SitesBLAST
Comparing 7026046 FitnessBrowser__ANA3:7026046 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)
68% identity, 98% coverage: 6:291/292 of query aligns to 3:292/303 of P16703
- N71 (= N73) binding
- S255 (= S254) binding
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
67% identity, 98% coverage: 6:291/292 of query aligns to 3:292/294 of 2bhtA
- active site: K41 (= K43), S69 (= S71), Q199 (= Q198), G203 (= G202), S255 (= S254), C280 (= C279)
- binding pyridoxal-5'-phosphate: K41 (= K43), N71 (= N73), M173 (= M172), G174 (= G173), T175 (= T174), T176 (= T175), T178 (= T177), G208 (= G207), S255 (= S254), C280 (= C279)
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
44% identity, 98% coverage: 7:292/292 of query aligns to 3:302/302 of 2efyA
- active site: K40 (= K43), S70 (= S71), E200 (≠ Q198), S204 (≠ G202), S263 (= S254)
- binding 5-oxohexanoic acid: T69 (= T70), G71 (= G72), T73 (= T74), Q141 (= Q139), G175 (= G173), G219 (≠ R210), M220 (≠ W211), P222 (≠ Q213)
- binding pyridoxal-5'-phosphate: K40 (= K43), N72 (= N73), Y172 (≠ S170), G175 (= G173), T176 (= T174), G177 (≠ T175), T179 (= T177), G219 (≠ R210), S263 (= S254), P289 (≠ C279), D290 (= D280)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
44% identity, 98% coverage: 7:292/292 of query aligns to 3:302/302 of 2ecqA
- active site: K40 (= K43), S70 (= S71), E200 (≠ Q198), S204 (≠ G202), S263 (= S254)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K43), G71 (= G72), T73 (= T74), Q141 (= Q139), G219 (≠ R210)
- binding pyridoxal-5'-phosphate: K40 (= K43), N72 (= N73), Y172 (≠ S170), G173 (≠ S171), G175 (= G173), T176 (= T174), T179 (= T177), G219 (≠ R210), S263 (= S254), P289 (≠ C279)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
44% identity, 98% coverage: 7:292/292 of query aligns to 3:302/302 of 2ecoA
- active site: K40 (= K43), S70 (= S71), E200 (≠ Q198), S204 (≠ G202), S263 (= S254)
- binding 4-methyl valeric acid: K40 (= K43), T69 (= T70), G71 (= G72), T73 (= T74), Q141 (= Q139), G175 (= G173), T176 (= T174), G219 (≠ R210)
- binding pyridoxal-5'-phosphate: K40 (= K43), N72 (= N73), Y172 (≠ S170), G175 (= G173), T176 (= T174), T179 (= T177), G219 (≠ R210), S263 (= S254), P289 (≠ C279), D290 (= D280)
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
41% identity, 98% coverage: 7:291/292 of query aligns to 15:314/329 of 3vbeC
- active site: K52 (= K43), S81 (= S71), E212 (≠ Q198), S216 (≠ G202), S275 (= S254), P302 (≠ C279)
- binding pyridoxal-5'-phosphate: K52 (= K43), N83 (= N73), M184 (≠ S170), G187 (= G173), S188 (≠ T174), G189 (≠ T175), T191 (= T177), G231 (vs. gap), S275 (= S254), P302 (≠ C279)
3vc3A Crystal structure of beta-cyanoalanine synthase k95a mutant in soybean (see paper)
41% identity, 98% coverage: 7:291/292 of query aligns to 8:307/322 of 3vc3A
- active site: A45 (≠ K43), S268 (= S254), P295 (≠ C279)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-cysteine: T73 (= T70), S74 (= S71), N76 (= N73), M77 (≠ T74), Q146 (= Q139), M177 (≠ S170), G180 (= G173), S181 (≠ T174), G182 (≠ T175), T184 (= T177), G224 (vs. gap), S268 (= S254), P295 (≠ C279)
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, 98% coverage: 7:291/292 of query aligns to 32:331/347 of Q9FS29
- E157 (≠ D123) mutation E->N,Q: No effect on catalytic activities.
8b9yC Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
40% identity, 99% coverage: 5:292/292 of query aligns to 12:313/330 of 8b9yC
8b9yA Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
40% identity, 99% coverage: 5:292/292 of query aligns to 10:296/313 of 8b9yA
- binding o-acetylserine: T76 (= T70), G78 (= G72), N79 (= N73), T80 (= T74)
- binding pyridoxal-5'-phosphate: V47 (= V42), K48 (= K43), N79 (= N73), G183 (= G173), T184 (= T174), G185 (≠ T175), T187 (= T177), S256 (= S254), P283 (≠ C279), S284 (≠ D280)
- binding alpha-D-ribofuranose: C40 (≠ G35), E41 (≠ N36), N42 (= N37), P43 (= P38), A45 (≠ G40), Y285 (≠ R281)
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
42% identity, 96% coverage: 11:291/292 of query aligns to 11:306/309 of 7n2tA
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
39% identity, 99% coverage: 5:292/292 of query aligns to 11:312/329 of 8b9wA
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
40% identity, 97% coverage: 9:292/292 of query aligns to 13:311/341 of Q93244
- P75 (≠ A69) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A82) mutation to V: In n5522; severe loss of protein stability.
