SitesBLAST
Comparing WP_081423433.1 NCBI__GCF_000008325.1:WP_081423433.1 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)
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
48% identity, 94% coverage: 23:407/411 of query aligns to 1:387/395 of 5m3zA
- active site: R58 (= R79), Y111 (≠ F132), D183 (= D204), K208 (= K229)
- binding norleucine: Y111 (≠ F132), H113 (≠ N134), K208 (= K229), V336 (≠ G356), S337 (≠ N357)
- binding pyridoxal-5'-phosphate: G86 (= G107), I87 (≠ M108), Y111 (≠ F132), E154 (= E175), D183 (= D204), T185 (≠ C206), S205 (= S226), T207 (= T228), K208 (= K229)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G107), I87 (≠ M108), Y111 (≠ F132), D183 (= D204), S205 (= S226), T207 (= T228), K208 (= K229), V336 (≠ G356), S337 (≠ N357), R372 (= R392)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
48% identity, 94% coverage: 23:407/411 of query aligns to 2:388/396 of 4omaA
- active site: R59 (= R79), Y112 (≠ F132), D184 (= D204), K209 (= K229)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G107), I88 (≠ M108), Y112 (≠ F132), D184 (= D204), S206 (= S226), T208 (= T228), K209 (= K229), V337 (≠ G356), S338 (≠ N357), R373 (= R392)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
48% identity, 94% coverage: 23:407/411 of query aligns to 2:388/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
48% identity, 94% coverage: 23:407/411 of query aligns to 2:388/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
48% identity, 94% coverage: 23:407/411 of query aligns to 2:388/396 of 3jw9A
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
48% identity, 94% coverage: 23:407/411 of query aligns to 2:388/396 of 6egrA
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
48% identity, 94% coverage: 23:407/411 of query aligns to 2:388/396 of 4hf8A
- active site: R59 (= R79), Y112 (≠ F132), D184 (= D204), K209 (= K229)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G107), I88 (≠ M108), Y112 (≠ F132), E155 (= E175), N159 (= N179), D184 (= D204), S206 (= S226), K209 (= K229), S338 (≠ N357), R373 (= R392)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
47% identity, 94% coverage: 23:407/411 of query aligns to 2:377/386 of 3mkjA
- active site: Y101 (≠ F132), D173 (= D204), K198 (= K229)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G107), I77 (≠ M108), Y101 (≠ F132), E144 (= E175), D173 (= D204), F176 (= F207), S195 (= S226), T197 (= T228), K198 (= K229)
P9WGB5 O-succinylhomoserine sulfhydrylase; OSH sulfhydrylase; OSHS sulfhydrylase; EC 2.5.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
46% identity, 92% coverage: 31:409/411 of query aligns to 21:403/406 of P9WGB5
- K219 (= K229) modified: N6-(pyridoxal phosphate)lysine
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
43% identity, 88% coverage: 47:409/411 of query aligns to 27:392/399 of 5dx5A
- active site: R59 (= R79), Y112 (≠ F132), D186 (= D204), K211 (= K229)
- binding pyridoxal-5'-phosphate: Y57 (= Y77), R59 (= R79), S86 (= S106), G87 (= G107), M88 (= M108), Y112 (≠ F132), D186 (= D204), F189 (= F207), S208 (= S226), T210 (= T228), K211 (= K229)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
43% identity, 92% coverage: 31:409/411 of query aligns to 11:391/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
43% identity, 92% coverage: 31:409/411 of query aligns to 7:387/393 of 5x30C
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
43% identity, 92% coverage: 31:409/411 of query aligns to 6:386/392 of 5x2xA
- active site: R55 (= R79), Y108 (≠ F132), D180 (= D204), K205 (= K229)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y77), R55 (= R79), G83 (= G107), M84 (= M108), Y108 (≠ F132), N155 (= N179), D180 (= D204), S202 (= S226), T204 (= T228), K205 (= K229), V333 (≠ G356), S334 (≠ N357), R369 (= R392)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
43% identity, 92% coverage: 31:409/411 of query aligns to 6:386/392 of 5x2wA
