SitesBLAST
Comparing WP_011799982.1 NCBI__GCF_000015505.1:WP_011799982.1 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)
P0A1E3 Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine sulfhydrylase A; EC 2.5.1.47 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
69% identity, 96% coverage: 1:317/329 of query aligns to 1:316/323 of P0A1E3
- M1 (= M1) modified: Initiator methionine, Removed
- N72 (= N75) binding pyridoxal 5'-phosphate
- S273 (= S274) binding pyridoxal 5'-phosphate
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
69% identity, 96% coverage: 1:317/329 of query aligns to 2:317/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K45), N73 (= N75), V177 (= V178), G178 (= G179), T179 (= T180), G180 (= G181), T182 (= T183), G230 (= G230), S274 (= S274), P301 (= P301)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K45), T70 (= T72), G72 (= G74), N73 (= N75), T74 (= T76), Q144 (= Q145), F145 (= F146), Q229 (= Q229), G230 (= G230), I231 (= I231), A233 (= A233)
P0ABK5 Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine sulfhydrylase A; S-carboxymethylcysteine synthase; Sulfate starvation-induced protein 5; SSI5; EC 2.5.1.47; EC 4.5.1.5 from Escherichia coli (strain K12) (see 5 papers)
69% identity, 96% coverage: 1:317/329 of query aligns to 1:316/323 of P0ABK5
- M1 (= M1) modified: Initiator methionine, Removed
- K42 (= K45) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Still stimulates tRNase activity of CdiA-CT in vitro and in vivo.
1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
68% identity, 96% coverage: 2:317/329 of query aligns to 1:315/322 of 1d6sA
- active site: A41 (≠ K45), G228 (= G230)
- binding methionine: T68 (= T72), N69 (≠ S73), N71 (= N75), T72 (= T76), Q142 (= Q145), F143 (= F146), G176 (= G179), G228 (= G230)
- binding pyridoxal-5'-phosphate: N71 (= N75), G176 (= G179), T177 (= T180), G178 (= G181), T180 (= T183), G228 (= G230), S272 (= S274), P299 (= P301)
1fcjA Crystal structure of oass complexed with chloride and sulfate (see paper)
69% identity, 92% coverage: 2:304/329 of query aligns to 1:302/302 of 1fcjA
- active site: K41 (= K45), G228 (= G230), S272 (= S274)
- binding pyridoxal-5'-phosphate: K41 (= K45), N71 (= N75), V175 (= V178), G176 (= G179), T177 (= T180), G178 (= G181), T180 (= T183), G228 (= G230), S272 (= S274), P299 (= P301)
- binding sulfate ion: G70 (= G74), T72 (= T76), Q142 (= Q145)
5dbhX Crystal structure of o-acetylserine sulfhydrylase from haemophilus influenzae in complex with reaction intermediate alpha-aminoacrylate
67% identity, 95% coverage: 4:315/329 of query aligns to 2:312/312 of 5dbhX
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: K41 (= K45), T68 (= T72), S69 (= S73), N71 (= N75), T72 (= T76), Q142 (= Q145), G176 (= G179), T177 (= T180), G178 (= G181), S180 (≠ T183), G227 (= G230), S271 (= S274), P298 (= P301)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
65% identity, 95% coverage: 4:316/329 of query aligns to 4:309/310 of 5xoqA
- binding : T72 (= T72), S73 (= S73), G74 (= G74), T76 (= T76), M123 (= M123), Q144 (= Q145), R218 (≠ E219), H219 (= H226), Q222 (= Q229), G223 (= G230), A226 (= A233)
1y7lA O-acetylserine sulfhydrylase complex (see paper)
67% identity, 94% coverage: 4:313/329 of query aligns to 2:310/310 of 1y7lA
4zu6X Crystal structure of o-acetylserine sulfhydrylase from haemophilus influenzae in complex with pre-reactive o-acetyl serine, alpha- aminoacrylate reaction intermediate and peptide inhibitor at the resolution of 2.25a
66% identity, 94% coverage: 4:313/329 of query aligns to 3:309/309 of 4zu6X
- binding o-acetylserine: T69 (= T72), S70 (= S73), T73 (= T76), Q141 (= Q145), G175 (= G179), G226 (= G230)
- binding pyridoxal-5'-phosphate: K42 (= K45), N72 (= N75), V174 (= V178), G175 (= G179), T176 (= T180), G177 (= G181), G178 (= G182), S179 (≠ T183), G226 (= G230), S270 (= S274), P297 (= P301)
- binding : S70 (= S73), T95 (= T98), M96 (= M99), K118 (= K121), G119 (= G122), P221 (= P225), H222 (= H226), K223 (= K227), A229 (= A233)
4oreX Cyrstal structure of o-acetylserine sulfhydrylase ternary complex from haemophilus influenzae at 2.2 a
66% identity, 94% coverage: 4:313/329 of query aligns to 2:308/308 of 4oreX
- binding o-acetylserine: K115 (= K121), G116 (= G122), M117 (= M123)
- binding : K41 (= K45), T68 (= T72), G69 (= G74), T71 (= T76), P91 (= P96), M117 (= M123), F141 (= F146), G219 (= G224), P220 (= P225), H221 (= H226), G225 (= G230), A228 (= A233)
