SitesBLAST
Comparing PP_2528 FitnessBrowser__Putida:PP_2528 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)
57% identity, 99% coverage: 5:424/425 of query aligns to 9:427/428 of 7kb1C
- binding pyridoxal-5'-phosphate: Y57 (= Y52), R59 (= R54)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: G87 (= G82), Q88 (≠ M83), Y112 (= Y107), N160 (= N154), D185 (= D179), S206 (= S201), T208 (= T203), K209 (= K204), N369 (= N366), I370 (= I367), R404 (= R401)
7kb1A Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
57% identity, 99% coverage: 5:424/425 of query aligns to 9:427/428 of 7kb1A
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y57 (= Y52), R59 (= R54), G87 (= G82), Q88 (≠ M83), Y112 (= Y107), N160 (= N154), D185 (= D179), S206 (= S201), T208 (= T203), K209 (= K204), N369 (= N366), I370 (= I367), R404 (= R401)
2ctzA Crystal structure of o-acetyl homoserine sulfhydrylase from thermus thermophilus hb8
55% identity, 99% coverage: 1:420/425 of query aligns to 1:420/421 of 2ctzA
- active site: R54 (= R54), Y107 (= Y107), D180 (= D179), K206 (= K204)
- binding pyridoxal-5'-phosphate: S81 (= S81), G82 (= G82), H83 (≠ M83), Q86 (≠ I86), Y107 (= Y107), D180 (= D179), T182 (= T181), S203 (= S201), T205 (= T203), K206 (= K204)
Q5SK88 O-acetyl-L-homoserine sulfhydrylase 1; OAH-sulfhydrylase 1; EC 2.5.1.- from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
55% identity, 99% coverage: 1:420/425 of query aligns to 1:420/421 of Q5SK88
- K206 (= K204) modified: N6-(pyridoxal phosphate)lysine
8erbK Crystal structure of fub7 in complex with vinylglycine ketimine (see paper)
53% identity, 100% coverage: 1:425/425 of query aligns to 4:429/429 of 8erbK
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y55 (= Y52), R57 (= R54), G85 (= G82), Q86 (≠ M83), Q89 (≠ I86), Y110 (= Y107), N157 (= N154), D182 (= D179), S205 (= S201), T207 (= T203), K208 (= K204), T385 (= T381), R405 (= R401)
8erjB Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
53% identity, 100% coverage: 1:425/425 of query aligns to 3:428/428 of 8erjB
- binding (2S)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]but-3-enoic acid: G84 (= G82), Q85 (≠ M83), Q88 (≠ I86), Y109 (= Y107), D181 (= D179), S204 (= S201), K207 (= K204), A368 (≠ V365), N369 (= N366), T384 (= T381), R404 (= R401)
8erjA Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
53% identity, 100% coverage: 1:425/425 of query aligns to 3:428/428 of 8erjA
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: S83 (= S81), G84 (= G82), Q85 (≠ M83), Q88 (≠ I86), Y109 (= Y107), N156 (= N154), D181 (= D179), S204 (= S201), T206 (= T203), K207 (= K204), R404 (= R401)
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)
54% identity, 99% coverage: 3:423/425 of query aligns to 8:429/429 of O13326
- G411 (= G405) mutation to D: Impairs homocysteine synthase activity.
