SitesBLAST
Comparing GFF810 FitnessBrowser__Marino:GFF810 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
69% identity, 98% coverage: 5:294/297 of query aligns to 3:292/303 of P16703
- N71 (= N73) binding
- S255 (= S257) binding
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
68% identity, 98% coverage: 5:294/297 of query aligns to 3:292/294 of 2bhtA
- active site: K41 (= K43), S69 (= S71), Q199 (= Q201), G203 (= G205), S255 (= S257), C280 (= C282)
- binding pyridoxal-5'-phosphate: K41 (= K43), N71 (= N73), M173 (= M175), G174 (= G176), T175 (= T177), T176 (= T178), T178 (= T180), G208 (= G210), S255 (= S257), C280 (= C282)
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)
44% identity, 97% coverage: 6:294/297 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 (= Q142) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H152) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (= G157) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (≠ GTTGT 176:180) binding
- T182 (= T177) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T180) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ R212) mutation to A: Impaired interaction with SAT1.
- H221 (≠ E216) mutation to A: Impaired interaction with SAT1.
- K222 (vs. gap) mutation to A: Impaired interaction with SAT1.
- S269 (= S257) binding ; mutation to A: Strong reduction of cysteine synthase activity.; mutation to T: Reduction of cysteine synthase activity.
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
44% identity, 97% coverage: 6:294/297 of query aligns to 7:306/309 of 7n2tA
2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
44% identity, 97% coverage: 6:294/297 of query aligns to 7:306/320 of 2isqA
- active site: K44 (= K43), S267 (= S257)
- binding pyridoxal-5'-phosphate: K44 (= K43), N75 (= N73), G177 (≠ S174), G179 (= G176), T180 (= T177), G181 (≠ T178), T183 (= T180), G223 (vs. gap), S267 (= S257), P294 (≠ C282)
- binding : T72 (= T70), S73 (= S71), G74 (= G72), T76 (= T74), G122 (= G120), M123 (= M121), K124 (≠ E122), G217 (≠ W214), P218 (= P215), H219 (≠ E216), Q222 (vs. gap), G223 (vs. gap)
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
44% identity, 97% coverage: 6:294/297 of query aligns to 3:301/302 of 2efyA
- active site: K40 (= K43), S70 (= S71), E200 (≠ Q201), S204 (≠ G205), S263 (= S257)
- binding 5-oxohexanoic acid: T69 (= T70), G71 (= G72), T73 (= T74), Q141 (= Q142), G175 (= G176), G219 (≠ R213), M220 (≠ W214), P222 (≠ E216)
- binding pyridoxal-5'-phosphate: K40 (= K43), N72 (= N73), Y172 (≠ S173), G175 (= G176), T176 (= T177), G177 (≠ T178), T179 (= T180), G219 (≠ R213), S263 (= S257), P289 (vs. gap), D290 (= D283)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
44% identity, 97% coverage: 6:294/297 of query aligns to 3:301/302 of 2ecqA
- active site: K40 (= K43), S70 (= S71), E200 (≠ Q201), S204 (≠ G205), S263 (= S257)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K43), G71 (= G72), T73 (= T74), Q141 (= Q142), G219 (≠ R213)
- binding pyridoxal-5'-phosphate: K40 (= K43), N72 (= N73), Y172 (≠ S173), G173 (≠ S174), G175 (= G176), T176 (= T177), T179 (= T180), G219 (≠ R213), S263 (= S257), P289 (vs. gap)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
44% identity, 97% coverage: 6:294/297 of query aligns to 3:301/302 of 2ecoA
- active site: K40 (= K43), S70 (= S71), E200 (≠ Q201), S204 (≠ G205), S263 (= S257)
- binding 4-methyl valeric acid: K40 (= K43), T69 (= T70), G71 (= G72), T73 (= T74), Q141 (= Q142), G175 (= G176), T176 (= T177), G219 (≠ R213)
- binding pyridoxal-5'-phosphate: K40 (= K43), N72 (= N73), Y172 (≠ S173), G175 (= G176), T176 (= T177), T179 (= T180), G219 (≠ R213), S263 (= S257), P289 (vs. gap), D290 (= D283)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
42% identity, 99% coverage: 2:294/297 of query aligns to 1:306/310 of 5xoqA
- binding : T72 (= T70), S73 (= S71), G74 (= G72), T76 (= T74), M123 (= M121), Q144 (= Q142), R218 (vs. gap), H219 (vs. gap), Q222 (≠ R212), G223 (≠ R213), A226 (≠ E216)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
43% identity, 97% coverage: 6:294/297 of query aligns to 7:306/320 of 1z7yA