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)
61% identity, 96% coverage: 3:318/329 of query aligns to 2:310/310 of P9WP55
- K44 (= K45) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N75) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 179:183) binding pyridoxal 5'-phosphate
- S266 (= S274) 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)
62% identity, 95% coverage: 3:313/329 of query aligns to 2:305/306 of 2q3dA
- active site: K44 (= K45), S266 (= S274), P293 (= P301)
- 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 (= Q145), V177 (= V178), G178 (= G179), T179 (= T180), G180 (= G181), T182 (= T183), G222 (= G230), I223 (= I231), S266 (= S274), P293 (= P301), D294 (= D302)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
62% identity, 93% coverage: 3:308/329 of query aligns to 2:300/300 of 3zeiA
- active site: K44 (= K45), S266 (= S274), P293 (= P301)
- 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 (= I127), Q144 (= Q145), F145 (= F146), K215 (≠ E220), G222 (= G230), A225 (= A233), F227 (= F235)
- binding pyridoxal-5'-phosphate: K44 (= K45), N74 (= N75), V177 (= V178), G178 (= G179), T179 (= T180), G180 (= G181), T182 (= T183), G222 (= G230), S266 (= S274), P293 (= P301), D294 (= D302)
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)
62% identity, 93% coverage: 3:308/329 of query aligns to 2:300/300 of 2q3cA
- active site: K44 (= K45), S266 (= S274), P293 (= P301)
- binding : T71 (= T72), S72 (= S73), G73 (= G74), T75 (= T76), M122 (= M123), Q144 (= Q145), K215 (≠ E220), G222 (= G230), A225 (= A233)
2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
56% identity, 95% coverage: 2:314/329 of query aligns to 1:307/320 of 2isqA
- active site: K44 (= K45), S267 (= S274)
- binding pyridoxal-5'-phosphate: K44 (= K45), N75 (= N75), G177 (= G177), G179 (= G179), T180 (= T180), G181 (= G181), T183 (= T183), G223 (= G230), S267 (= S274), P294 (= P301)
- binding : T72 (= T72), S73 (= S73), G74 (= G74), T76 (= T76), G122 (= G122), M123 (= M123), K124 (= K124), G217 (= G224), P218 (= P225), H219 (= H226), Q222 (= Q229), G223 (= G230)
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)
56% identity, 95% coverage: 2:314/329 of query aligns to 3:309/322 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 pyridoxal 5'-phosphate; 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 (= Q145) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H155) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (= G160) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 179:183) binding pyridoxal 5'-phosphate
- T182 (= T180) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T183) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (= K222) mutation to A: Impaired interaction with SAT1.
- H221 (= H226) mutation to A: Impaired interaction with SAT1.
- K222 (= K227) mutation to A: Impaired interaction with SAT1.
- S269 (= S274) binding pyridoxal 5'-phosphate; mutation to A: Strong reduction of cysteine synthase activity.; mutation to T: Reduction of cysteine synthase activity.
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
56% identity, 95% coverage: 2:314/329 of query aligns to 1:307/320 of 1z7yA
- active site: A44 (≠ K45), S267 (= S274)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G74), N75 (= N75), T76 (= T76), Q145 (= Q145), I178 (≠ V178), G179 (= G179), T180 (= T180), G181 (= G181), T183 (= T183), G223 (= G230), S267 (= S274), P294 (= P301), S295 (≠ D302)
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
56% identity, 96% coverage: 2:316/329 of query aligns to 1:309/309 of 7n2tA
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)
56% identity, 95% coverage: 6:316/329 of query aligns to 76:381/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
54% identity, 95% coverage: 4:316/329 of query aligns to 3:311/318 of 4lmaA
Query Sequence
>WP_011799982.1 NCBI__GCF_000015505.1:WP_011799982.1
MSTIYADNSQSIGRTPLIQLRRITDGAHATVLAKIEGRNPAASVKCRIGAALIWDAEQRG
LLGAGKEIVEPTSGNTGIALAFVAAARGIPITLTMPETMSIERRKLLLAYGAKLVLTEGA
KGMKGAIAKAEEIAASDPKYVLLQQFKNPANPAIHEATTGPEIWQDTDGGIDIFISGVGT
GGTITGVSRYLKKTQGKAIISVAVEPSASPILTQHRAGEELKAGPHKIQGIGAGFVPEVL
DLSLVDAIEQVSNEEAIDHARRLAREEGILAGISGGAAVAAAVRWAKKPESAGKTLVVII
PDSGERYLSSVLFEGIFDASGAAVNQELA
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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