SitesBLAST
Comparing BWI76_RS20685 FitnessBrowser__Koxy:BWI76_RS20685 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)
91% identity, 100% coverage: 1:303/303 of query aligns to 1:303/303 of P16703
- N71 (= N71) binding
- S255 (= S255) binding
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
90% identity, 97% coverage: 1:294/303 of query aligns to 1:294/294 of 2bhtA
- active site: K41 (= K41), S69 (= S69), Q199 (= Q199), G203 (= G203), S255 (= S255), C280 (= C280)
- binding pyridoxal-5'-phosphate: K41 (= K41), N71 (= N71), M173 (= M173), G174 (= G174), T175 (= T175), T176 (= T176), T178 (= T178), G208 (= G208), S255 (= S255), C280 (= C280)
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)
45% identity, 94% coverage: 8:292/303 of query aligns to 13:308/322 of P47998
- K46 (= K41) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T68) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S69) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N71) binding ; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T72) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q140) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H150) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (= G155) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (≠ GTTGT 174:178) binding
- T182 (= T175) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T178) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ R210) mutation to A: Impaired interaction with SAT1.
- H221 (vs. gap) mutation to A: Impaired interaction with SAT1.
- K222 (vs. gap) mutation to A: Impaired interaction with SAT1.
- S269 (= S255) 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)
45% identity, 94% coverage: 8:292/303 of query aligns to 11:306/320 of 2isqA
- active site: K44 (= K41), S267 (= S255)
- binding pyridoxal-5'-phosphate: K44 (= K41), N75 (= N71), G177 (≠ S172), G179 (= G174), T180 (= T175), G181 (≠ T176), T183 (= T178), G223 (vs. gap), S267 (= S255), P294 (≠ C280)
- binding : T72 (= T68), S73 (= S69), G74 (= G70), T76 (= T72), G122 (= G118), M123 (= M119), K124 (≠ E120), G217 (≠ W212), P218 (= P213), H219 (vs. gap), Q222 (vs. gap), G223 (vs. gap)
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
44% identity, 95% coverage: 4:292/303 of query aligns to 3:301/302 of 2efyA
- active site: K40 (= K41), S70 (= S69), E200 (≠ Q199), S204 (≠ G203), S263 (= S255)
- binding 5-oxohexanoic acid: T69 (= T68), G71 (= G70), T73 (= T72), Q141 (= Q140), G175 (= G174), G219 (≠ R211), M220 (≠ W212), P222 (≠ A214)
- binding pyridoxal-5'-phosphate: K40 (= K41), N72 (= N71), Y172 (≠ S171), G175 (= G174), T176 (= T175), G177 (≠ T176), T179 (= T178), G219 (≠ R211), S263 (= S255), P289 (≠ C280), D290 (= D281)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
44% identity, 95% coverage: 4:292/303 of query aligns to 3:301/302 of 2ecqA
- active site: K40 (= K41), S70 (= S69), E200 (≠ Q199), S204 (≠ G203), S263 (= S255)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K41), G71 (= G70), T73 (= T72), Q141 (= Q140), G219 (≠ R211)
- binding pyridoxal-5'-phosphate: K40 (= K41), N72 (= N71), Y172 (≠ S171), G173 (≠ S172), G175 (= G174), T176 (= T175), T179 (= T178), G219 (≠ R211), S263 (= S255), P289 (≠ C280)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
44% identity, 95% coverage: 4:292/303 of query aligns to 3:301/302 of 2ecoA
- active site: K40 (= K41), S70 (= S69), E200 (≠ Q199), S204 (≠ G203), S263 (= S255)
- binding 4-methyl valeric acid: K40 (= K41), T69 (= T68), G71 (= G70), T73 (= T72), Q141 (= Q140), G175 (= G174), T176 (= T175), G219 (≠ R211)
- binding pyridoxal-5'-phosphate: K40 (= K41), N72 (= N71), Y172 (≠ S171), G175 (= G174), T176 (= T175), T179 (= T178), G219 (≠ R211), S263 (= S255), P289 (≠ C280), D290 (= D281)
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)
44% identity, 95% coverage: 8:294/303 of query aligns to 11:307/310 of P9WP55
- K44 (= K41) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N71) binding
- GTGGT 178:182 (≠ GTTGT 174:178) binding
- S266 (= S255) binding
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
45% identity, 94% coverage: 8:292/303 of query aligns to 11:306/309 of 7n2tA
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
45% identity, 94% coverage: 8:292/303 of query aligns to 11:306/320 of 1z7yA
- active site: A44 (≠ K41), S267 (= S255)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G70), N75 (= N71), T76 (= T72), Q145 (= Q140), I178 (≠ M173), G179 (= G174), T180 (= T175), G181 (≠ T176), T183 (= T178), G223 (vs. gap), S267 (= S255), P294 (≠ C280), S295 (≠ D281)
