SitesBLAST
Comparing WP_022948641.1 NCBI__GCF_000421465.1:WP_022948641.1 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)
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, 96% coverage: 12:301/303 of query aligns to 3:292/303 of P16703
- N71 (= N80) binding pyridoxal 5'-phosphate
- S255 (= S264) binding pyridoxal 5'-phosphate
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
67% identity, 96% coverage: 10:301/303 of query aligns to 1:292/294 of 2bhtA
- active site: K41 (= K50), S69 (= S78), Q199 (= Q208), G203 (= G212), S255 (= S264), C280 (= C289)
- binding pyridoxal-5'-phosphate: K41 (= K50), N71 (= N80), M173 (= M182), G174 (= G183), T175 (= T184), T176 (= T185), T178 (= T187), G208 (= G217), S255 (= S264), C280 (= C289)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
46% identity, 94% coverage: 17:301/303 of query aligns to 12:306/310 of 5xoqA
- binding : T72 (= T77), S73 (= S78), G74 (= G79), T76 (= T81), M123 (= M128), Q144 (= Q149), R218 (vs. gap), H219 (vs. gap), Q222 (≠ R219), G223 (≠ R220), A226 (≠ P223)
P47999 Cysteine synthase, chloroplastic/chromoplastic; At.OAS.7-4; Beta-substituted Ala synthase 2;1; ARAth-Bsas2;1; CSase B; AtCS-B; CS-B; O-acetylserine (thiol)-lyase; O-acetylserine sulfhydrylase; OAS-TL B; cpACS1; EC 2.5.1.47 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
44% identity, 94% coverage: 17:301/303 of query aligns to 83:378/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
45% identity, 94% coverage: 17:301/303 of query aligns to 11:306/309 of 7n2tA
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
43% identity, 96% coverage: 12:301/303 of query aligns to 16:316/323 of 4aecA
- active site: K54 (= K50), S277 (= S264)
- binding pyridoxal-5'-phosphate: K54 (= K50), N85 (= N80), I188 (≠ M182), G189 (= G183), T190 (= T184), G191 (≠ T185), G192 (= G186), T193 (= T187), G233 (vs. gap), S277 (= S264), P304 (≠ C289)
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, 95% coverage: 16:303/303 of query aligns to 12:310/322 of P47998
- K46 (= K50) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T77) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S78) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N80) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T81) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q149) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H159) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (= G164) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (≠ GTTGT 183:187) binding pyridoxal 5'-phosphate
- T182 (= T184) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T187) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ R219) mutation to A: Impaired interaction with SAT1.
- H221 (≠ P223) mutation to A: Impaired interaction with SAT1.
- K222 (≠ E224) mutation to A: Impaired interaction with SAT1.
- S269 (= S264) 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, 95% coverage: 16:303/303 of query aligns to 10:308/320 of 2isqA
- active site: K44 (= K50), S267 (= S264)
- binding pyridoxal-5'-phosphate: K44 (= K50), N75 (= N80), G177 (≠ S181), G179 (= G183), T180 (= T184), G181 (≠ T185), T183 (= T187), G223 (vs. gap), S267 (= S264), P294 (≠ C289)
- binding : T72 (= T77), S73 (= S78), G74 (= G79), T76 (= T81), G122 (= G127), M123 (= M128), K124 (≠ E129), G217 (≠ W221), P218 (= P222), H219 (≠ P223), Q222 (vs. gap), G223 (vs. gap)
8b9yC Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
42% identity, 96% coverage: 11:301/303 of query aligns to 12:312/330 of 8b9yC
8b9yA Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
42% identity, 96% coverage: 11:301/303 of query aligns to 10:295/313 of 8b9yA
- binding o-acetylserine: T76 (= T77), G78 (= G79), N79 (= N80), T80 (= T81)
- binding pyridoxal-5'-phosphate: V47 (= V49), K48 (= K50), N79 (= N80), G183 (= G183), T184 (= T184), G185 (≠ T185), T187 (= T187), S256 (= S264), P283 (≠ C289), S284 (≠ D290)
- binding alpha-D-ribofuranose: C40 (≠ G42), E41 (≠ N43), N42 (= N44), P43 (= P45), A45 (≠ G47), Y285 (≠ R291)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
43% identity, 95% coverage: 15:301/303 of query aligns to 13:310/341 of Q93244
- P75 (≠ A76) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A89) mutation to V: In n5522; severe loss of protein stability.
- S144 (≠ K145) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (≠ S181) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G183) 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 (= R252) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S265) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (= T286) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
43% identity, 95% coverage: 16:303/303 of query aligns to 10:308/320 of 1z7yA
- active site: A44 (≠ K50), S267 (= S264)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G79), N75 (= N80), T76 (= T81), Q145 (= Q149), I178 (≠ M182), G179 (= G183), T180 (= T184), G181 (≠ T185), T183 (= T187), G223 (vs. gap), S267 (= S264), P294 (≠ C289), S295 (≠ D290)
P0ABK5 Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine sulfhydrylase A; S-carboxymethylcysteine synthase; Sulfate starvation-induced protein 5; SSI5; EC 2.5.1.47; EC 4.5.1.5 from Escherichia coli (strain K12) (see 5 papers)
44% identity, 94% coverage: 16:301/303 of query aligns to 11:312/323 of P0ABK5
- K42 (= K50) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Still stimulates tRNase activity of CdiA-CT in vitro and in vivo.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
42% identity, 95% coverage: 13:301/303 of query aligns to 7:305/306 of 2q3dA
- active site: K44 (= K50), S266 (= S264), P293 (≠ C289)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K50), T71 (= T77), S72 (= S78), N74 (= N80), T75 (= T81), Q144 (= Q149), V177 (≠ M182), G178 (= G183), T179 (= T184), G180 (≠ T185), T182 (= T187), G222 (vs. gap), I223 (vs. gap), S266 (= S264), P293 (≠ C289), D294 (= D290)
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)
42% identity, 95% coverage: 13:301/303 of query aligns to 7:305/310 of P9WP55