SitesBLAST
Comparing WP_011881440.1 NCBI__GCF_000016205.1:WP_011881440.1 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)
55% identity, 98% coverage: 8:430/431 of query aligns to 1:425/428 of 7kb1C
- binding pyridoxal-5'-phosphate: Y57 (= Y60), R59 (= R62)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: G87 (= G90), Q88 (= Q91), Y112 (= Y115), N160 (= N162), D185 (= D187), S206 (= S209), T208 (= T211), K209 (= K212), N369 (= N374), I370 (= I375), R404 (= R409)
7kb1A Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
55% identity, 98% coverage: 8:430/431 of query aligns to 1:425/428 of 7kb1A
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y57 (= Y60), R59 (= R62), G87 (= G90), Q88 (= Q91), Y112 (= Y115), N160 (= N162), D185 (= D187), S206 (= S209), T208 (= T211), K209 (= K212), N369 (= N374), I370 (= I375), R404 (= R409)
2ctzA Crystal structure of o-acetyl homoserine sulfhydrylase from thermus thermophilus hb8
53% identity, 97% coverage: 10:429/431 of query aligns to 2:421/421 of 2ctzA
- active site: R54 (= R62), Y107 (= Y115), D180 (= D187), K206 (= K212)
- binding pyridoxal-5'-phosphate: S81 (= S89), G82 (= G90), H83 (≠ Q91), Q86 (≠ V94), Y107 (= Y115), D180 (= D187), T182 (= T189), S203 (= S209), T205 (= T211), K206 (= K212)
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: 10:429/431 of query aligns to 2:421/421 of Q5SK88
- K206 (= K212) modified: N6-(pyridoxal phosphate)lysine
8erjB Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
53% identity, 97% coverage: 11:430/431 of query aligns to 5:425/428 of 8erjB
- binding (2S)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]but-3-enoic acid: G84 (= G90), Q85 (= Q91), Q88 (≠ V94), Y109 (= Y115), D181 (= D187), S204 (= S209), K207 (= K212), A368 (≠ V373), N369 (= N374), T384 (= T389), R404 (= R409)
8erjA Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
53% identity, 97% coverage: 11:430/431 of query aligns to 5:425/428 of 8erjA
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: S83 (= S89), G84 (= G90), Q85 (= Q91), Q88 (≠ V94), Y109 (= Y115), N156 (= N162), D181 (= D187), S204 (= S209), T206 (= T211), K207 (= K212), R404 (= R409)
8erbK Crystal structure of fub7 in complex with vinylglycine ketimine (see paper)
53% identity, 97% coverage: 11:430/431 of query aligns to 6:426/429 of 8erbK
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y55 (= Y60), R57 (= R62), G85 (= G90), Q86 (= Q91), Q89 (≠ V94), Y110 (= Y115), N157 (= N162), D182 (= D187), S205 (= S209), T207 (= T211), K208 (= K212), T385 (= T389), R405 (= R409)
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, 97% coverage: 11:428/431 of query aligns to 8:426/429 of O13326
- G411 (= G413) mutation to D: Impairs homocysteine synthase activity.
