SitesBLAST
Comparing WP_012282809.1 NCBI__GCF_000019165.1:WP_012282809.1 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)
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)
69% identity, 98% coverage: 3:306/309 of query aligns to 2:305/306 of 2q3dA
- active site: K44 (= K45), S266 (= S267), P293 (= P294)
- 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 (= G223), I223 (= I224), S266 (= S267), P293 (= P294), D294 (= D295)
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)
69% identity, 98% coverage: 3:306/309 of query aligns to 2:305/310 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 (= S267) binding pyridoxal 5'-phosphate
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
69% identity, 97% coverage: 3:301/309 of query aligns to 2:300/300 of 3zeiA
- active site: K44 (= K45), S266 (= S267), P293 (= P294)
- 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 (≠ V127), Q144 (= Q145), F145 (= F146), K215 (≠ P216), G222 (= G223), A225 (≠ P226), F227 (= F228)
- binding pyridoxal-5'-phosphate: K44 (= K45), N74 (= N75), V177 (= V178), G178 (= G179), T179 (= T180), G180 (= G181), T182 (= T183), G222 (= G223), S266 (= S267), P293 (= P294), D294 (= D295)
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)
69% identity, 97% coverage: 3:301/309 of query aligns to 2:300/300 of 2q3cA
- active site: K44 (= K45), S266 (= S267), P293 (= P294)
- binding : T71 (= T72), S72 (= S73), G73 (= G74), T75 (= T76), M122 (= M123), Q144 (= Q145), K215 (≠ P216), G222 (= G223), A225 (≠ P226)
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
65% identity, 98% coverage: 4:307/309 of query aligns to 3:309/310 of 4lmbA
- active site: K46 (= K45), S269 (= S267)
- binding cysteine: K46 (= K45), T74 (= T72), S75 (= S73), N77 (= N75), T78 (= T76), M101 (≠ F99), M125 (= M123), M125 (= M123), Q147 (= Q145), F148 (= F146), Q224 (= Q222), G225 (= G223), G225 (= G223), I226 (= I224), A228 (≠ P226)
- binding pyridoxal-5'-phosphate: K46 (= K45), N77 (= N75), V180 (= V178), G181 (= G179), T182 (= T180), G183 (= G181), T185 (= T183), G225 (= G223), S269 (= S267), P296 (= P294)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
62% identity, 99% coverage: 3:307/309 of query aligns to 2:309/318 of 4lmaA
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)
64% identity, 99% coverage: 4:308/309 of query aligns to 75:380/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
62% identity, 98% coverage: 4:307/309 of query aligns to 13:317/323 of 4aecA
- active site: K54 (= K45), S277 (= S267)
- binding pyridoxal-5'-phosphate: K54 (= K45), N85 (= N75), I188 (≠ V178), G189 (= G179), T190 (= T180), G191 (= G181), G192 (= G182), T193 (= T183), G233 (= G223), S277 (= S267), P304 (= P294)
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
61% identity, 99% coverage: 2:307/309 of query aligns to 1:307/309 of 7n2tA
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
62% identity, 98% coverage: 4:307/309 of query aligns to 4:307/310 of 5xoqA
- binding : T72 (= T72), S73 (= S73), G74 (= G74), T76 (= T76), M123 (= M123), Q144 (= Q145), R218 (≠ P218), H219 (= H219), Q222 (= Q222), G223 (= G223), A226 (≠ P226)
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)
58% identity, 99% coverage: 2:306/309 of query aligns to 3:308/322 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 (≠ A160) 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 (≠ Q215) mutation to A: Impaired interaction with SAT1.
- H221 (= H219) mutation to A: Impaired interaction with SAT1.
- K222 (= K220) mutation to A: Impaired interaction with SAT1.
