SitesBLAST
Comparing 8501944 FitnessBrowser__Miya:8501944 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)
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)
60% identity, 100% coverage: 1:310/310 of query aligns to 1:310/310 of P9WP55
- K44 (= K44) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N74) binding
- GTGGT 178:182 (= GTGGT 178:182) binding
- S266 (= S266) 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)
61% identity, 98% coverage: 1:305/310 of query aligns to 1:305/306 of 2q3dA
- active site: K44 (= K44), S266 (= S266), P293 (≠ C293)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K44), T71 (= T71), S72 (= S72), G73 (= G73), N74 (= N74), T75 (= T75), Q144 (= Q144), G176 (= G176), V177 (= V177), G178 (= G178), T179 (= T179), G180 (= G180), G181 (= G181), T182 (= T182), Q221 (= Q221), G222 (= G222), I223 (= I223), S266 (= S266), P293 (≠ C293), D294 (= D294)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
60% identity, 97% coverage: 1:300/310 of query aligns to 1:300/300 of 3zeiA
- active site: K44 (= K44), S266 (= S266), P293 (≠ C293)
- 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 (= T71), S72 (= S72), G73 (= G73), T75 (= T75), M122 (= M122), I126 (= I126), Q144 (= Q144), F145 (= F145), K215 (≠ P215), G222 (= G222), G224 (= G224), A225 (= A225), F227 (= F227)
- binding pyridoxal-5'-phosphate: V43 (= V43), K44 (= K44), N74 (= N74), G176 (= G176), V177 (= V177), G178 (= G178), T179 (= T179), G180 (= G180), G181 (= G181), T182 (= T182), Q221 (= Q221), G222 (= G222), I223 (= I223), S266 (= S266), P293 (≠ C293), D294 (= D294)
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)
60% identity, 97% coverage: 1:300/310 of query aligns to 1:300/300 of 2q3cA
- active site: K44 (= K44), S266 (= S266), P293 (≠ C293)
- binding : K44 (= K44), T71 (= T71), S72 (= S72), G73 (= G73), N74 (= N74), T75 (= T75), G121 (= G121), M122 (= M122), Q144 (= Q144), F145 (= F145), G178 (= G178), K215 (≠ P215), Q221 (= Q221), G222 (= G222), G224 (= G224), A225 (= A225)
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
57% identity, 99% coverage: 1:308/310 of query aligns to 11:319/323 of 4aecA
- active site: K54 (= K44), S277 (= S266)
- binding pyridoxal-5'-phosphate: V53 (= V43), K54 (= K44), N85 (= N74), G187 (= G176), I188 (≠ V177), G189 (= G178), T190 (= T179), G191 (= G180), G192 (= G181), T193 (= T182), Q232 (= Q221), G233 (= G222), S277 (= S266), P304 (≠ C293), S305 (≠ D294)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
57% identity, 100% coverage: 1:310/310 of query aligns to 1:313/318 of 4lmaA
- active site: K46 (= K44), S269 (= S266)
- binding pyridoxal-5'-phosphate: V45 (= V43), K46 (= K44), N77 (= N74), G179 (= G176), V180 (= V177), G181 (= G178), T182 (= T179), G183 (= G180), G184 (= G181), T185 (= T182), Q224 (= Q221), G225 (= G222), I226 (= I223), S269 (= S266), P296 (≠ C293), S297 (≠ D294)
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
58% identity, 98% coverage: 3:305/310 of query aligns to 3:306/309 of 7n2tA
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)
57% identity, 99% coverage: 1:308/310 of query aligns to 73:381/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
57% identity, 98% coverage: 3:305/310 of query aligns to 3:306/320 of 2isqA
- active site: K44 (= K44), S267 (= S266)
- binding pyridoxal-5'-phosphate: K44 (= K44), N75 (= N74), G177 (= G176), I178 (≠ V177), G179 (= G178), T180 (= T179), G181 (= G180), G182 (= G181), T183 (= T182), Q222 (= Q221), G223 (= G222), I224 (= I223), S267 (= S266), P294 (≠ C293), S295 (≠ D294)
- binding : K44 (= K44), T72 (= T71), S73 (= S72), G74 (= G73), N75 (= N74), T76 (= T75), S98 (= S97), K121 (= K120), G122 (= G121), M123 (= M122), K124 (≠ R123), Q145 (= Q144), F146 (= F145), G179 (= G178), G217 (= G216), P218 (= P217), H219 (= H218), Q222 (= Q221), G223 (= G222), G225 (= G224), A226 (= A225), F228 (= F227)
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)
57% identity, 98% coverage: 3:305/310 of query aligns to 5:308/322 of P47998
- K46 (= K44) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T71) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S72) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N74) binding ; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T75) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q144) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H154) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (≠ A159) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 178:182) binding
- T182 (= T179) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T182) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ A214) mutation to A: Impaired interaction with SAT1.
- H221 (= H218) mutation to A: Impaired interaction with SAT1.
- K222 (≠ P219) mutation to A: Impaired interaction with SAT1.
- S269 (= S266) binding ; mutation to A: Strong reduction of cysteine synthase activity.; mutation to T: Reduction of cysteine synthase activity.
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
57% identity, 99% coverage: 1:307/310 of query aligns to 1:310/310 of 4lmbA
- active site: K46 (= K44), S269 (= S266)
- binding cysteine: K46 (= K44), T74 (= T71), S75 (= S72), S75 (= S72), G76 (= G73), N77 (= N74), T78 (= T75), M101 (= M98), M125 (= M122), M125 (= M122), Q147 (= Q144), F148 (= F145), F148 (= F145), I223 (= I220), Q224 (= Q221), G225 (= G222), G225 (= G222), I226 (= I223), G227 (= G224), A228 (= A225)
- binding pyridoxal-5'-phosphate: K46 (= K44), N77 (= N74), G179 (= G176), V180 (= V177), G181 (= G178), T182 (= T179), G183 (= G180), G184 (= G181), T185 (= T182), Q224 (= Q221), G225 (= G222), I226 (= I223), S269 (= S266), P296 (≠ C293), S297 (≠ D294)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
56% identity, 98% coverage: 3:305/310 of query aligns to 3:306/320 of 1z7yA
- active site: A44 (≠ K44), S267 (= S266)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: T72 (= T71), G74 (= G73), N75 (= N74), T76 (= T75), Q145 (= Q144), G177 (= G176), I178 (≠ V177), G179 (= G178), T180 (= T179), G181 (= G180), G182 (= G181), T183 (= T182), Q222 (= Q221), G223 (= G222), I224 (= I223), S267 (= S266), P294 (≠ C293), S295 (≠ D294)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
53% identity, 99% coverage: 3:308/310 of query aligns to 7:313/341 of Q93244
- P75 (= P70) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A83) mutation to V: In n5522; severe loss of protein stability.
- S144 (≠ A139) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (= G176) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G178) mutation to R: In n5515; severe loss of protein stability.
- G229 (= G224) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (= R254) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S267) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (≠ F290) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
8b9yC Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
53% identity, 99% coverage: 3:310/310 of query aligns to 10:317/330 of 8b9yC