SitesBLAST
Comparing WP_014448615.1 NCBI__GCF_000284315.1:WP_014448615.1 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)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
42% identity, 97% coverage: 9:396/398 of query aligns to 5:392/396 of 4hf8A
- active site: R59 (= R62), Y112 (= Y115), D184 (= D190), K209 (= K215)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G90), I88 (≠ M91), Y112 (= Y115), E155 (= E161), N159 (= N165), D184 (= D190), S206 (= S212), K209 (= K215), S338 (= S342), R373 (= R377)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
42% identity, 97% coverage: 9:396/398 of query aligns to 5:392/396 of 4omaA
- active site: R59 (= R62), Y112 (= Y115), D184 (= D190), K209 (= K215)
- 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 (= Y115), D184 (= D190), S206 (= S212), T208 (= T214), K209 (= K215), V337 (= V341), S338 (= S342), R373 (= R377)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
42% identity, 97% coverage: 9:396/398 of query aligns to 5:392/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
42% identity, 97% coverage: 9:396/398 of query aligns to 5:392/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
42% identity, 97% coverage: 9:396/398 of query aligns to 5:392/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
42% identity, 97% coverage: 9:396/398 of query aligns to 4:391/395 of 5m3zA
- active site: R58 (= R62), Y111 (= Y115), D183 (= D190), K208 (= K215)
- binding norleucine: Y111 (= Y115), H113 (≠ G117), K208 (= K215), V336 (= V341), S337 (= S342)
- binding pyridoxal-5'-phosphate: G86 (= G90), I87 (≠ M91), Y111 (= Y115), E154 (= E161), D183 (= D190), T185 (= T192), S205 (= S212), T207 (= T214), K208 (= K215)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G90), I87 (≠ M91), Y111 (= Y115), D183 (= D190), S205 (= S212), T207 (= T214), K208 (= K215), V336 (= V341), S337 (= S342), R372 (= R377)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
42% identity, 97% coverage: 9:396/398 of query aligns to 5:392/396 of 6egrA
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
44% identity, 98% coverage: 10:398/398 of query aligns to 2:390/392 of 5x2xA
- active site: R55 (= R62), Y108 (= Y115), D180 (= D190), K205 (= K215)
- 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 (= Y115), N155 (= N165), D180 (= D190), S202 (= S212), T204 (= T214), K205 (= K215), V333 (= V341), S334 (= S342), R369 (= R377)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
44% identity, 98% coverage: 10:398/398 of query aligns to 2:390/392 of 5x2wA
- active site: R55 (= R62), Y108 (= Y115), D180 (= D190), K205 (= K215)
- 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 (= Y115), D180 (= D190), S202 (= S212), K205 (= K215), V333 (= V341), S334 (= S342), R369 (= R377)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
44% identity, 98% coverage: 10:398/398 of query aligns to 8:396/398 of 1pg8A
- active site: R61 (= R62), Y114 (= Y115), D186 (= D190), K211 (= K215)
- binding pyridoxal-5'-phosphate: Y59 (= Y60), R61 (= R62), S88 (= S89), G89 (= G90), M90 (= M91), Y114 (= Y115), D186 (= D190), S208 (= S212), T210 (= T214), K211 (= K215)
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, 98% coverage: 10:398/398 of query aligns to 8:396/398 of P13254
- YSR 59:61 (≠ YGR 60:62) binding pyridoxal 5'-phosphate
- 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 (= Y115) binding substrate
- C116 (≠ G117) 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 212:214) binding in other chain
- K211 (= K215) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ G243) 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 (≠ S244) 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
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
44% identity, 98% coverage: 10:398/398 of query aligns to 7:395/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
44% identity, 98% coverage: 10:398/398 of query aligns to 3:391/393 of 5x30C
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
43% identity, 99% coverage: 5:397/398 of query aligns to 1:395/399 of 5dx5A
- active site: R59 (= R62), Y112 (= Y115), D186 (= D190), K211 (= K215)
- binding pyridoxal-5'-phosphate: Y57 (= Y60), R59 (= R62), S86 (= S89), G87 (= G90), M88 (= M91), Y112 (= Y115), D186 (= D190), F189 (= F193), S208 (= S212), T210 (= T214), K211 (= K215)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
40% identity, 97% coverage: 12:398/398 of query aligns to 5:391/393 of 1e5fA
- active site: R55 (= R62), Y108 (= Y115), D181 (= D190), K206 (= K215)
- binding pyridoxal-5'-phosphate: Y53 (= Y60), R55 (= R62), G83 (= G90), M84 (= M91), Y108 (= Y115), D181 (= D190), S203 (= S212), K206 (= K215)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
40% identity, 97% coverage: 12:398/398 of query aligns to 5:391/394 of 1e5eA
- active site: R55 (= R62), Y108 (= Y115), D181 (= D190), K206 (= K215)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y60), R55 (= R62), G83 (= G90), M84 (= M91), Y108 (= Y115), N155 (= N165), D181 (= D190), S203 (= S212), T205 (= T214), K206 (= K215), S335 (= S342), T350 (≠ S357), R370 (= R377)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
41% identity, 97% coverage: 9:396/398 of query aligns to 5:381/386 of 3mkjA
- active site: Y101 (= Y115), D173 (= D190), K198 (= K215)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G90), I77 (≠ M91), Y101 (= Y115), E144 (= E161), D173 (= D190), F176 (= F193), S195 (= S212), T197 (= T214), K198 (= K215)
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
42% identity, 96% coverage: 13:396/398 of query aligns to 4:370/373 of 4l0oH
- active site: R40 (= R62), Y92 (= Y115), D164 (= D190), K189 (= K215)
- binding pyridoxal-5'-phosphate: Y38 (= Y60), R40 (= R62), S67 (= S89), G68 (= G90), L69 (≠ M91), Y92 (= Y115), D164 (= D190), S186 (= S212), T188 (= T214), K189 (= K215)
7d7oB Crystal structure of cystathionine gamma-lyase from bacillus cereus atcc 14579 (see paper)
41% identity, 96% coverage: 13:396/398 of query aligns to 4:376/377 of 7d7oB
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, 96% coverage: 14:396/398 of query aligns to 6:380/384 of 4iyoD
- active site: R47 (= R62), Y99 (= Y115), D172 (= D190), K197 (= K215)
- binding serine: Y45 (= Y60), T48 (≠ M63), Y99 (= Y115), Y99 (= Y115), R104 (≠ A120), K197 (= K215), N227 (≠ G243), E325 (≠ V341), S326 (= S342), T341 (≠ S357), R361 (= R377)
Query Sequence
>WP_014448615.1 NCBI__GCF_000284315.1:WP_014448615.1
MKNKKNYLTPGPRTKCIHTSGPEDPWRALTPPLYQTSTFTFPDFDQVDRVLKGEEEGFVY
GRMGNPTTERFETLVSELEGGEKTRAFASGMGAISAILIHLTKSRPEMAFPKVLYGGTRA
FIEKYLIPQGCLIHWFDPREEGWGEELSRRLSPKTAAVFAETPSNPVMTVIDLGRLSGIA
KSAGVPLVVDNTFATPILQKPLALGADIVVHSATKYLGGHGDLLGGTVTGNASLMERLSF
EEGSYLGATLSPFHSWLLLRGMKTLPLRMEAHCRGAMNIAEFLSHHPMVKSVHYPGLPGD
PGHKVAALQMKGFGGMLSFSLGDDQKARKVASRLEFFKIAVSLGDPESLIEHPASLSHRQ
MSPEGRMALGIDPGFLRVSVGLEDPEDLILDLKRALEA
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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