- S269 (= S267) 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)
58% identity, 99% coverage: 2:306/309 of query aligns to 1:306/320 of 2isqA
- active site: K44 (= K45), S267 (= S267)
- binding pyridoxal-5'-phosphate: K44 (= K45), N75 (= N75), G177 (= G177), G179 (= G179), T180 (= T180), G181 (= G181), T183 (= T183), G223 (= G223), S267 (= S267), P294 (= P294)
- binding : T72 (= T72), S73 (= S73), G74 (= G74), T76 (= T76), G122 (= G122), M123 (= M123), K124 (= K124), G217 (= G217), P218 (= P218), H219 (= H219), Q222 (= Q222), G223 (= G223)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
58% identity, 99% coverage: 2:306/309 of query aligns to 1:306/320 of 1z7yA
- active site: A44 (≠ K45), S267 (= S267)
- 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 (= G223), S267 (= S267), P294 (= P294), S295 (≠ D295)
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
52% identity, 98% coverage: 4:307/309 of query aligns to 11:315/329 of 3vbeC
- active site: K52 (= K45), S81 (= S73), E212 (= E204), S216 (= S208), S275 (= S267), P302 (= P294)
- binding pyridoxal-5'-phosphate: K52 (= K45), N83 (= N75), M184 (≠ G176), G187 (= G179), S188 (≠ T180), G189 (= G181), T191 (= T183), G231 (= G223), S275 (= S267), P302 (= P294)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
55% identity, 98% coverage: 3:306/309 of query aligns to 6:310/341 of Q93244
- P75 (= P71) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A84) mutation to V: In n5522; severe loss of protein stability.
- S144 (≠ A140) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (= G177) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G179) mutation to R: In n5515; severe loss of protein stability.
- G229 (= G225) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (= R255) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S268) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (≠ V291) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
3vc3A Crystal structure of beta-cyanoalanine synthase k95a mutant in soybean (see paper)
52% identity, 98% coverage: 4:307/309 of query aligns to 4:308/322 of 3vc3A
- active site: A45 (≠ K45), S268 (= S267), P295 (= P294)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-cysteine: T73 (= T72), S74 (= S73), N76 (= N75), M77 (≠ T76), Q146 (= Q145), M177 (≠ G176), G180 (= G179), S181 (≠ T180), G182 (= G181), T184 (= T183), G224 (= G223), S268 (= S267), P295 (= P294)
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)
55% identity, 99% coverage: 1:306/309 of query aligns to 1:312/323 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.
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
55% identity, 99% coverage: 1:306/309 of query aligns to 2:313/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K45), N73 (= N75), V177 (= V178), G178 (= G179), T179 (= T180), G180 (= G181), T182 (= T183), G230 (= G223), S274 (= S267), P301 (= P294)
- 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 (= Q222), G230 (= G223), I231 (= I224), A233 (≠ P226)
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)
55% identity, 99% coverage: 1:306/309 of query aligns to 1:312/323 of P0A1E3
- M1 (= M1) modified: Initiator methionine, Removed
- N72 (= N75) binding pyridoxal 5'-phosphate
- S273 (= S267) binding pyridoxal 5'-phosphate
1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
54% identity, 99% coverage: 2:306/309 of query aligns to 1:311/322 of 1d6sA
- active site: A41 (≠ K45), G228 (= G223)
- binding methionine: T68 (= T72), N69 (≠ S73), N71 (= N75), T72 (= T76), Q142 (= Q145), F143 (= F146), G176 (= G179), G228 (= G223)
- binding pyridoxal-5'-phosphate: N71 (= N75), G176 (= G179), T177 (= T180), G178 (= G181), T180 (= T183), G228 (= G223), S272 (= S267), P299 (= P294)
Query Sequence
>WP_012282809.1 NCBI__GCF_000019165.1:WP_012282809.1
MAKIANNITDLIGKTPLVRLNRVTEGLEADVVAKLEYFNPGGSVKDRIGYAMIKDAEEKG
LLHKDSVIIEPTSGNTGIALSFVAATLGYRVILTMPETFSIERRNLLKAYGAELVLTPGT
EGMKGAVRRAEELAAQIPNAFIPQQFNNPANPKIHRATTAEEIWADTDGKVDILVGGVGT
GGTITGVGETLKARKPGLQVIAVEPFDSPVLSGGQPGPHKIQGIGPGFVPQVLNLEVADE
IYKVRNDEAFETSRRIAREEGILVGISSGAAAYAALQIAKRPENAGKLIVVVLPDTGERY
LSTPLFQGA
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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