SitesBLAST
Comparing WP_020175871.1 NCBI__GCF_000385335.1:WP_020175871.1 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)
7kb1C Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
56% identity, 97% coverage: 9:426/429 of query aligns to 6:423/428 of 7kb1C
- binding pyridoxal-5'-phosphate: Y57 (= Y59), R59 (= R61)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: G87 (= G89), Q88 (≠ H90), Y112 (= Y114), N160 (= N161), D185 (= D186), S206 (= S208), T208 (= T210), K209 (= K211), N369 (= N372), I370 (≠ V373), R404 (= R407)
7kb1A Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
56% identity, 97% coverage: 9:426/429 of query aligns to 6:423/428 of 7kb1A
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y57 (= Y59), R59 (= R61), G87 (= G89), Q88 (≠ H90), Y112 (= Y114), N160 (= N161), D185 (= D186), S206 (= S208), T208 (= T210), K209 (= K211), N369 (= N372), I370 (≠ V373), R404 (= R407)
8wkoA Crystal structure of o-acetylhomoserine sulfhydrylase from lactobacillus plantarum in the closed form (see paper)
52% identity, 97% coverage: 10:426/429 of query aligns to 9:422/425 of 8wkoA
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: G87 (= G89), S88 (≠ H90), Y112 (= Y114), E155 (= E157), D184 (= D186), T186 (= T188), S206 (= S208), A207 (= A209), T208 (= T210), F209 (= F212), G212 (= G215), M217 (≠ I220), V369 (= V373), A370 (≠ G374)
- binding proline: H213 (= H216), Q284 (≠ T288), S288 (≠ T292)
2ctzA Crystal structure of o-acetyl homoserine sulfhydrylase from thermus thermophilus hb8
53% identity, 97% coverage: 10:426/429 of query aligns to 3:420/421 of 2ctzA
- active site: R54 (= R61), Y107 (= Y114), D180 (= D186), K206 (= K211)
- binding pyridoxal-5'-phosphate: S81 (= S88), G82 (= G89), H83 (= H90), Q86 (= Q93), Y107 (= Y114), D180 (= D186), T182 (= T188), S203 (= S208), T205 (= T210), K206 (= K211)
Q5SK88 O-acetyl-L-homoserine sulfhydrylase 1; OAH-sulfhydrylase 1; EC 2.5.1.- from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
53% identity, 97% coverage: 10:426/429 of query aligns to 3:420/421 of Q5SK88
- K206 (= K211) modified: N6-(pyridoxal phosphate)lysine
O13326 Homocysteine synthase; O-acetylhomoserine sulfhydrylase; OAH SHL; OAH sulfhydrylase; EC 2.5.1.49 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
52% identity, 98% coverage: 10:429/429 of query aligns to 8:429/429 of O13326
- G411 (= G411) mutation to D: Impairs homocysteine synthase activity.
8erbK Crystal structure of fub7 in complex with vinylglycine ketimine (see paper)
50% identity, 98% coverage: 10:429/429 of query aligns to 6:427/429 of 8erbK
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y55 (= Y59), R57 (= R61), G85 (= G89), Q86 (≠ H90), Q89 (= Q93), Y110 (= Y114), N157 (= N161), D182 (= D186), S205 (= S208), T207 (= T210), K208 (= K211), T385 (= T387), R405 (= R407)
8erjB Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
50% identity, 98% coverage: 10:429/429 of query aligns to 5:426/428 of 8erjB
- binding (2S)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]but-3-enoic acid: G84 (= G89), Q85 (≠ H90), Q88 (= Q93), Y109 (= Y114), D181 (= D186), S204 (= S208), K207 (= K211), A368 (= A371), N369 (= N372), T384 (= T387), R404 (= R407)
8erjA Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
50% identity, 98% coverage: 10:429/429 of query aligns to 5:426/428 of 8erjA
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: S83 (= S88), G84 (= G89), Q85 (≠ H90), Q88 (= Q93), Y109 (= Y114), N156 (= N161), D181 (= D186), S204 (= S208), T206 (= T210), K207 (= K211), R404 (= R407)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
41% identity, 98% coverage: 9:429/429 of query aligns to 7:395/396 of 4hf8A
- active site: R59 (= R61), Y112 (= Y114), D184 (= D186), K209 (= K211)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G89), I88 (≠ H90), Y112 (= Y114), E155 (= E157), N159 (= N161), D184 (= D186), S206 (= S208), K209 (= K211), S338 (≠ N372), R373 (= R407)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