- active site: R55 (= R79), Y108 (≠ F132), D180 (= D204), K205 (= K229)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y77), R55 (= R79), S82 (= S106), G83 (= G107), M84 (= M108), Y108 (≠ F132), D180 (= D204), S202 (= S226), K205 (= K229), V333 (≠ G356), S334 (≠ N357), R369 (= R392)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
43% identity, 92% coverage: 31:409/411 of query aligns to 12:392/398 of 1pg8A
- active site: R61 (= R79), Y114 (≠ F132), D186 (= D204), K211 (= K229)
- binding pyridoxal-5'-phosphate: Y59 (= Y77), R61 (= R79), S88 (= S106), G89 (= G107), M90 (= M108), Y114 (≠ F132), D186 (= D204), S208 (= S226), T210 (= T228), K211 (= K229)
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)
43% identity, 92% coverage: 31:409/411 of query aligns to 12:392/398 of P13254
- YSR 59:61 (= YSR 77:79) binding
- R61 (= R79) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 107:108) binding in other chain
- Y114 (≠ F132) binding
- C116 (≠ N134) 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 226:228) binding in other chain
- K211 (= K229) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ L257) 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 (≠ R258) 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 (= R392) binding
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)
48% identity, 88% coverage: 49:409/411 of query aligns to 25:378/384 of 4iyoD
- active site: R47 (= R79), Y99 (≠ F132), D172 (= D204), K197 (= K229)
- binding serine: Y45 (= Y77), T48 (≠ F80), Y99 (≠ F132), Y99 (≠ F132), R104 (≠ L137), K197 (= K229), N227 (≠ T259), E325 (≠ G356), S326 (≠ N357), T341 (= T372), R361 (= R392)
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)
48% identity, 88% coverage: 49:409/411 of query aligns to 25:378/381 of 4iyoB
- active site: R47 (= R79), Y99 (≠ F132), D172 (= D204), K197 (= K229)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y77), R47 (= R79)
- binding amino-acrylate: Y99 (≠ F132), K197 (= K229), S326 (≠ N357), T341 (= T372), R361 (= R392)
- binding pyruvic acid: Q221 (≠ I253), F224 (= F256)
- binding serine: Y45 (= Y77), T48 (≠ F80), Y99 (≠ F132), R104 (≠ L137), N227 (≠ T259), E325 (≠ G356)
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)
48% identity, 88% coverage: 49:409/411 of query aligns to 25:378/381 of 4iy7B
- active site: R47 (= R79), Y99 (≠ F132), D172 (= D204), K197 (= K229)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y77), R47 (= R79)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: G75 (= G107), M76 (= M108), Y99 (≠ F132), E143 (= E175), N147 (= N179), D172 (= D204), S194 (= S226), K197 (= K229), S326 (≠ N357), L327 (= L358), T341 (= T372), R361 (= R392)
- binding pyruvic acid: Q221 (≠ I253), F224 (= F256)
- binding serine: Y45 (= Y77), T48 (≠ F80), Y99 (≠ F132), R104 (≠ L137), N227 (≠ T259), E325 (≠ G356)
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)
48% identity, 88% coverage: 49:409/411 of query aligns to 25:378/381 of 4iy7A
- active site: R47 (= R79), Y99 (≠ F132), D172 (= D204), K197 (= K229)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: G75 (= G107), M76 (= M108), Y99 (≠ F132), E143 (= E175), N147 (= N179), D172 (= D204), S194 (= S226), K197 (= K229), S326 (≠ N357), L327 (= L358), T341 (= T372), R361 (= R392)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: Y45 (= Y77), R47 (= R79)
- binding serine: Y45 (= Y77), T48 (≠ F80), Y99 (≠ F132), R104 (≠ L137), N227 (≠ T259), E325 (≠ G356)
Query Sequence
>WP_081423433.1 NCBI__GCF_000008325.1:WP_081423433.1
MRPRPPSIFTTPSKGAGAVDDLDWNEFAMETRAVRAGQRRTMEQEHAEPIFATSSYVFAS
AAEAAERFAGKAAGNIYSRFTNPTVRTFEERLAALEGGERCVAVGSGMAAIASTAFGLLK
AGDHVVCSRSVFGNTTLLFQNYLAKFGVPTTFVGLTDYDGWAAAIRPETRFLFIETPSNP
LTEIADIPRLAEIAHSRGCLLVVDNCFCTPALQRPLALGADIVIHSATKYLDGQGRCVGG
AIVGGRELLDAEIYPFLRTGGPSMSPFNAWVFLKGLETLNLRMKAHCENALGLARWLEAQ
PWVERVHYPGLASHPQHELAARQQSGFGGIVSFEVKGGQEAAWRLIDSTRLLSITGNLGD
AKTTITHPATTTHGRLSPEARAAAGIADGLIRIAVGLENLADIQADLARFA
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