SitesBLAST
Comparing WP_014449906.1 NCBI__GCF_000284315.1:WP_014449906.1 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)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
52% identity, 95% coverage: 16:312/312 of query aligns to 12:309/310 of 5xoqA
- binding : T72 (= T76), S73 (= S77), G74 (= G78), T76 (= T80), M123 (= M127), Q144 (= Q149), R218 (≠ P222), H219 (= H223), Q222 (= Q226), G223 (= G227), A226 (= A230)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
49% identity, 97% coverage: 11:312/312 of query aligns to 10:313/341 of Q93244
- P75 (≠ A75) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A88) mutation to V: In n5522; severe loss of protein stability.
- S144 (≠ L144) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (= G181) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G183) mutation to R: In n5515; severe loss of protein stability.
- G229 (= G229) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (= R259) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S272) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (= T294) 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)
47% identity, 96% coverage: 15:312/312 of query aligns to 10:308/310 of P9WP55
- K44 (= K49) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N79) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 183:187) binding pyridoxal 5'-phosphate
- S266 (≠ T271) binding pyridoxal 5'-phosphate
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)
48% identity, 93% coverage: 15:305/312 of query aligns to 10:301/306 of 2q3dA
- active site: K44 (= K49), S266 (≠ T271), P293 (≠ D298)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K49), T71 (= T76), S72 (= S77), N74 (= N79), T75 (= T80), Q144 (= Q149), V177 (= V182), G178 (= G183), T179 (= T184), G180 (= G185), T182 (= T187), G222 (= G227), I223 (= I228), S266 (≠ T271), P293 (≠ D298), D294 (≠ S299)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
48% identity, 93% coverage: 15:304/312 of query aligns to 10:300/300 of 3zeiA
- active site: K44 (= K49), S266 (≠ T271), P293 (≠ D298)
- 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 (= T76), S72 (= S77), I126 (= I131), Q144 (= Q149), F145 (= F150), K215 (≠ P220), G222 (= G227), A225 (= A230), F227 (= F232)
- binding pyridoxal-5'-phosphate: K44 (= K49), N74 (= N79), V177 (= V182), G178 (= G183), T179 (= T184), G180 (= G185), T182 (= T187), G222 (= G227), S266 (≠ T271), P293 (≠ D298), D294 (≠ S299)
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)
48% identity, 93% coverage: 15:304/312 of query aligns to 10:300/300 of 2q3cA
- active site: K44 (= K49), S266 (≠ T271), P293 (≠ D298)
- binding : T71 (= T76), S72 (= S77), G73 (= G78), T75 (= T80), M122 (= M127), Q144 (= Q149), K215 (≠ P220), G222 (= G227), A225 (= A230)
6ahiB Crystal structure of o-acetylserine dependent cystathionine beta- synthase from helicobacter pylori. (see paper)
42% identity, 95% coverage: 16:310/312 of query aligns to 11:306/306 of 6ahiB
5xemA Crystal structure of a hydrogen sulfide-producing enzyme (fn1220) from fusobacterium nucleatum in complex with l-lanthionine-plp schiff base
45% identity, 94% coverage: 13:305/312 of query aligns to 7:301/302 of 5xemA
- binding (2R)-2-azanyl-3-[(2R)-2-azanyl-3-oxidanyl-3-oxidanylidene-propyl]sulfanyl-propanoic acid: K42 (= K49), T69 (= T76), S70 (= S77), N72 (= N79), T73 (= T80), M120 (= M127), Q142 (= Q149), G176 (= G183), T177 (= T184), G220 (= G227), M221 (≠ I228), G222 (= G229), S224 (vs. gap)
- binding calcium ion: L300 (≠ F304), S301 (= S305)
- binding pyridoxal-5'-phosphate: K42 (= K49), N72 (= N79), T175 (≠ V182), G176 (= G183), T177 (= T184), G178 (= G185), S180 (≠ T187), G220 (= G227), S266 (≠ T271), T293 (≠ C297), D294 (= D298)
Sites not aligning to the query:
5xenA Crystal structure of a hydrogen sulfide-producing enzyme (fn1220) from fusobacterium nucleatum in complex with l-serine-plp schiff base
44% identity, 94% coverage: 13:304/312 of query aligns to 7:300/300 of 5xenA
- binding pyridoxal-5'-phosphate: K42 (= K49), K42 (= K49), N72 (= N79), N72 (= N79), T175 (≠ V182), T175 (≠ V182), G176 (= G183), G176 (= G183), T177 (= T184), T177 (= T184), G178 (= G185), G178 (= G185), S180 (≠ T187), S180 (≠ T187), G220 (= G227), G220 (= G227), S266 (≠ T271), S266 (≠ T271), T293 (≠ C297), T293 (≠ C297), D294 (= D298), D294 (= D298)
- binding serine: K42 (= K49), T69 (= T76), S70 (= S77), N72 (= N79), T73 (= T80), Q142 (= Q149)
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
46% identity, 99% coverage: 5:312/312 of query aligns to 6:314/329 of 8b9wA
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)
46% identity, 96% coverage: 8:305/312 of query aligns to 5:304/322 of P47998
- K46 (= K49) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T76) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S77) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N79) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T80) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q149) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H159) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (= G164) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 183:187) binding pyridoxal 5'-phosphate
- T182 (= T184) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T187) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ S219) mutation to A: Impaired interaction with SAT1.
- H221 (= H223) mutation to A: Impaired interaction with SAT1.
