SitesBLAST
Comparing WP_011371790.1 NCBI__GCF_000012965.1:WP_011371790.1 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)
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)
55% identity, 99% coverage: 1:303/307 of query aligns to 1:305/310 of P9WP55
- K44 (= K42) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N72) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (≠ GTGGS 176:180) binding pyridoxal 5'-phosphate
- S266 (= S264) 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)
55% identity, 99% coverage: 1:303/307 of query aligns to 1:305/306 of 2q3dA
- active site: K44 (= K42), S266 (= S264), P293 (≠ C291)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K42), T71 (= T69), S72 (= S70), N74 (= N72), T75 (= T73), Q144 (= Q142), V177 (= V175), G178 (= G176), T179 (= T177), G180 (= G178), T182 (≠ S180), G222 (= G220), I223 (= I221), S266 (= S264), P293 (≠ C291), D294 (= D292)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
56% identity, 97% coverage: 1:298/307 of query aligns to 1:300/300 of 3zeiA
- active site: K44 (= K42), S266 (= S264), P293 (≠ C291)
- 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 (= T69), S72 (= S70), I126 (≠ V124), Q144 (= Q142), F145 (= F143), K215 (≠ A213), G222 (= G220), A225 (= A223), F227 (= F225)
- binding pyridoxal-5'-phosphate: K44 (= K42), N74 (= N72), V177 (= V175), G178 (= G176), T179 (= T177), G180 (= G178), T182 (≠ S180), G222 (= G220), S266 (= S264), P293 (≠ C291), D294 (= D292)
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)
56% identity, 97% coverage: 1:298/307 of query aligns to 1:300/300 of 2q3cA
- active site: K44 (= K42), S266 (= S264), P293 (≠ C291)
- binding : T71 (= T69), S72 (= S70), G73 (= G71), T75 (= T73), M122 (= M120), Q144 (= Q142), K215 (≠ A213), G222 (= G220), A225 (= A223)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
56% identity, 100% coverage: 1:307/307 of query aligns to 1:312/318 of 4lmaA
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
53% identity, 99% coverage: 1:303/307 of query aligns to 11:316/323 of 4aecA
- active site: K54 (= K42), S277 (= S264)
- binding pyridoxal-5'-phosphate: K54 (= K42), N85 (= N72), I188 (≠ V175), G189 (= G176), T190 (= T177), G191 (= G178), G192 (= G179), T193 (≠ S180), G233 (= G220), S277 (= S264), P304 (≠ C291)
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
55% identity, 98% coverage: 4:304/307 of query aligns to 4:307/309 of 7n2tA
2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
53% identity, 99% coverage: 2:304/307 of query aligns to 2:307/320 of 2isqA
- active site: K44 (= K42), S267 (= S264)
- binding pyridoxal-5'-phosphate: K44 (= K42), N75 (= N72), G177 (= G174), G179 (= G176), T180 (= T177), G181 (= G178), T183 (≠ S180), G223 (= G220), S267 (= S264), P294 (≠ C291)
- binding : T72 (= T69), S73 (= S70), G74 (= G71), T76 (= T73), G122 (= G119), M123 (= M120), K124 (≠ M121), G217 (= G214), P218 (= P215), H219 (= H216), Q222 (= Q219), G223 (= G220)
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)
53% identity, 99% coverage: 2:304/307 of query aligns to 4:309/322 of P47998
- K46 (= K42) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T69) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S70) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N72) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T73) 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 (≠ A157) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (≠ GTGGS 176:180) binding pyridoxal 5'-phosphate
- T182 (= T177) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (≠ S180) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ E212) mutation to A: Impaired interaction with SAT1.
- H221 (= H216) mutation to A: Impaired interaction with SAT1.
- K222 (≠ E217) mutation to A: Impaired interaction with SAT1.
- S269 (= S264) binding pyridoxal 5'-phosphate; mutation to A: Strong reduction of cysteine synthase activity.; mutation to T: Reduction of cysteine synthase activity.
