SitesBLAST
Comparing WP_012759846.1 NCBI__GCF_000023185.1:WP_012759846.1 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)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
61% identity, 97% coverage: 9:318/320 of query aligns to 2:311/318 of 4lmaA
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)
63% identity, 96% coverage: 10:315/320 of query aligns to 3:305/306 of 2q3dA
- active site: K44 (= K53), S266 (= S276), P293 (= P303)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K53), T71 (= T81), S72 (= S82), N74 (= N84), T75 (= T85), Q144 (= Q154), V177 (≠ I187), G178 (= G188), T179 (= T189), G180 (= G190), T182 (= T192), G222 (= G232), I223 (= I233), S266 (= S276), P293 (= P303), D294 (≠ S304)
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)
63% identity, 96% coverage: 10:315/320 of query aligns to 3:305/310 of P9WP55
- K44 (= K53) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N84) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 188:192) binding pyridoxal 5'-phosphate
- S266 (= S276) binding pyridoxal 5'-phosphate
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
62% identity, 96% coverage: 10:316/320 of query aligns to 3:309/310 of 4lmbA
- active site: K46 (= K53), S269 (= S276)
- binding cysteine: K46 (= K53), T74 (= T81), S75 (= S82), N77 (= N84), T78 (= T85), M101 (= M108), M125 (= M132), M125 (= M132), Q147 (= Q154), F148 (= F155), Q224 (= Q231), G225 (= G232), G225 (= G232), I226 (= I233), A228 (= A235)
- binding pyridoxal-5'-phosphate: K46 (= K53), N77 (= N84), V180 (≠ I187), G181 (= G188), T182 (= T189), G183 (= G190), T185 (= T192), G225 (= G232), S269 (= S276), P296 (= P303)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
62% identity, 94% coverage: 10:310/320 of query aligns to 3:300/300 of 3zeiA
- active site: K44 (= K53), S266 (= S276), P293 (= P303)
- 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 (= T81), S72 (= S82), I126 (= I136), Q144 (= Q154), F145 (= F155), K215 (≠ P225), G222 (= G232), A225 (= A235), F227 (= F237)
- binding pyridoxal-5'-phosphate: K44 (= K53), N74 (= N84), V177 (≠ I187), G178 (= G188), T179 (= T189), G180 (= G190), T182 (= T192), G222 (= G232), S266 (= S276), P293 (= P303), D294 (≠ S304)
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, 94% coverage: 10:310/320 of query aligns to 3:300/300 of 2q3cA
- active site: K44 (= K53), S266 (= S276), P293 (= P303)
- binding : T71 (= T81), S72 (= S82), G73 (= G83), T75 (= T85), M122 (= M132), Q144 (= Q154), K215 (≠ P225), G222 (= G232), A225 (= A235)
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
60% identity, 97% coverage: 10:318/320 of query aligns to 13:319/323 of 4aecA
- active site: K54 (= K53), S277 (= S276)
- binding pyridoxal-5'-phosphate: K54 (= K53), N85 (= N84), I188 (= I187), G189 (= G188), T190 (= T189), G191 (= G190), G192 (= G191), T193 (= T192), G233 (= G232), S277 (= S276), P304 (= P303)
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)
59% identity, 97% coverage: 10:318/320 of query aligns to 75:381/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
59% identity, 97% coverage: 10:318/320 of query aligns to 3:309/309 of 7n2tA
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)
59% identity, 96% coverage: 9:316/320 of query aligns to 4:309/322 of P47998
- K46 (= K53) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T81) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S82) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N84) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T85) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q154) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H164) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (≠ A169) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 188:192) binding pyridoxal 5'-phosphate
- T182 (= T189) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T192) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ N224) mutation to A: Impaired interaction with SAT1.
- H221 (= H228) mutation to A: Impaired interaction with SAT1.
- K222 (= K229) mutation to A: Impaired interaction with SAT1.