- K222 (≠ R224) mutation to A: Impaired interaction with SAT1.
- S269 (≠ T271) binding pyridoxal 5'-phosphate; 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)
46% identity, 96% coverage: 8:305/312 of query aligns to 3:302/320 of 2isqA
- active site: K44 (= K49), S267 (≠ T271)
- binding pyridoxal-5'-phosphate: K44 (= K49), N75 (= N79), G177 (= G181), G179 (= G183), T180 (= T184), G181 (= G185), T183 (= T187), G223 (= G227), S267 (≠ T271), P294 (≠ D298)
- binding : T72 (= T76), S73 (= S77), G74 (= G78), T76 (= T80), G122 (= G126), M123 (= M127), K124 (≠ V128), G217 (= G221), P218 (= P222), H219 (= H223), Q222 (= Q226), G223 (= G227)
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
49% identity, 94% coverage: 16:309/312 of query aligns to 7:301/302 of 2efyA
- active site: K40 (= K49), S70 (= S77), E200 (= E208), S204 (= S212), S263 (≠ T271)
- binding 5-oxohexanoic acid: T69 (= T76), G71 (= G78), T73 (= T80), Q141 (= Q149), G175 (= G183), G219 (= G227), M220 (≠ I228), P222 (≠ A230)
- binding pyridoxal-5'-phosphate: K40 (= K49), N72 (= N79), Y172 (≠ A180), G175 (= G183), T176 (= T184), G177 (= G185), T179 (= T187), G219 (= G227), S263 (≠ T271), P289 (≠ C297), D290 (= D298)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
49% identity, 94% coverage: 16:309/312 of query aligns to 7:301/302 of 2ecqA
- active site: K40 (= K49), S70 (= S77), E200 (= E208), S204 (= S212), S263 (≠ T271)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K49), G71 (= G78), T73 (= T80), Q141 (= Q149), G219 (= G227)
- binding pyridoxal-5'-phosphate: K40 (= K49), N72 (= N79), Y172 (≠ A180), G173 (= G181), G175 (= G183), T176 (= T184), T179 (= T187), G219 (= G227), S263 (≠ T271), P289 (≠ C297)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
49% identity, 94% coverage: 16:309/312 of query aligns to 7:301/302 of 2ecoA
- active site: K40 (= K49), S70 (= S77), E200 (= E208), S204 (= S212), S263 (≠ T271)
- binding 4-methyl valeric acid: K40 (= K49), T69 (= T76), G71 (= G78), T73 (= T80), Q141 (= Q149), G175 (= G183), T176 (= T184), G219 (= G227)
- binding pyridoxal-5'-phosphate: K40 (= K49), N72 (= N79), Y172 (≠ A180), G175 (= G183), T176 (= T184), T179 (= T187), G219 (= G227), S263 (≠ T271), P289 (≠ C297), D290 (= D298)
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)
43% identity, 99% coverage: 4:312/312 of query aligns to 24:334/347 of Q9FS29
- E157 (= E136) mutation E->N,Q: No effect on catalytic activities.
8b9yC Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
46% identity, 99% coverage: 4:312/312 of query aligns to 6:315/330 of 8b9yC
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
45% identity, 96% coverage: 8:305/312 of query aligns to 3:302/320 of 1z7yA
- active site: A44 (≠ K49), S267 (≠ T271)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G78), N75 (= N79), T76 (= T80), Q145 (= Q149), I178 (≠ V182), G179 (= G183), T180 (= T184), G181 (= G185), T183 (= T187), G223 (= G227), S267 (≠ T271), P294 (≠ D298), S295 (= S299)
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
45% identity, 93% coverage: 15:305/312 of query aligns to 18:310/329 of 3vbeC
- active site: K52 (= K49), S81 (= S77), E212 (= E208), S216 (= S212), S275 (≠ T271), P302 (≠ C297)
- binding pyridoxal-5'-phosphate: K52 (= K49), N83 (= N79), M184 (≠ A180), G187 (= G183), S188 (≠ T184), G189 (= G185), T191 (= T187), G231 (= G227), S275 (≠ T271), P302 (≠ C297)
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
44% identity, 93% coverage: 16:305/312 of query aligns to 8:288/294 of 2bhtA
- active site: K41 (= K49), S69 (= S77), Q199 (≠ E208), G203 (≠ S212), S255 (≠ T271), C280 (= C297)
- binding pyridoxal-5'-phosphate: K41 (= K49), N71 (= N79), M173 (≠ V182), G174 (= G183), T175 (= T184), T176 (≠ G185), T178 (= T187), G208 (= G217), S255 (≠ T271), C280 (= C297)
Query Sequence
>WP_014449906.1 NCBI__GCF_000284315.1:WP_014449906.1
MTSPEGDVIRNPLALIGNTPLLPLSKVTAGLDRTVWVKLESRNLGGSVKDRPALFMIEQA
ERDGRLGKDGRIVEATSGNTGIALAQIAVLKGYAITIVMPEGVSGERVSHLKALGAEVLL
TPSREGMVGAIGKATEMEKSEKGLFMPRQFENPSNPESHYRTTGPEIFRQLGRVPDGFVA
GVGTGGTISGVGRYLREKKRDLKIWALEPAASPVLSGGSPGPHRIQGIGAGFEPRTFNRS
VVDRIEKISDREAIDMARRLSQEEGIMAGITSGANVVGALRLAGELPPGSHVVTIVCDSF
ERYFSMEKYLNL
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