41% identity, 98% coverage: 9:429/429 of query aligns to 7:395/396 of 4omaA
- active site: R59 (= R61), Y112 (= Y114), D184 (= D186), K209 (= K211)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G89), I88 (≠ H90), Y112 (= Y114), D184 (= D186), S206 (= S208), T208 (= T210), K209 (= K211), V337 (≠ A371), S338 (≠ N372), R373 (= R407)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
41% identity, 98% coverage: 9:429/429 of query aligns to 7:395/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
41% identity, 98% coverage: 9:429/429 of query aligns to 7:395/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
41% identity, 98% coverage: 9:429/429 of query aligns to 7:395/396 of 3jw9A
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
41% identity, 98% coverage: 9:429/429 of query aligns to 7:395/396 of 6egrA
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
41% identity, 98% coverage: 9:429/429 of query aligns to 6:394/395 of 5m3zA
- active site: R58 (= R61), Y111 (= Y114), D183 (= D186), K208 (= K211)
- binding norleucine: Y111 (= Y114), H113 (≠ G116), K208 (= K211), V336 (≠ A371), S337 (≠ N372)
- binding pyridoxal-5'-phosphate: G86 (= G89), I87 (≠ H90), Y111 (= Y114), E154 (= E157), D183 (= D186), T185 (= T188), S205 (= S208), T207 (= T210), K208 (= K211)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G89), I87 (≠ H90), Y111 (= Y114), D183 (= D186), S205 (= S208), T207 (= T210), K208 (= K211), V336 (≠ A371), S337 (≠ N372), R372 (= R407)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
40% identity, 98% coverage: 9:429/429 of query aligns to 7:384/386 of 3mkjA
- active site: Y101 (= Y114), D173 (= D186), K198 (= K211)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G89), I77 (≠ H90), Y101 (= Y114), E144 (= E157), D173 (= D186), F176 (≠ L189), S195 (= S208), T197 (= T210), K198 (= K211)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
42% identity, 98% coverage: 8:429/429 of query aligns to 8:397/398 of 1pg8A
- active site: R61 (= R61), Y114 (= Y114), D186 (= D186), K211 (= K211)
- binding pyridoxal-5'-phosphate: Y59 (= Y59), R61 (= R61), S88 (= S88), G89 (= G89), M90 (≠ H90), Y114 (= Y114), D186 (= D186), S208 (= S208), T210 (= T210), K211 (= K211)
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: 8:429/429 of query aligns to 8:397/398 of P13254
- YSR 59:61 (≠ YTR 59:61) binding pyridoxal 5'-phosphate
- R61 (= R61) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (≠ GH 89:90) binding in other chain
- Y114 (= Y114) binding substrate
- C116 (≠ G116) 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 208:210) binding in other chain
- K211 (= K211) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R272) 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 (= D273) 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 (= R407) binding substrate
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
42% identity, 98% coverage: 8:429/429 of query aligns to 2:391/392 of 5x2xA
- active site: R55 (= R61), Y108 (= Y114), D180 (= D186), K205 (= K211)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y59), R55 (= R61), G83 (= G89), M84 (≠ H90), Y108 (= Y114), N155 (= N161), D180 (= D186), S202 (= S208), T204 (= T210), K205 (= K211), V333 (≠ A371), S334 (≠ N372), R369 (= R407)
Query Sequence
>WP_020175871.1 NCBI__GCF_000385335.1:WP_020175871.1
MTDLIAPPGFATQAVHAGARPDPTTGARATPIYQTTSFVFEDVDHAAALFGLQAFGNIYT
RITNPTNAVLEERIAALEGGTAGLAVASGHAAQLLVFHTLLEPGDEIVAATKLYGGSINQ
LNHAFKKFGWGVKWADPDDLPSFAAAITPKTKAIFIESIANPGGVVTDIEAIAAIAHEKH
LPLVVDNTLATPYLVRPFEHGADIIVHSATKFLGGHGNSIGGLIVDGGTFDWMADQRYPS
LSAPRPEYGGMVLGEVFGNFAFAIAARVLGLRDLGPALSPFNAFLILTGIETLPLRMQRH
SENALAVAEHLAQHNAVNWVSYPGLSGDRYHNLAKKYCPAGAGAVFTFGLKGGYDSGIAL
VKRLKLFSHLANVGDTRSLVIHPASTTHRQLADDQKILAGAGPDVVRLSVGIEDKADLIA
DLDQALLAA
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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