SitesBLAST
Comparing WP_013136878.1 NCBI__GCF_000092245.1:WP_013136878.1 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)
56% identity, 98% coverage: 1:304/309 of query aligns to 1:305/310 of P9WP55
- K44 (= K43) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N73) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (≠ GTGGS 177:181) binding pyridoxal 5'-phosphate
- S266 (= S265) 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)
56% identity, 98% coverage: 1:304/309 of query aligns to 1:305/306 of 2q3dA
- active site: K44 (= K43), S266 (= S265), P293 (≠ C292)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K43), T71 (= T70), S72 (= S71), N74 (= N73), T75 (= T74), Q144 (= Q143), V177 (≠ I176), G178 (= G177), T179 (= T178), G180 (= G179), T182 (≠ S181), G222 (= G221), I223 (= I222), S266 (= S265), P293 (≠ C292), D294 (= D293)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
57% identity, 100% coverage: 1:309/309 of query aligns to 1:313/318 of 4lmaA
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
56% identity, 97% coverage: 1:299/309 of query aligns to 1:300/300 of 3zeiA
- active site: K44 (= K43), S266 (= S265), P293 (≠ C292)
- 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 (= T70), S72 (= S71), I126 (≠ V125), Q144 (= Q143), F145 (= F144), K215 (≠ P214), G222 (= G221), A225 (= A224), F227 (= F226)
- binding pyridoxal-5'-phosphate: K44 (= K43), N74 (= N73), V177 (≠ I176), G178 (= G177), T179 (= T178), G180 (= G179), T182 (≠ S181), G222 (= G221), S266 (= S265), P293 (≠ C292), D294 (= D293)
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: 1:299/309 of query aligns to 1:300/300 of 2q3cA
- active site: K44 (= K43), S266 (= S265), P293 (≠ C292)
- binding : T71 (= T70), S72 (= S71), G73 (= G72), T75 (= T74), M122 (= M121), Q144 (= Q143), K215 (≠ P214), G222 (= G221), A225 (= A224)
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
56% identity, 98% coverage: 4:305/309 of query aligns to 4:307/309 of 7n2tA
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
54% identity, 99% coverage: 1:305/309 of query aligns to 11:317/323 of 4aecA
- active site: K54 (= K43), S277 (= S265)
- binding pyridoxal-5'-phosphate: K54 (= K43), N85 (= N73), I188 (= I176), G189 (= G177), T190 (= T178), G191 (= G179), G192 (= G180), T193 (≠ S181), G233 (= G221), S277 (= S265), P304 (≠ C292)
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
53% identity, 99% coverage: 1:305/309 of query aligns to 1:309/310 of 4lmbA
- active site: K46 (= K43), S269 (= S265)
- binding cysteine: K46 (= K43), T74 (= T70), S75 (= S71), N77 (= N73), T78 (= T74), M101 (= M97), M125 (= M121), M125 (= M121), Q147 (= Q143), F148 (= F144), Q224 (= Q220), G225 (= G221), G225 (= G221), I226 (= I222), A228 (= A224)
- binding pyridoxal-5'-phosphate: K46 (= K43), N77 (= N73), V180 (≠ I176), G181 (= G177), T182 (= T178), G183 (= G179), T185 (≠ S181), G225 (= G221), S269 (= S265), P296 (≠ C292)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
57% identity, 95% coverage: 10:304/309 of query aligns to 14:310/341 of Q93244
- P75 (= P69) mutation to L: In n5537; severe loss of protein stability.
- A88 (≠ C82) mutation to V: In n5522; severe loss of protein stability.
- S144 (= S138) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (≠ A175) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G177) mutation to R: In n5515; severe loss of protein stability.
- G229 (= G223) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (≠ N253) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (≠ A266) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (= T289) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
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, 98% coverage: 2:304/309 of query aligns to 4:308/322 of P47998
- K46 (= K43) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T70) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S71) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N73) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T74) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q143) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H153) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (≠ A158) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (≠ GTGGS 177:181) binding pyridoxal 5'-phosphate
- T182 (= T178) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (≠ S181) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ N213) mutation to A: Impaired interaction with SAT1.
