SitesBLAST
Comparing GFF3937 FitnessBrowser__WCS417:GFF3937 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)
71% identity, 97% coverage: 7:298/300 of query aligns to 3:294/303 of P16703
- N71 (= N75) binding
- S255 (= S259) binding
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
71% identity, 97% coverage: 7:298/300 of query aligns to 3:294/294 of 2bhtA
- active site: K41 (= K45), S69 (= S73), Q199 (= Q203), G203 (= G207), S255 (= S259), C280 (= C284)
- binding pyridoxal-5'-phosphate: K41 (= K45), N71 (= N75), M173 (= M177), G174 (= G178), T175 (= T179), T176 (= T180), T178 (= T182), G208 (= G212), S255 (= S259), C280 (= C284)
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, 97% coverage: 8:297/300 of query aligns to 9:309/322 of P47998
- K46 (= K45) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T72) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S73) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N75) binding ; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T76) 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 (= G159) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (≠ GTTGT 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 (≠ R214) mutation to A: Impaired interaction with SAT1.
- H221 (≠ E218) mutation to A: Impaired interaction with SAT1.
- K222 (≠ E219) mutation to A: Impaired interaction with SAT1.
- S269 (= S259) 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)
43% identity, 97% coverage: 8:297/300 of query aligns to 7:307/320 of 2isqA
- active site: K44 (= K45), S267 (= S259)
- binding pyridoxal-5'-phosphate: K44 (= K45), N75 (= N75), G177 (≠ S176), G179 (= G178), T180 (= T179), G181 (≠ T180), T183 (= T182), G223 (vs. gap), S267 (= S259), P294 (≠ C284)
- binding : T72 (= T72), S73 (= S73), G74 (= G74), T76 (= T76), G122 (= G122), M123 (= M123), K124 (≠ E124), G217 (≠ W216), P218 (= P217), H219 (≠ E218), Q222 (vs. gap), G223 (vs. gap)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
43% identity, 97% coverage: 8:297/300 of query aligns to 7:307/320 of 1z7yA
- active site: A44 (≠ K45), S267 (= S259)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G74), N75 (= N75), T76 (= T76), Q145 (= Q144), I178 (≠ M177), G179 (= G178), T180 (= T179), G181 (≠ T180), T183 (= T182), G223 (vs. gap), S267 (= S259), P294 (≠ C284), S295 (≠ D285)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
42% identity, 96% coverage: 9:297/300 of query aligns to 9:307/310 of 5xoqA
- binding : T72 (= T72), S73 (= S73), G74 (= G74), T76 (= T76), M123 (= M123), Q144 (= Q144), R218 (vs. gap), H219 (vs. gap), Q222 (≠ R214), G223 (≠ R215), A226 (≠ E218)
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
42% identity, 97% coverage: 6:296/300 of query aligns to 11:311/329 of 8b9wA
8b9yC Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
42% identity, 97% coverage: 6:296/300 of query aligns to 12:312/330 of 8b9yC
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
43% identity, 97% coverage: 8:297/300 of query aligns to 7:307/309 of 7n2tA
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, 96% coverage: 8:296/300 of query aligns to 7:305/310 of P9WP55
- K44 (= K45) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N75) binding
- GTGGT 178:182 (≠ GTTGT 178:182) binding
- S266 (= S259) 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)
41% identity, 96% coverage: 8:296/300 of query aligns to 7:305/306 of 2q3dA
- active site: K44 (= K45), S266 (= S259), P293 (≠ C284)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K45), T71 (= T72), S72 (= S73), N74 (= N75), T75 (= T76), Q144 (= Q144), V177 (≠ M177), G178 (= G178), T179 (= T179), G180 (≠ T180), T182 (= T182), G222 (vs. gap), I223 (vs. gap), S266 (= S259), P293 (≠ C284), D294 (= D285)
8b9yA Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
42% identity, 97% coverage: 6:296/300 of query aligns to 10:295/313 of 8b9yA
- binding o-acetylserine: T76 (= T72), G78 (= G74), N79 (= N75), T80 (= T76)
- binding pyridoxal-5'-phosphate: V47 (= V44), K48 (= K45), N79 (= N75), G183 (= G178), T184 (= T179), G185 (≠ T180), T187 (= T182), S256 (= S259), P283 (≠ C284), S284 (≠ D285)
- binding alpha-D-ribofuranose: C40 (≠ G37), E41 (≠ N38), N42 (= N39), P43 (= P40), A45 (≠ G42), Y285 (≠ R286)
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: 9:298/300 of query aligns to 12:312/341 of Q93244
- P75 (≠ A71) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A84) mutation to V: In n5522; severe loss of protein stability.