- active site: A44 (≠ K43), S267 (= S257)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G72), N75 (= N73), T76 (= T74), Q145 (= Q142), I178 (≠ M175), G179 (= G176), T180 (= T177), G181 (≠ T178), T183 (= T180), G223 (vs. gap), S267 (= S257), P294 (≠ C282), S295 (≠ D283)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
43% identity, 96% coverage: 10:294/297 of query aligns to 15:310/341 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 (≠ T138) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (≠ S174) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G176) 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 (≠ A245) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S258) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (≠ A279) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
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)
43% identity, 97% coverage: 6:294/297 of query aligns to 7:305/310 of P9WP55
- K44 (= K43) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N73) binding
- GTGGT 178:182 (≠ GTTGT 176:180) binding
- S266 (= S257) 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)
43% identity, 97% coverage: 6:294/297 of query aligns to 7:305/306 of 2q3dA
- active site: K44 (= K43), S266 (= S257), P293 (≠ C282)
- 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 (= Q142), V177 (≠ M175), G178 (= G176), T179 (= T177), G180 (≠ T178), T182 (= T180), G222 (vs. gap), I223 (vs. gap), S266 (= S257), P293 (≠ C282), D294 (= D283)
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
41% identity, 97% coverage: 6:294/297 of query aligns to 15:314/329 of 3vbeC
- active site: K52 (= K43), S81 (= S71), E212 (≠ Q201), S216 (≠ G205), S275 (= S257), P302 (≠ C282)
- binding pyridoxal-5'-phosphate: K52 (= K43), N83 (= N73), M184 (≠ S173), G187 (= G176), S188 (≠ T177), G189 (≠ T178), T191 (= T180), G231 (vs. gap), S275 (= S257), P302 (≠ C282)
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, 96% coverage: 10:294/297 of query aligns to 83:378/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
3vc3A Crystal structure of beta-cyanoalanine synthase k95a mutant in soybean (see paper)
41% identity, 97% coverage: 6:294/297 of query aligns to 8:307/322 of 3vc3A
- active site: A45 (≠ K43), S268 (= S257), P295 (≠ C282)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-cysteine: T73 (= T70), S74 (= S71), N76 (= N73), M77 (≠ T74), Q146 (= Q142), M177 (≠ S173), G180 (= G176), S181 (≠ T177), G182 (≠ T178), T184 (= T180), G224 (vs. gap), S268 (= S257), P295 (≠ C282)
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)
41% identity, 97% coverage: 6:294/297 of query aligns to 32:331/347 of Q9FS29
- E157 (≠ L129) mutation E->N,Q: No effect on catalytic activities.
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
43% identity, 98% coverage: 5:294/297 of query aligns to 16:316/323 of 4aecA
- active site: K54 (= K43), S277 (= S257)
- binding pyridoxal-5'-phosphate: K54 (= K43), N85 (= N73), I188 (≠ M175), G189 (= G176), T190 (= T177), G191 (≠ T178), G192 (= G179), T193 (= T180), G233 (vs. gap), S277 (= S257), P304 (≠ C282)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
43% identity, 96% coverage: 6:289/297 of query aligns to 7:300/300 of 3zeiA
- active site: K44 (= K43), S266 (= S257), P293 (≠ C282)
- 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 (= T70), S72 (= S71), I126 (≠ R125), Q144 (= Q142), F145 (= F143), K215 (≠ R213), G222 (vs. gap), A225 (vs. gap), F227 (≠ Y218)
- binding pyridoxal-5'-phosphate: K44 (= K43), N74 (= N73), V177 (≠ M175), G178 (= G176), T179 (= T177), G180 (≠ T178), T182 (= T180), G222 (vs. gap), S266 (= S257), P293 (≠ C282), D294 (= D283)
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)
43% identity, 96% coverage: 6:289/297 of query aligns to 7:300/300 of 2q3cA
- active site: K44 (= K43), S266 (= S257), P293 (≠ C282)
- binding : T71 (= T70), S72 (= S71), G73 (= G72), T75 (= T74), M122 (= M121), Q144 (= Q142), K215 (≠ R213), G222 (vs. gap), A225 (vs. gap)
Query Sequence
>GFF810 FitnessBrowser__Marino:GFF810
MHFPTIEDYVGHTPLVRLQRLPGETSNVILAKLEGNNPAGSVKDRPAISMIQEAERRGDI
KPGDTLIEATSGNTGIALAMAAAIKGYRMVLIMPANMSEERRASMRAYGAEIVTVTREEG
METARDLALKMQAEGKGTVLDQFSNQDNPLAHYRTTGPEIWEQTGGRVTHFVSSMGTTGT
IMGVSRYLKERNPDIRIIGLQPKEGASIPGIRRWPEAYLPKIYDAARVDQVLDVGQEEAE
TTMRALASEEGIFCGVSSGGSIAAALKLSQQVENAIIVAIICDRGDRYLSTGVFPGA
Or try a new SitesBLAST search
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