SitesBLAST
Comparing HSERO_RS04915 FitnessBrowser__HerbieS:HSERO_RS04915 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)
64% identity, 98% coverage: 5:298/300 of query aligns to 3:292/303 of P16703
- N71 (= N77) binding
- S255 (= S261) binding
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
64% 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)
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, 98% coverage: 6:300/300 of query aligns to 9:310/322 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 ; 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
- 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 ; 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)
44% identity, 98% coverage: 6:300/300 of query aligns to 7:308/320 of 2isqA
- active site: K44 (= K47), S267 (= S261)
- binding pyridoxal-5'-phosphate: K44 (= K47), N75 (= N77), G177 (≠ A178), G179 (= G180), T180 (= T181), G181 (≠ T182), T183 (= T184), G223 (vs. gap), S267 (= S261), P294 (vs. gap)
- 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)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
45% identity, 97% coverage: 9:298/300 of query aligns to 11:306/310 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)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
43% identity, 98% coverage: 6:300/300 of query aligns to 7:308/320 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 (vs. gap), S295 (≠ D287)
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
42% identity, 98% coverage: 4:298/300 of query aligns to 11:311/329 of 8b9wA
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
43% identity, 98% coverage: 6:298/300 of query aligns to 17:316/323 of 4aecA
- active site: K54 (= K47), S277 (= S261)
- binding pyridoxal-5'-phosphate: K54 (= K47), N85 (= N77), I188 (≠ M179), G189 (= G180), T190 (= T181), G191 (≠ T182), G192 (= G183), T193 (= T184), G233 (vs. gap), S277 (= S261), P304 (≠ C286)
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, 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)
43% 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
- GTGGT 178:182 (≠ GTTGT 180:184) binding
- S266 (= S261) binding
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
43% identity, 96% coverage: 10:298/300 of query aligns to 11:306/309 of 7n2tA
8b9yC Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
41% identity, 98% coverage: 4:298/300 of query aligns to 12:312/330 of 8b9yC
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
43% identity, 96% coverage: 6:293/300 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)
43% 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)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
41% identity, 96% coverage: 10:298/300 of query aligns to 15:310/341 of Q93244
- P75 (≠ A73) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A86) 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 (≠ A178) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G180) 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 (≠ K249) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (≠ A262) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (≠ V285) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
8b9yA Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
41% identity, 98% coverage: 4:298/300 of query aligns to 10:295/313 of 8b9yA
- binding o-acetylserine: T76 (= T74), G78 (= G76), N79 (= N77), T80 (= T78)
- binding pyridoxal-5'-phosphate: V47 (= V46), K48 (= K47), N79 (= N77), G183 (= G180), T184 (= T181), G185 (≠ T182), T187 (= T184), S256 (= S261), P283 (≠ C286), S284 (≠ D287)
- binding alpha-D-ribofuranose: C40 (≠ G39), E41 (≠ N40), N42 (= N41), P43 (= P42), A45 (≠ G44), Y285 (≠ R288)
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
41% identity, 98% coverage: 6:298/300 of query aligns to 15:314/329 of 3vbeC
- active site: K52 (= K47), S81 (= S75), E212 (≠ Q205), S216 (≠ G209), S275 (= S261), P302 (≠ C286)
- binding pyridoxal-5'-phosphate: K52 (= K47), N83 (= N77), M184 (≠ S177), G187 (= G180), S188 (≠ T181), G189 (≠ T182), T191 (= T184), G231 (vs. gap), S275 (= S261), P302 (≠ C286)
3dwgA Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of mycobacterium tuberculosis (see paper)
41% 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)
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)
41% identity, 99% coverage: 3:298/300 of query aligns to 4:306/323 of P9WP53
- N81 (= N77) binding
- 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
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.
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: 10:298/300 of query aligns to 83:378/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
Query Sequence
>HSERO_RS04915 FitnessBrowser__HerbieS:HSERO_RS04915
MSYPTIESTIGNTPLILLPRIGGEEAKRRNNLILGKLEGNNPAGSVKDRAAFSMITRAEA
RGQIKPGDTLIEATSGNTGIALAMVAAMRGYKMILLMPENLSEERRQSMAAYGAKIVLTP
KSGGMEYARDLAEQMQKNGEGLILDQFANPDNPLAHYETTGPEIWRDTKGSITHFVSAMG
TTGTIMGVAQYLKEQNAQVQIVGAQPEEGSSIPGIRKWPEAYLPKIFDRSRVDQIESVSQ
ADAENMARKLAVTEGVFCGISAAGACEVAVRLSHQLENATIVFIVCDRGDRYLSTGVFPA
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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