- S144 (vs. gap) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (≠ S176) 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 (vs. gap) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (= R247) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S260) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (≠ A281) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
41% identity, 95% coverage: 8:291/300 of query aligns to 7:300/300 of 3zeiA
- active site: K44 (= K45), S266 (= S259), P293 (≠ C284)
- 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 (= T72), S72 (= S73), I126 (≠ R127), Q144 (= Q144), F145 (= F145), K215 (≠ R215), G222 (vs. gap), A225 (vs. gap), F227 (≠ Y220)
- binding pyridoxal-5'-phosphate: K44 (= K45), N74 (= N75), V177 (≠ M177), G178 (= G178), T179 (= T179), G180 (≠ T180), T182 (= T182), G222 (vs. gap), S266 (= S259), P293 (≠ C284), D294 (= D285)
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)
41% identity, 95% coverage: 8:291/300 of query aligns to 7:300/300 of 2q3cA
- active site: K44 (= K45), S266 (= S259), P293 (≠ C284)
- binding : T71 (= T72), S72 (= S73), G73 (= G74), T75 (= T76), M122 (= M123), Q144 (= Q144), K215 (≠ R215), G222 (vs. gap), A225 (vs. gap)
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
40% identity, 96% coverage: 8:296/300 of query aligns to 17:316/323 of 4aecA
- active site: K54 (= K45), S277 (= S259)
- binding pyridoxal-5'-phosphate: K54 (= K45), N85 (= N75), I188 (≠ M177), G189 (= G178), T190 (= T179), G191 (≠ T180), G192 (= G181), T193 (= T182), G233 (vs. gap), S277 (= S259), P304 (≠ C284)
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)
41% identity, 96% coverage: 9:297/300 of query aligns to 80:379/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
41% identity, 96% coverage: 8:296/300 of query aligns to 3:301/302 of 2efyA
- active site: K40 (= K45), S70 (= S73), E200 (≠ Q203), S204 (≠ G207), S263 (= S259)
- binding 5-oxohexanoic acid: T69 (= T72), G71 (= G74), T73 (= T76), Q141 (= Q144), G175 (= G178), G219 (≠ R215), M220 (≠ W216), P222 (≠ E218)
- binding pyridoxal-5'-phosphate: K40 (= K45), N72 (= N75), Y172 (≠ S175), G175 (= G178), T176 (= T179), G177 (≠ T180), T179 (= T182), G219 (≠ R215), S263 (= S259), P289 (vs. gap), D290 (= D285)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
41% identity, 96% coverage: 8:296/300 of query aligns to 3:301/302 of 2ecqA
- active site: K40 (= K45), S70 (= S73), E200 (≠ Q203), S204 (≠ G207), S263 (= S259)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K45), G71 (= G74), T73 (= T76), Q141 (= Q144), G219 (≠ R215)
- binding pyridoxal-5'-phosphate: K40 (= K45), N72 (= N75), Y172 (≠ S175), G173 (≠ S176), G175 (= G178), T176 (= T179), T179 (= T182), G219 (≠ R215), S263 (= S259), P289 (vs. gap)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
41% identity, 96% coverage: 8:296/300 of query aligns to 3:301/302 of 2ecoA
- active site: K40 (= K45), S70 (= S73), E200 (≠ Q203), S204 (≠ G207), S263 (= S259)
- binding 4-methyl valeric acid: K40 (= K45), T69 (= T72), G71 (= G74), T73 (= T76), Q141 (= Q144), G175 (= G178), T176 (= T179), G219 (≠ R215)
- binding pyridoxal-5'-phosphate: K40 (= K45), N72 (= N75), Y172 (≠ S175), G175 (= G178), T176 (= T179), T179 (= T182), G219 (≠ R215), S263 (= S259), P289 (vs. gap), D290 (= D285)
Query Sequence
>GFF3937 FitnessBrowser__WCS417:GFF3937
MTLQYPTIADCVGNTPLVRLQRMAGDTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRG
QIKPGDTLIEATSGNTGIALAMAAAIKGYKMILIMPDNGSAERKAAMTAYGAQLILVTQE
DGMEGARDLAERMAAEGRGLVLDQFANGDNPEAHYTSTGPEIWRQTQGTITHFVSSMGTT
GTIMGNSRYLKEQNPAIQIVGLQPMEGSAIPGIRRWPEEYLPKIYNSSRVDRIIDMAQRE
AEDTTRRLAREEGIFCGVSSGGAVAGMLRLSKEVENAVIVAIICDRGDRYLSTGIFDEPN
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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