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)
44% identity, 94% coverage: 8:293/303 of query aligns to 11:306/306 of 2q3dA
- active site: K44 (= K41), S266 (= S255), P293 (≠ C280)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K41), T71 (= T68), S72 (= S69), N74 (= N71), T75 (= T72), Q144 (= Q140), V177 (≠ M173), G178 (= G174), T179 (= T175), G180 (≠ T176), T182 (= T178), G222 (vs. gap), I223 (vs. gap), S266 (= S255), P293 (≠ C280), D294 (= D281)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
43% identity, 94% coverage: 7:292/303 of query aligns to 11:306/310 of 5xoqA
- binding : T72 (= T68), S73 (= S69), G74 (= G70), T76 (= T72), M123 (= M119), Q144 (= Q140), R218 (vs. gap), H219 (vs. gap), Q222 (≠ R210), G223 (≠ R211), A226 (= A214)
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
42% identity, 95% coverage: 8:294/303 of query aligns to 19:316/329 of 3vbeC
- active site: K52 (= K41), S81 (= S69), E212 (≠ Q199), S216 (≠ G203), S275 (= S255), P302 (≠ C280)
- binding pyridoxal-5'-phosphate: K52 (= K41), N83 (= N71), M184 (≠ S171), G187 (= G174), S188 (≠ T175), G189 (≠ T176), T191 (= T178), G231 (vs. gap), S275 (= S255), P302 (≠ C280)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
44% identity, 92% coverage: 8:287/303 of query aligns to 11:300/300 of 3zeiA
- active site: K44 (= K41), S266 (= S255), P293 (≠ C280)
- 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 (= T68), S72 (= S69), I126 (≠ R123), Q144 (= Q140), F145 (= F141), K215 (≠ R211), G222 (vs. gap), A225 (= A214), F227 (≠ Y216)
- binding pyridoxal-5'-phosphate: K44 (= K41), N74 (= N71), V177 (≠ M173), G178 (= G174), T179 (= T175), G180 (≠ T176), T182 (= T178), G222 (vs. gap), S266 (= S255), P293 (≠ C280), D294 (= D281)
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)
44% identity, 92% coverage: 8:287/303 of query aligns to 11:300/300 of 2q3cA
- active site: K44 (= K41), S266 (= S255), P293 (≠ C280)
- binding : T71 (= T68), S72 (= S69), G73 (= G70), T75 (= T72), M122 (= M119), Q144 (= Q140), K215 (≠ R211), G222 (vs. gap), A225 (= A214)
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
42% identity, 96% coverage: 3:293/303 of query aligns to 12:312/329 of 8b9wA
3vc3A Crystal structure of beta-cyanoalanine synthase k95a mutant in soybean (see paper)
41% identity, 95% coverage: 8:294/303 of query aligns to 12:309/322 of 3vc3A
- active site: A45 (≠ K41), S268 (= S255), P295 (≠ C280)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-cysteine: T73 (= T68), S74 (= S69), N76 (= N71), M77 (≠ T72), Q146 (= Q140), M177 (≠ S171), G180 (= G174), S181 (≠ T175), G182 (≠ T176), T184 (= T178), G224 (vs. gap), S268 (= S255), P295 (≠ C280)
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
43% identity, 94% coverage: 8:292/303 of query aligns to 21:316/323 of 4aecA
- active site: K54 (= K41), S277 (= S255)
- binding pyridoxal-5'-phosphate: K54 (= K41), N85 (= N71), I188 (≠ M173), G189 (= G174), T190 (= T175), G191 (≠ T176), G192 (= G177), T193 (= T178), G233 (vs. gap), S277 (= S255), P304 (≠ C280)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
42% identity, 94% coverage: 8:292/303 of query aligns to 15:310/341 of Q93244
- P75 (≠ A67) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A80) mutation to V: In n5522; severe loss of protein stability.
- S144 (≠ K136) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (≠ S172) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G174) 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 (≠ M243) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S256) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (≠ A277) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
3bm5A Crystal structure of o-acetyl-serine sulfhydrylase from entamoeba histolytica in complex with cysteine (see paper)
42% identity, 96% coverage: 2:292/303 of query aligns to 15:318/338 of 3bm5A
Query Sequence
>BWI76_RS20685 FitnessBrowser__Koxy:BWI76_RS20685
MNTLEYTIGNTPLVKLQRMGPDNGSEIWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIKP
GDVLIEATSGNTGIALAMIAALKGYQMKLLMPDNMSQERRAAMRAYGAELILVTKEQGME
GARDLALAMAQRGEGKLLDQFNNPDNPYAHYTTTGPEIWRQTDGRITHFVSSMGTTGTIT
GVSRFLREQDKAVSIVGLQPEEGSSIPGIRRWPAEYMPGIFNAQLVDVVLDIHQQDAENT
MRMLAVKEGIFCGVSSGGAVVGALRVARENPGAVVVAIVCDRGDRYLSTGVFGEEHFTQG
AGI
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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