SitesBLAST
Comparing H281DRAFT_03911 FitnessBrowser__Burk376:H281DRAFT_03911 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)
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
63% identity, 98% coverage: 5:298/300 of query aligns to 3:292/294 of 2bhtA
- active site: K41 (= K47), S69 (= S75), Q199 (= Q205), G203 (= G209), S255 (= S261), C280 (= C286)
- binding pyridoxal-5'-phosphate: K41 (= K47), N71 (= N77), M173 (= M179), G174 (= G180), T175 (= T181), T176 (= T182), T178 (= T184), G208 (= G214), S255 (= S261), C280 (= C286)
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)
63% identity, 98% coverage: 5:298/300 of query aligns to 3:292/303 of P16703
- N71 (= N77) binding pyridoxal 5'-phosphate
- S255 (= S261) binding pyridoxal 5'-phosphate
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
46% identity, 99% coverage: 3:298/300 of query aligns to 5:306/310 of 5xoqA
- binding : T72 (= T74), S73 (= S75), G74 (= G76), T76 (= T78), M123 (= M125), Q144 (= Q146), R218 (vs. gap), H219 (vs. gap), Q222 (≠ R216), G223 (≠ K217), A226 (≠ E220)
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)
44% identity, 98% coverage: 6:298/300 of query aligns to 7:305/306 of 2q3dA
- active site: K44 (= K47), S266 (= S261), P293 (≠ C286)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K47), T71 (= T74), S72 (= S75), N74 (= N77), T75 (= T78), Q144 (= Q146), V177 (≠ M179), G178 (= G180), T179 (= T181), G180 (≠ T182), T182 (= T184), G222 (vs. gap), I223 (vs. gap), S266 (= S261), P293 (≠ C286), D294 (= D287)
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)
44% identity, 98% coverage: 6:298/300 of query aligns to 7:305/310 of P9WP55
- K44 (= K47) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N77) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (≠ GTTGT 180:184) binding pyridoxal 5'-phosphate
- S266 (= S261) binding pyridoxal 5'-phosphate
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)
43% identity, 99% coverage: 4:300/300 of query aligns to 7:310/322 of P47998
- K46 (= K47) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T74) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S75) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N77) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T78) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q146) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H156) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (= G161) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (≠ GTTGT 180:184) binding pyridoxal 5'-phosphate
- T182 (= T181) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T184) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ R216) mutation to A: Impaired interaction with SAT1.
- H221 (≠ E220) mutation to A: Impaired interaction with SAT1.
- K222 (vs. gap) mutation to A: Impaired interaction with SAT1.
- S269 (= S261) binding pyridoxal 5'-phosphate; 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)
43% identity, 99% coverage: 4:300/300 of query aligns to 5:308/320 of 2isqA
- active site: K44 (= K47), S267 (= S261)
- binding pyridoxal-5'-phosphate: K44 (= K47), N75 (= N77), G177 (≠ S178), G179 (= G180), T180 (= T181), G181 (≠ T182), T183 (= T184), G223 (vs. gap), S267 (= S261), P294 (≠ C286)
- binding : T72 (= T74), S73 (= S75), G74 (= G76), T76 (= T78), G122 (= G124), M123 (= M125), K124 (≠ E126), G217 (≠ W218), P218 (= P219), H219 (≠ E220), Q222 (vs. gap), G223 (vs. gap)
P9WP53 O-phosphoserine sulfhydrylase; OPS sulfhydrylase; CysO-thiocarboxylate-dependent cysteine synthase; Cysteine synthase B; CSase B; O-phosphoserine-specific cysteine synthase; [CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase; EC 2.5.1.113 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
42% identity, 99% coverage: 3:298/300 of query aligns to 4:306/323 of P9WP53
- N81 (= N77) binding pyridoxal 5'-phosphate
- R220 (= R216) mutation to A: 700-fold decrease in the rate of the first half-reaction using OPS. Affects neither the rate of the first half-reaction using OAS nor the rate of the second half-reaction using sulfide or CysO-COSH.
- S265 (= S261) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 319:323 mutation Missing: Decreased lifetime of the alpha-aminoacrylate reaction intermediate, increased susceptibility to oxidation by oxidative agents such as hydrogen peroxide, and partial loss of selectivity towards CysO-COSH as sulfur donor.
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
44% identity, 96% coverage: 6:293/300 of query aligns to 7:300/300 of 3zeiA
- active site: K44 (= K47), S266 (= S261), P293 (≠ C286)
- 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 (= T74), S72 (= S75), I126 (≠ R129), Q144 (= Q146), F145 (= F147), K215 (= K217), G222 (vs. gap), A225 (vs. gap), F227 (≠ Y222)
- binding pyridoxal-5'-phosphate: K44 (= K47), N74 (= N77), V177 (≠ M179), G178 (= G180), T179 (= T181), G180 (≠ T182), T182 (= T184), G222 (vs. gap), S266 (= S261), P293 (≠ C286), D294 (= D287)
2q3cA 2.1 a resolution crystal structure of o-acetylserine sulfhydrylase (oass) holoenzyme from mycobacterium tuberculosis in complex with the inhibitory peptide dfsi (see paper)
44% identity, 96% coverage: 6:293/300 of query aligns to 7:300/300 of 2q3cA
- active site: K44 (= K47), S266 (= S261), P293 (≠ C286)
- binding : T71 (= T74), S72 (= S75), G73 (= G76), T75 (= T78), M122 (= M125), Q144 (= Q146), K215 (= K217), G222 (vs. gap), A225 (vs. gap)
3dwgA Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of mycobacterium tuberculosis (see paper)
42% identity, 99% coverage: 3:298/300 of query aligns to 6:308/325 of 3dwgA
- active site: K53 (= K47), S267 (= S261)
- binding pyridoxal-5'-phosphate: K53 (= K47), N83 (= N77), G186 (= G180), T187 (= T181), T188 (= T182), G189 (= G183), T190 (= T184), S267 (= S261), A296 (≠ C286), D297 (= D287)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
43% identity, 99% coverage: 4:300/300 of query aligns to 5:308/320 of 1z7yA
- active site: A44 (≠ K47), S267 (= S261)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G76), N75 (= N77), T76 (= T78), Q145 (= Q146), I178 (≠ M179), G179 (= G180), T180 (= T181), G181 (≠ T182), T183 (= T184), G223 (vs. gap), S267 (= S261), P294 (≠ C286), S295 (≠ D287)
3bm5A Crystal structure of o-acetyl-serine sulfhydrylase from entamoeba histolytica in complex with cysteine (see paper)
41% identity, 99% coverage: 3:298/300 of query aligns to 13:318/338 of 3bm5A
4jbnA Crystal structure of o-acetyl serine sulfhydrylase from entamoeba histolytica in complex with serine acetyl transferase derived tetrapeptide, spsi (see paper)
41% identity, 99% coverage: 3:298/300 of query aligns to 13:318/336 of 4jbnA
4il5A Crystal structure of o-acetyl serine sulfhydrylase from entamoeba histolytica in complex with isoleucine (see paper)
41% identity, 99% coverage: 3:298/300 of query aligns to 13:318/336 of 4il5A