SitesBLAST
Comparing 202695 FitnessBrowser__MR1:202695 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)
P16703 Cysteine synthase B; CSase B; O-acetylserine (thiol)-lyase B; OAS-TL B; O-acetylserine sulfhydrylase B; EC 2.5.1.47 from Escherichia coli (strain K12) (see paper)
67% identity, 99% coverage: 2:287/288 of query aligns to 3:292/303 of P16703
- N71 (= N69) binding
- S255 (= S250) binding
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
67% identity, 99% coverage: 2:287/288 of query aligns to 3:292/294 of 2bhtA
- active site: K41 (= K39), S69 (= S67), Q199 (= Q194), G203 (= G198), S255 (= S250), C280 (= C275)
- binding pyridoxal-5'-phosphate: K41 (= K39), N71 (= N69), M173 (= M168), G174 (= G169), T175 (= T170), T176 (= T171), T178 (= T173), G208 (= G203), S255 (= S250), C280 (= C275)
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
44% identity, 100% coverage: 1:288/288 of query aligns to 1:302/302 of 2efyA
- active site: K40 (= K39), S70 (= S67), E200 (≠ Q194), S204 (≠ G198), S263 (= S250)
- binding 5-oxohexanoic acid: T69 (= T66), G71 (= G68), T73 (= T70), Q141 (= Q135), G175 (= G169), G219 (≠ R206), M220 (≠ W207), P222 (≠ Q209)
- binding pyridoxal-5'-phosphate: K40 (= K39), N72 (= N69), Y172 (≠ S166), G175 (= G169), T176 (= T170), G177 (≠ T171), T179 (= T173), G219 (≠ R206), S263 (= S250), P289 (≠ C275), D290 (= D276)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
44% identity, 100% coverage: 1:288/288 of query aligns to 1:302/302 of 2ecqA
- active site: K40 (= K39), S70 (= S67), E200 (≠ Q194), S204 (≠ G198), S263 (= S250)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K39), G71 (= G68), T73 (= T70), Q141 (= Q135), G219 (≠ R206)
- binding pyridoxal-5'-phosphate: K40 (= K39), N72 (= N69), Y172 (≠ S166), G173 (≠ S167), G175 (= G169), T176 (= T170), T179 (= T173), G219 (≠ R206), S263 (= S250), P289 (≠ C275)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
44% identity, 100% coverage: 1:288/288 of query aligns to 1:302/302 of 2ecoA
- active site: K40 (= K39), S70 (= S67), E200 (≠ Q194), S204 (≠ G198), S263 (= S250)
- binding 4-methyl valeric acid: K40 (= K39), T69 (= T66), G71 (= G68), T73 (= T70), Q141 (= Q135), G175 (= G169), T176 (= T170), G219 (≠ R206)
- binding pyridoxal-5'-phosphate: K40 (= K39), N72 (= N69), Y172 (≠ S166), G175 (= G169), T176 (= T170), T179 (= T173), G219 (≠ R206), S263 (= S250), P289 (≠ C275), D290 (= D276)
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
41% identity, 99% coverage: 3:287/288 of query aligns to 15:314/329 of 3vbeC
- active site: K52 (= K39), S81 (= S67), E212 (≠ Q194), S216 (≠ G198), S275 (= S250), P302 (≠ C275)
- binding pyridoxal-5'-phosphate: K52 (= K39), N83 (= N69), M184 (≠ S166), G187 (= G169), S188 (≠ T170), G189 (≠ T171), T191 (= T173), G231 (vs. gap), S275 (= S250), P302 (≠ C275)
3vc3A Crystal structure of beta-cyanoalanine synthase k95a mutant in soybean (see paper)
41% identity, 99% coverage: 3:287/288 of query aligns to 8:307/322 of 3vc3A
- active site: A45 (≠ K39), S268 (= S250), P295 (≠ C275)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-cysteine: T73 (= T66), S74 (= S67), N76 (= N69), M77 (≠ T70), Q146 (= Q135), M177 (≠ S166), G180 (= G169), S181 (≠ T170), G182 (≠ T171), T184 (= T173), G224 (vs. gap), S268 (= S250), P295 (≠ C275)
Q9FS29 Bifunctional L-3-cyanoalanine synthase/cysteine synthase 2, mitochondrial; EC 2.5.1.47; EC 4.4.1.9 from Solanum tuberosum (Potato) (see paper)
40% identity, 99% coverage: 3:287/288 of query aligns to 32:331/347 of Q9FS29
- E157 (≠ D119) mutation E->N,Q: No effect on catalytic activities.
8b9yC Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
40% identity, 100% coverage: 2:288/288 of query aligns to 13:313/330 of 8b9yC
8b9yA Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
40% identity, 100% coverage: 2:288/288 of query aligns to 11:296/313 of 8b9yA
- binding o-acetylserine: T76 (= T66), G78 (= G68), N79 (= N69), T80 (= T70)
- binding pyridoxal-5'-phosphate: V47 (= V38), K48 (= K39), N79 (= N69), G183 (= G169), T184 (= T170), G185 (≠ T171), T187 (= T173), S256 (= S250), P283 (≠ C275), S284 (≠ D276)
- binding alpha-D-ribofuranose: C40 (≠ G31), E41 (≠ N32), N42 (= N33), P43 (= P34), A45 (≠ G36), Y285 (≠ R277)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
40% identity, 99% coverage: 5:288/288 of query aligns to 13:311/341 of Q93244
- P75 (≠ A65) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A78) mutation to V: In n5522; severe loss of protein stability.