- H221 (= H217) mutation to A: Impaired interaction with SAT1.
- K222 (= K218) mutation to A: Impaired interaction with SAT1.
- S269 (= S265) 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)
56% identity, 98% coverage: 2:304/309 of query aligns to 2:306/320 of 2isqA
- active site: K44 (= K43), S267 (= S265)
- binding pyridoxal-5'-phosphate: K44 (= K43), N75 (= N73), G177 (≠ A175), G179 (= G177), T180 (= T178), G181 (= G179), T183 (≠ S181), G223 (= G221), S267 (= S265), P294 (≠ C292)
- binding : T72 (= T70), S73 (= S71), G74 (= G72), T76 (= T74), G122 (= G120), M123 (= M121), K124 (= K122), G217 (= G215), P218 (= P216), H219 (= H217), Q222 (= Q220), G223 (= G221)
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)
55% identity, 98% coverage: 4:305/309 of query aligns to 76:379/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
56% identity, 98% coverage: 2:304/309 of query aligns to 2:306/320 of 1z7yA
- active site: A44 (≠ K43), S267 (= S265)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G72), N75 (= N73), T76 (= T74), Q145 (= Q143), I178 (= I176), G179 (= G177), T180 (= T178), G181 (= G179), T183 (≠ S181), G223 (= G221), S267 (= S265), P294 (≠ C292), S295 (≠ D293)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
54% identity, 99% coverage: 1:305/309 of query aligns to 2:307/310 of 5xoqA
- binding : T72 (= T70), S73 (= S71), G74 (= G72), T76 (= T74), M123 (= M121), Q144 (= Q143), R218 (≠ P216), H219 (= H217), Q222 (= Q220), G223 (= G221), A226 (= A224)
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)
54% identity, 98% coverage: 2:304/309 of query aligns to 3:312/323 of P0ABK5
- K42 (= K43) 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
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)
53% identity, 98% coverage: 2:304/309 of query aligns to 3:312/323 of P0A1E3
- N72 (= N73) binding pyridoxal 5'-phosphate
- S273 (= S265) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
51% identity, 97% coverage: 4:304/309 of query aligns to 10:311/329 of 8b9wA
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
51% identity, 97% coverage: 6:305/309 of query aligns to 14:315/329 of 3vbeC
- active site: K52 (= K43), S81 (= S71), E212 (= E202), S216 (= S206), S275 (= S265), P302 (≠ C292)
- binding pyridoxal-5'-phosphate: K52 (= K43), N83 (= N73), M184 (≠ I174), G187 (= G177), S188 (≠ T178), G189 (= G179), T191 (≠ S181), G231 (= G221), S275 (= S265), P302 (≠ C292)
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
53% identity, 98% coverage: 2:304/309 of query aligns to 4:313/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K43), N73 (= N73), V177 (≠ I176), G178 (= G177), T179 (= T178), G180 (= G179), T182 (≠ S181), G230 (= G221), S274 (= S265), P301 (≠ C292)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K43), T70 (= T70), G72 (= G72), N73 (= N73), T74 (= T74), Q144 (= Q143), F145 (= F144), Q229 (= Q220), G230 (= G221), I231 (= I222), A233 (= A224)
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)
51% identity, 97% coverage: 5:305/309 of query aligns to 30:332/347 of Q9FS29
- E157 (= E130) mutation E->N,Q: No effect on catalytic activities.
Query Sequence
>WP_013136878.1 NCBI__GCF_000092245.1:WP_013136878.1
MKYANDVTELIGNTPLVKLKKASTNGTTVLGKCEFMNPTHSVKDRIGFNMINEAIKSGKI
TEGTTVIEPTSGNTGIALASVCAAKGIKLILTMPSSMSIERRKLLKALGAQIVLTEPEKG
MKGAVEKANELSESLDNSIVLQQFANEANPDIHRKTTALEILRDTDDKVDVLVIAIGTGG
SITGISEVVKAKNPNVKVIAVEPTDSPVLSGGNPGPHKIQGIGAGFVPAVLNTKIYDEII
TVSNDDAMETARNLAKDEGLLVGISAGANVFASTALAQREEYKGKTIVTILCDTGERYLS
TPLYQFDDE
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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