8wkoA Crystal structure of o-acetylhomoserine sulfhydrylase from lactobacillus plantarum in the closed form (see paper)
50% identity, 99% coverage: 7:431/431 of query aligns to 5:425/425 of 8wkoA
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: G87 (= G90), S88 (≠ Q91), Y112 (= Y115), E155 (= E158), D184 (= D187), T186 (= T189), S206 (= S209), A207 (≠ L210), T208 (= T211), F209 (≠ Y213), G212 (= G216), M217 (≠ L221), V369 (≠ I375), A370 (≠ G376)
- binding proline: H213 (= H217), Q284 (= Q290), S288 (≠ T294)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
40% identity, 98% coverage: 8:428/431 of query aligns to 5:392/396 of 4hf8A
- active site: R59 (= R62), Y112 (= Y115), D184 (= D187), K209 (= K212)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G90), I88 (≠ Q91), Y112 (= Y115), E155 (= E158), N159 (= N162), D184 (= D187), S206 (= S209), K209 (= K212), S338 (≠ N374), R373 (= R409)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
40% identity, 98% coverage: 8:428/431 of query aligns to 5:392/396 of 4omaA
- active site: R59 (= R62), Y112 (= Y115), D184 (= D187), K209 (= K212)
- 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 (≠ Q91), Y112 (= Y115), D184 (= D187), S206 (= S209), T208 (= T211), K209 (= K212), V337 (= V373), S338 (≠ N374), R373 (= R409)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
40% identity, 98% coverage: 8:428/431 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)
40% identity, 98% coverage: 8:428/431 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)
40% identity, 98% coverage: 8:428/431 of query aligns to 5:392/396 of 3jw9A
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
40% identity, 98% coverage: 8:428/431 of query aligns to 5:392/396 of 6egrA
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
40% identity, 98% coverage: 8:428/431 of query aligns to 4:391/395 of 5m3zA
- active site: R58 (= R62), Y111 (= Y115), D183 (= D187), K208 (= K212)
- binding norleucine: Y111 (= Y115), H113 (≠ G117), K208 (= K212), V336 (= V373), S337 (≠ N374)
- binding pyridoxal-5'-phosphate: G86 (= G90), I87 (≠ Q91), Y111 (= Y115), E154 (= E158), D183 (= D187), T185 (= T189), S205 (= S209), T207 (= T211), K208 (= K212)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G90), I87 (≠ Q91), Y111 (= Y115), D183 (= D187), S205 (= S209), T207 (= T211), K208 (= K212), V336 (= V373), S337 (≠ N374), R372 (= R409)
8ovhA Crystal structure of o-acetyl-l-homoserine sulfhydrolase from saccharomyces cerevisiae in complex with pyridoxal-5'-phosphate (see paper)
44% identity, 97% coverage: 11:428/431 of query aligns to 5:391/400 of 8ovhA
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
40% identity, 97% coverage: 13:428/431 of query aligns to 12:394/398 of 1pg8A
- active site: R61 (= R62), Y114 (= Y115), D186 (= D187), K211 (= K212)
- binding pyridoxal-5'-phosphate: Y59 (= Y60), R61 (= R62), S88 (= S89), G89 (= G90), M90 (≠ Q91), Y114 (= Y115), D186 (= D187), S208 (= S209), T210 (= T211), K211 (= K212)
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)
40% identity, 97% coverage: 13:428/431 of query aligns to 12:394/398 of P13254
- YSR 59:61 (≠ YTR 60:62) binding pyridoxal 5'-phosphate
- R61 (= R62) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (≠ GQ 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 (≠ SLT 209:211) binding in other chain
- K211 (= K212) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R274) 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 (≠ N275) 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 (= R409) binding substrate
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
40% identity, 97% coverage: 13:428/431 of query aligns to 6:388/392 of 5x2xA
- active site: R55 (= R62), Y108 (= Y115), D180 (= D187), K205 (= K212)
- 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 (≠ Q91), Y108 (= Y115), N155 (= N162), D180 (= D187), S202 (= S209), T204 (= T211), K205 (= K212), V333 (= V373), S334 (≠ N374), R369 (= R409)
Query Sequence
>WP_011881440.1 NCBI__GCF_000016205.1:WP_011881440.1
MTDQASSNWRLETIAVHGGYRPDPTTRAVAVPIYQTVAYAFDDTQHGADLFDLKVQGNIY
TRIMNPTTDVLEQRIAALEGGVGALALASGQAAVTYSIQTIAEAGDNIVSASSLYGGTYN
LFAHTLPQYGITTRFADPRDPASFDALIDARTKAIFAESVGNPLGNVTDIAALADIAHRH
GIPLIVDNTVPSPYLLRPFEHGADIVVHSLTKYLGGHGTSLGGAIVDSGKFPWAQHADRF
KRLNEPDVSYHGVVYTEAFGAAAYIGRARVVPLRNMGAAISPFNAFQILQGIETLALRIE
RISDNALKVAQHLARHENVEWVNYAGLPDHPDHPLVARYLSGRAPGILTFGVKGGRDGGA
KFQDALKLFTRLVNIGDTKSLATHPASTTHRQLSPAELAKAGVKEETVRLSIGIEHIDDL
LADLDQALAQL
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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