ M93), Y101 (≠ F117), E144 (= E160), D173 (= D189), F176 (= F192), S195 (= S211), T197 (= T213), K198 (= K214)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
40% identity, 91% coverage: 34:396/397 of query aligns to 25:389/393 of 1e5fA
- active site: R55 (= R64), Y108 (≠ F117), D181 (= D189), K206 (= K214)
- binding pyridoxal-5'-phosphate: Y53 (= Y62), R55 (= R64), G83 (= G92), M84 (= M93), Y108 (≠ F117), D181 (= D189), S203 (= S211), K206 (= K214)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
40% identity, 91% coverage: 34:396/397 of query aligns to 25:389/394 of 1e5eA
- active site: R55 (= R64), Y108 (≠ F117), D181 (= D189), K206 (= K214)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y62), R55 (= R64), G83 (= G92), M84 (= M93), Y108 (≠ F117), N155 (= N164), D181 (= D189), S203 (= S211), T205 (= T213), K206 (= K214), S335 (≠ N342), T350 (= T357), R370 (= R377)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
42% identity, 98% coverage: 9:396/397 of query aligns to 5:394/398 of 1pg8A
- active site: R61 (= R64), Y114 (≠ F117), D186 (= D189), K211 (= K214)
- binding pyridoxal-5'-phosphate: Y59 (= Y62), R61 (= R64), S88 (= S91), G89 (= G92), M90 (= M93), Y114 (≠ F117), D186 (= D189), S208 (= S211), T210 (= T213), K211 (= K214)
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)
42% identity, 98% coverage: 9:396/397 of query aligns to 5:394/398 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 (≠ F117) binding substrate
- C116 (≠ T119) 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 211:213) binding in other chain
- K211 (= K214) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ I242) 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 (≠ R243) 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 (= R377) binding substrate
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
42% identity, 97% coverage: 11:396/397 of query aligns to 1:388/392 of 5x2xA
- active site: R55 (= R64), Y108 (≠ F117), D180 (= D189), K205 (= K214)
- 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 (≠ F117), N155 (= N164), D180 (= D189), S202 (= S211), T204 (= T213), K205 (= K214), V333 (≠ G341), S334 (≠ N342), R369 (= R377)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
42% identity, 97% coverage: 11:396/397 of query aligns to 1:388/392 of 5x2wA
- active site: R55 (= R64), Y108 (≠ F117), D180 (= D189), K205 (= K214)
- 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 (≠ F117), D180 (= D189), S202 (= S211), K205 (= K214), V333 (≠ G341), S334 (≠ N342), R369 (= R377)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
42% identity, 98% coverage: 9:396/397 of query aligns to 4:393/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
42% identity, 97% coverage: 11:396/397 of query aligns to 2:389/393 of 5x30C
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)
44% identity, 91% coverage: 34:396/397 of query aligns to 25:380/381 of 4iyoB
- active site: R47 (= R64), Y99 (≠ F117), D172 (= D189), K197 (= K214)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y62), R47 (= R64)
- binding amino-acrylate: Y99 (≠ F117), K197 (= K214), S326 (≠ N342), T341 (= T357), R361 (= R377)
- binding pyruvic acid: Q221 (≠ E237), F224 (≠ G240)
- binding serine: Y45 (= Y62), T48 (≠ F65), Y99 (≠ F117), R104 (≠ S122), N227 (≠ R243), E325 (≠ G341)
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)
44% identity, 91% coverage: 34:396/397 of query aligns to 25:380/381 of 4iy7B
- active site: R47 (= R64), Y99 (≠ F117), D172 (= D189), K197 (= K214)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y62), R47 (= R64)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: G75 (= G92), M76 (= M93), Y99 (≠ F117), E143 (= E160), N147 (= N164), D172 (= D189), S194 (= S211), K197 (= K214), S326 (≠ N342), L327 (= L343), T341 (= T357), R361 (= R377)
- binding pyruvic acid: Q221 (≠ E237), F224 (≠ G240)
- binding serine: Y45 (= Y62), T48 (≠ F65), Y99 (≠ F117), R104 (≠ S122), N227 (≠ R243), E325 (≠ G341)
Query Sequence
>WP_011814583.1 NCBI__GCF_000015585.1:WP_011814583.1
MCTTRPDDDPLAGFESRAVRAGQVRTDAQEQSEPIYPTSSFTFESAAQAAARFSGEDPGN
VYSRFTNPTVRTFCDRLAALEGGQACVGTASGMSAVLATCLGLLQAGDHVVASRTLFGTT
LSLLTKYLPRWGIEVSWVPLSDERAWADAVQPNTRLLFAETPSNPLNEVVDIRRLAEVAH
AHEALLAIDNCFCTPALQRPLEMGADLVIHSATKYLDGQGRCVGGAVVGDAQRVGEEIHG
FIRTAGPCMSPFNAWVFLKGLETLSLRMHAHSRNAQQVAEWLQGHPGVERVHYAGLPDHP
HHRLAAAQQSGFGGIVAFELPGGREAAWRLIDSTRMLSITGNLGDTKSTITHPATTTHGT
ISDELRAAAGIREGLVRVSVGLEDPADIIRDLERGLG
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