- S144 (≠ K135) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (≠ S171) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G173) 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 (≠ T242) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S255) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (≠ A276) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
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)
41% identity, 100% coverage: 1:292/292 of query aligns to 1:306/306 of 2q3dA
- active site: K44 (= K43), S266 (= S254), P293 (≠ C279)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K43), T71 (= T70), S72 (= S71), N74 (= N73), T75 (= T74), Q144 (= Q139), V177 (≠ M172), G178 (= G173), T179 (= T174), G180 (≠ T175), T182 (= T177), G222 (vs. gap), I223 (vs. gap), S266 (= S254), P293 (≠ C279), D294 (= D280)
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)
41% identity, 100% coverage: 1:292/292 of query aligns to 1:306/310 of P9WP55
- K44 (= K43) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N73) binding
- GTGGT 178:182 (≠ GTTGT 173:177) binding
- S266 (= S254) binding
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)
41% identity, 98% coverage: 7:291/292 of query aligns to 9:308/322 of P47998
- K46 (= K43) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T70) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S71) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N73) binding ; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T74) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q139) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H149) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (= G154) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (≠ GTTGT 173:177) binding
- T182 (= T174) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T177) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ R209) mutation to A: Impaired interaction with SAT1.
- H221 (≠ Q213) mutation to A: Impaired interaction with SAT1.
- K222 (≠ E214) mutation to A: Impaired interaction with SAT1.
- S269 (= S254) 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)
41% identity, 98% coverage: 7:291/292 of query aligns to 7:306/320 of 2isqA
- active site: K44 (= K43), S267 (= S254)
- binding pyridoxal-5'-phosphate: K44 (= K43), N75 (= N73), G177 (≠ S171), G179 (= G173), T180 (= T174), G181 (≠ T175), T183 (= T177), G223 (vs. gap), S267 (= S254), P294 (≠ C279)
- binding : T72 (= T70), S73 (= S71), G74 (= G72), T76 (= T74), G122 (≠ N117), M123 (= M118), K124 (≠ E119), G217 (≠ W211), P218 (= P212), H219 (≠ Q213), Q222 (vs. gap), G223 (vs. gap)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
41% identity, 96% coverage: 11:291/292 of query aligns to 12:306/310 of 5xoqA
- binding : T72 (= T70), S73 (= S71), G74 (= G72), T76 (= T74), M123 (= M118), Q144 (= Q139), R218 (vs. gap), H219 (vs. gap), Q222 (≠ R209), G223 (≠ R210), A226 (≠ Q213)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
40% identity, 98% coverage: 7:291/292 of query aligns to 7:306/320 of 1z7yA
- active site: A44 (≠ K43), S267 (= S254)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G72), N75 (= N73), T76 (= T74), Q145 (= Q139), I178 (≠ M172), G179 (= G173), T180 (= T174), G181 (≠ T175), T183 (= T177), G223 (vs. gap), S267 (= S254), P294 (≠ C279), S295 (≠ D280)
D2Z027 O-ureido-L-serine synthase; Cysteine synthase homolog DscD; O-acetylserine sulfhydrylase; EC 2.6.99.3; EC 2.5.1.47 from Streptomyces lavendulae (see paper)
39% identity, 100% coverage: 1:291/292 of query aligns to 1:303/324 of D2Z027
- K43 (= K43) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Loss of catalytic activity, no longer binds N6-(pyridoxal phosphate)lysine.
- V74 (≠ T74) mutation to T: KM for OAS is 61 mM, KM for H(2)S is unchanged.
- Y97 (≠ S97) mutation to F: KM for OAS is unchanged, KM for H(2)S is 0.073 mM.; mutation to M: KM for OAS is 330 mM, KM for H(2)S is 0.084.
- S121 (≠ A121) mutation to A: KM for OAS is 140 mM, KM for H(2)S is 0.095 mM.; mutation to M: KM for OAS is 44 mM, KM for H(2)S is 0.20 mM.
Query Sequence
>7026046 FitnessBrowser__ANA3:7026046
MSDFPTIEACIGQTPLVRLQRLDCGSSTVLLKLEGNNPAGSVKDRAALNMIIQAELRQEI
APGDTLIEATSGNTGIALAMAAAIKGYKMILIMPSNSTQERKDAMQAYGAELLLVDNMEA
ARDLALDLQAQGKGKVLDQFNNQDNANAHFQTTGPEIWQQSQGKITHFVSSMGTTGTIMG
VSKYLKSRNPDITIVGLQPADGSSIPGIRRWPQEYLPGIFDAARVDAVMDIEEQDAKAMA
RTLAREEGICAGVSSGGAVFAALEIARQNPGSVVVAIVCDRGDRYLSSGLFS
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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