8wkoA Crystal structure of o-acetylhomoserine sulfhydrylase from lactobacillus plantarum in the closed form
51% identity, 98% coverage: 3:420/425 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 (= G82), S88 (≠ M83), Y112 (= Y107), E155 (= E150), D184 (= D179), T186 (= T181), S206 (= S201), A207 (≠ L202), T208 (= T203), F209 (≠ Y205), G212 (= G208), M217 (≠ I213), V369 (≠ I367), A370 (≠ G368)
- binding proline: H213 (= H209), Q284 (= Q282), S288 (≠ T286)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
42% identity, 98% coverage: 3:420/425 of query aligns to 8:392/396 of 4hf8A
- active site: R59 (= R54), Y112 (= Y107), D184 (= D179), K209 (= K204)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G82), I88 (≠ M83), Y112 (= Y107), E155 (= E150), N159 (= N154), D184 (= D179), S206 (= S201), K209 (= K204), S338 (≠ N366), R373 (= R401)
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: 3:420/425 of query aligns to 8:392/396 of 4omaA
- active site: R59 (= R54), Y112 (= Y107), D184 (= D179), K209 (= K204)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G82), I88 (≠ M83), Y112 (= Y107), D184 (= D179), S206 (= S201), T208 (= T203), K209 (= K204), V337 (= V365), S338 (≠ N366), R373 (= R401)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
41% identity, 98% coverage: 3:420/425 of query aligns to 8:392/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
41% identity, 98% coverage: 3:420/425 of query aligns to 8:392/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
41% identity, 98% coverage: 3:420/425 of query aligns to 8:392/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
41% identity, 98% coverage: 3:420/425 of query aligns to 7:391/395 of 5m3zA
- active site: R58 (= R54), Y111 (= Y107), D183 (= D179), K208 (= K204)
- binding norleucine: Y111 (= Y107), H113 (≠ G109), K208 (= K204), V336 (= V365), S337 (≠ N366)
- binding pyridoxal-5'-phosphate: G86 (= G82), I87 (≠ M83), Y111 (= Y107), E154 (= E150), D183 (= D179), T185 (= T181), S205 (= S201), T207 (= T203), K208 (= K204)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G82), I87 (≠ M83), Y111 (= Y107), D183 (= D179), S205 (= S201), T207 (= T203), K208 (= K204), V336 (= V365), S337 (≠ N366), R372 (= R401)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
41% identity, 98% coverage: 3:420/425 of query aligns to 8:392/396 of 6egrA
8ovhA Crystal structure of o-acetyl-l-homoserine sulfhydrolase from saccharomyces cerevisiae in complex with pyridoxal-5'-phosphate (see paper)
45% identity, 99% coverage: 3:421/425 of query aligns to 5:392/400 of 8ovhA
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
40% identity, 98% coverage: 3:420/425 of query aligns to 8:381/386 of 3mkjA
- active site: Y101 (= Y107), D173 (= D179), K198 (= K204)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G82), I77 (≠ M83), Y101 (= Y107), E144 (= E150), D173 (= D179), F176 (≠ V182), S195 (= S201), T197 (= T203), K198 (= K204)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
41% identity, 99% coverage: 5:423/425 of query aligns to 12:397/398 of 1pg8A
- active site: R61 (= R54), Y114 (= Y107), D186 (= D179), K211 (= K204)
- binding pyridoxal-5'-phosphate: Y59 (= Y52), R61 (= R54), S88 (= S81), G89 (= G82), M90 (= M83), Y114 (= Y107), D186 (= D179), S208 (= S201), T210 (= T203), K211 (= K204)
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)
41% identity, 99% coverage: 5:423/425 of query aligns to 12:397/398 of P13254
- YSR 59:61 (= YSR 52:54) binding
- R61 (= R54) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 82:83) binding in other chain
- Y114 (= Y107) binding
- C116 (≠ G109) 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 (≠ SLT 201:203) binding in other chain
- K211 (= K204) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R266) 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 (≠ N267) 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 (= R401) binding
Query Sequence
>PP_2528 FitnessBrowser__Putida:PP_2528
MKLETLAIHAGFSPDPTTKAVAVPIYQTTSFAFDDTQHGADLFDLKVAGNIYSRIMNPTN
DVLEQRMAALEGGVGALAVASGMAAITYAIQTVAEAGDNIVSVAKLYGGTYNLLAHTLPR
MGIHTRFAAHDDIAALEALIDARTKAVFCESIGNPAGNIVDIAALAEAAHRHGVPLIVDN
TVATPVLCRPFEHGADIVVHSLTKYIGGHGTSIGGIVIDSGKFPWAENKERFALLNTPDP
SYHGVTYTEAFGPAAFIGRCRVVPLRNTGAALSPFNAFLILQGLETLALRMERHTENALK
VAHYLQAHEQVAWVKFAGLPDHPEHALAQRYTGGKPASILSFGIKGGQAAGARFIDALQL
VVRLVNIGDAKSLACHPASTTHRQLNDDELEKAGVPRDMVRLSIGIEHSDDIIADLAQAL
EASRG
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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