- S144 (≠ K131) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (≠ S167) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G169) mutation to R: In n5515; severe loss of protein stability.
- G229 (vs. gap) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (≠ A238) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S251) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (≠ A272) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
P9WP55 O-acetylserine sulfhydrylase; OAS sulfhydrylase; OASS; Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine-specific cysteine synthase; Sulfide-dependent cysteine synthase; EC 2.5.1.47 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
40% identity, 99% coverage: 3:288/288 of query aligns to 7:306/310 of P9WP55
- K44 (= K39) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N69) binding
- GTGGT 178:182 (≠ GTTGT 169:173) binding
- S266 (= S250) binding
2q3dA 2.2 a resolution crystal structure of o-acetylserine sulfhydrylase (oass) from mycobacterium tuberculosis in complex with the reaction intermediate alpha-aminoacrylate (see paper)
40% identity, 99% coverage: 3:288/288 of query aligns to 7:306/306 of 2q3dA
- active site: K44 (= K39), S266 (= S250), P293 (≠ C275)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K39), T71 (= T66), S72 (= S67), N74 (= N69), T75 (= T70), Q144 (= Q135), V177 (≠ M168), G178 (= G169), T179 (= T170), G180 (≠ T171), T182 (= T173), G222 (vs. gap), I223 (vs. gap), S266 (= S250), P293 (≠ C275), D294 (= D276)
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
41% identity, 98% coverage: 7:287/288 of query aligns to 11:306/309 of 7n2tA
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
38% identity, 100% coverage: 2:288/288 of query aligns to 12:312/329 of 8b9wA
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
40% identity, 98% coverage: 7:287/288 of query aligns to 12:306/310 of 5xoqA
- binding : T72 (= T66), S73 (= S67), G74 (= G68), T76 (= T70), M123 (= M114), Q144 (= Q135), R218 (vs. gap), H219 (vs. gap), Q222 (≠ R205), G223 (≠ R206), A226 (≠ Q209)
P47998 Cysteine synthase 1; At.OAS.5-8; Beta-substituted Ala synthase 1;1; ARAth-Bsas1;1; CSase A; AtCS-A; Cys-3A; O-acetylserine (thiol)-lyase 1; OAS-TL A; O-acetylserine sulfhydrylase; Protein ONSET OF LEAF DEATH 3; EC 2.5.1.47 from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
40% identity, 99% coverage: 3:287/288 of query aligns to 9:308/322 of P47998
- K46 (= K39) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T66) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S67) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N69) binding ; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T70) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q135) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H145) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (= G150) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (≠ GTTGT 169:173) binding
- T182 (= T170) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T173) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ R205) mutation to A: Impaired interaction with SAT1.
- H221 (≠ Q209) mutation to A: Impaired interaction with SAT1.
- K222 (≠ E210) mutation to A: Impaired interaction with SAT1.
- S269 (= S250) binding ; mutation to A: Strong reduction of cysteine synthase activity.; mutation to T: Reduction of cysteine synthase activity.
2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
40% identity, 99% coverage: 3:287/288 of query aligns to 7:306/320 of 2isqA
- active site: K44 (= K39), S267 (= S250)
- binding pyridoxal-5'-phosphate: K44 (= K39), N75 (= N69), G177 (≠ S167), G179 (= G169), T180 (= T170), G181 (≠ T171), T183 (= T173), G223 (vs. gap), S267 (= S250), P294 (≠ C275)
- binding : T72 (= T66), S73 (= S67), G74 (= G68), T76 (= T70), G122 (≠ N113), M123 (= M114), K124 (≠ E115), G217 (≠ W207), P218 (= P208), H219 (≠ Q209), Q222 (vs. gap), G223 (vs. gap)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
39% identity, 99% coverage: 3:287/288 of query aligns to 7:308/318 of 4lmaA
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
40% identity, 97% coverage: 3:282/288 of query aligns to 7:300/300 of 3zeiA
- active site: K44 (= K39), S266 (= S250), P293 (≠ C275)
- binding 3-[(Z)-[(5Z)-5-[[2-(2-hydroxy-2-oxoethyloxy)phenyl]methylidene]-3-methyl-4-oxidanylidene-1,3-thiazolidin-2-ylidene]amino]benzoic acid: T71 (= T66), S72 (= S67), I126 (≠ R118), Q144 (= Q135), F145 (= F136), K215 (≠ R206), G222 (vs. gap), A225 (vs. gap), F227 (≠ Y211)
- binding pyridoxal-5'-phosphate: K44 (= K39), N74 (= N69), V177 (≠ M168), G178 (= G169), T179 (= T170), G180 (≠ T171), T182 (= T173), G222 (vs. gap), S266 (= S250), P293 (≠ C275), D294 (= D276)
Query Sequence
>202695 FitnessBrowser__MR1:202695
MTIEACIGQTPLVRLQRLDCGSSTVLLKLEGNNPAGSVKDRAALNMINQAELRQEIAPGD
TLIEATSGNTGIALAMAAAIKGYKMILIMPSNSTQERKDAMQAYGAELLLVDNMEAARDL
ALALQAEGKGKVLDQFNNQDNANAHFLTTGPEIWQQSQGKITHFVSSMGTTGTIMGVSKY
LKSRNPDITIVGLQPADGSSIPGIRRWPQEYLPGIFDAARVDLMMDIEEQDAKAMARALA
REEGICAGVSSGGAVYAALELARQYPGSVVVAIVCDRGDRYLSSGLFS
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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