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
52% identity, 99% coverage: 1:305/307 of query aligns to 1:310/310 of 4lmbA
- active site: K46 (= K42), S269 (= S264)
- binding cysteine: K46 (= K42), T74 (= T69), S75 (= S70), N77 (= N72), T78 (= T73), M101 (= M96), M125 (= M120), M125 (= M120), Q147 (= Q142), F148 (= F143), Q224 (= Q219), G225 (= G220), G225 (= G220), I226 (= I221), A228 (= A223)
- binding pyridoxal-5'-phosphate: K46 (= K42), N77 (= N72), V180 (= V175), G181 (= G176), T182 (= T177), G183 (= G178), T185 (≠ S180), G225 (= G220), S269 (= S264), P296 (≠ C291)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
52% identity, 99% coverage: 2:304/307 of query aligns to 2:307/320 of 1z7yA
- active site: A44 (≠ K42), S267 (= S264)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G71), N75 (= N72), T76 (= T73), Q145 (= Q142), I178 (≠ V175), G179 (= G176), T180 (= T177), G181 (= G178), T183 (≠ S180), G223 (= G220), S267 (= S264), P294 (≠ C291), S295 (≠ D292)
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)
54% identity, 98% coverage: 4:303/307 of query aligns to 76:378/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
51% identity, 98% coverage: 5:305/307 of query aligns to 13:316/329 of 3vbeC
- active site: K52 (= K42), S81 (= S70), E212 (= E201), S216 (= S205), S275 (= S264), P302 (≠ C291)
- binding pyridoxal-5'-phosphate: K52 (= K42), N83 (= N72), M184 (≠ L173), G187 (= G176), S188 (≠ T177), G189 (= G178), T191 (≠ S180), G231 (= G220), S275 (= S264), P302 (≠ C291)
3vc3A Crystal structure of beta-cyanoalanine synthase k95a mutant in soybean (see paper)
51% identity, 98% coverage: 5:305/307 of query aligns to 6:309/322 of 3vc3A
- active site: A45 (≠ K42), S268 (= S264), P295 (≠ C291)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-cysteine: T73 (= T69), S74 (= S70), N76 (= N72), M77 (≠ T73), Q146 (= Q142), M177 (≠ L173), G180 (= G176), S181 (≠ T177), G182 (= G178), T184 (≠ S180), G224 (= G220), S268 (= S264), P295 (≠ C291)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
52% identity, 98% coverage: 5:305/307 of query aligns to 9:312/341 of Q93244
- P75 (= P68) mutation to L: In n5537; severe loss of protein stability.
- A88 (≠ C81) mutation to V: In n5522; severe loss of protein stability.
- S144 (≠ A137) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (= G174) 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 (= G222) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (≠ E252) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S265) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (= T288) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
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)
49% identity, 97% coverage: 7:305/307 of query aligns to 32:333/347 of Q9FS29
- E157 (= E129) mutation E->N,Q: No effect on catalytic activities.
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
51% identity, 99% coverage: 1:304/307 of query aligns to 2:307/310 of 5xoqA
- binding : T72 (= T69), S73 (= S70), G74 (= G71), T76 (= T73), M123 (= M120), Q144 (= Q142), R218 (≠ P215), H219 (= H216), Q222 (= Q219), G223 (= G220), A226 (= A223)
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
50% identity, 98% coverage: 4:303/307 of query aligns to 10:311/329 of 8b9wA
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)
50% identity, 95% coverage: 11:303/307 of query aligns to 12:312/323 of P0ABK5
- K42 (= K42) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Still stimulates tRNase activity of CdiA-CT in vitro and in vivo.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
49% identity, 95% coverage: 11:303/307 of query aligns to 13:313/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K42), N73 (= N72), V177 (= V175), G178 (= G176), T179 (= T177), G180 (= G178), T182 (≠ S180), G230 (= G220), S274 (= S264), P301 (≠ C291)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K42), T70 (= T69), G72 (= G71), N73 (= N72), T74 (= T73), Q144 (= Q142), F145 (= F143), Q229 (= Q219), G230 (= G220), I231 (= I221), A233 (= A223)
Query Sequence
>WP_011371790.1 NCBI__GCF_000012965.1:WP_011371790.1
MKYAKNVTELIGNTPLVRINIASQNALVLGKCEFMNPTHSIKDRIGKYMIQEALTQGLIT
KNTTVIEPTSGNTGIALASVCASLGIKLILTMPSSMSKERIQLLRALGARVVLTDAKQGM
MGAVREAKELCSQHSEALMLQQFSNRANPEIHRKTTALEIIRDTQGKVDILVLGVGTGGS
ITGVGEVLKKHNPNIKIIAVEPENSPVLSGGEAGPHEIQGIGAGFIPEILNTEIYDEIIR
VSGEDAINCSREMAKKEGLLVGISSGANVFASTQAAKRQENRGKTIVTILCDTAERYLSC
GLYDEDE
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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