- S269 (= S276) 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)
59% identity, 96% coverage: 9:316/320 of query aligns to 2:307/320 of 2isqA
- active site: K44 (= K53), S267 (= S276)
- binding pyridoxal-5'-phosphate: K44 (= K53), N75 (= N84), G177 (= G186), G179 (= G188), T180 (= T189), G181 (= G190), T183 (= T192), G223 (= G232), S267 (= S276), P294 (= P303)
- binding : T72 (= T81), S73 (= S82), G74 (= G83), T76 (= T85), G122 (= G131), M123 (= M132), K124 (= K133), G217 (= G226), P218 (= P227), H219 (= H228), Q222 (= Q231), G223 (= G232)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
59% identity, 97% coverage: 10:318/320 of query aligns to 4:309/310 of 5xoqA
- binding : T72 (= T81), S73 (= S82), G74 (= G83), T76 (= T85), M123 (= M132), Q144 (= Q154), R218 (≠ P227), H219 (= H228), Q222 (= Q231), G223 (= G232), A226 (= A235)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
59% identity, 96% coverage: 9:316/320 of query aligns to 2:307/320 of 1z7yA
- active site: A44 (≠ K53), S267 (= S276)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G83), N75 (= N84), T76 (= T85), Q145 (= Q154), I178 (= I187), G179 (= G188), T180 (= T189), G181 (= G190), T183 (= T192), G223 (= G232), S267 (= S276), P294 (= P303), S295 (= S304)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
54% identity, 97% coverage: 7:315/320 of query aligns to 4:310/341 of Q93244
- P75 (= P80) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A93) mutation to V: In n5522; severe loss of protein stability.
- S144 (≠ A149) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (= G186) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G188) mutation to R: In n5515; severe loss of protein stability.
- G229 (= G234) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (≠ L264) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S277) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (≠ I300) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
55% identity, 97% coverage: 9:318/320 of query aligns to 4:316/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K53), N73 (= N84), V177 (≠ I187), G178 (= G188), T179 (= T189), G180 (= G190), T182 (= T192), G230 (= G232), S274 (= S276), P301 (= P303)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K53), T70 (= T81), G72 (= G83), N73 (= N84), T74 (= T85), Q144 (= Q154), F145 (= F155), Q229 (= Q231), G230 (= G232), I231 (= I233), A233 (= A235)
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
52% identity, 95% coverage: 13:315/320 of query aligns to 12:311/329 of 8b9wA
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, 97% coverage: 9:318/320 of query aligns to 3:315/323 of P0A1E3
- N72 (= N84) binding pyridoxal 5'-phosphate
- S273 (= S276) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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, 97% coverage: 9:318/320 of query aligns to 3:315/323 of P0ABK5
- K42 (= K53) 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
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
51% identity, 97% coverage: 9:318/320 of query aligns to 10:317/329 of 3vbeC
- active site: K52 (= K53), S81 (= S82), E212 (= E213), S216 (= S217), S275 (= S276), P302 (= P303)
- binding pyridoxal-5'-phosphate: K52 (= K53), N83 (= N84), M184 (≠ S185), G187 (= G188), S188 (≠ T189), G189 (= G190), T191 (= T192), G231 (= G232), S275 (= S276), P302 (= P303)
1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
55% identity, 97% coverage: 9:318/320 of query aligns to 2:314/322 of 1d6sA
- active site: A41 (≠ K53), G228 (= G232)
- binding methionine: T68 (= T81), N69 (≠ S82), N71 (= N84), T72 (= T85), Q142 (= Q154), F143 (= F155), G176 (= G188), G228 (= G232)
- binding pyridoxal-5'-phosphate: N71 (= N84), G176 (= G188), T177 (= T189), G178 (= G190), T180 (= T192), G228 (= G232), S272 (= S276), P299 (= P303)
Query Sequence
>WP_012759846.1 NCBI__GCF_000023185.1:WP_012759846.1
MSHKPGRGRIYSSITETIGDTPLVRFDKLAREKGVVANLIGKLEFFNPIASVKDRIGVAM
IEGLEAQGKITPGKTVLIEPTSGNTGIALAFAAAAKGYRLILTMPETMSVERRKMLALLG
AELVLTEGPKGMKGAIAKAEELASSLPDAVIPQQFENPDNPEIHRKTTAEEIWNDTDGTV
DMVVSGIGTGGTITGVGQVLKSRKPEIKIIAVEPADSPILSGGNPGPHKIQGIGAGFAPK
ILDTGIYDEVVTVTNDEAFEQARLVARLEGVPVGISSGAALTAAIKVGVRPENAGKNIVI
IIPSFAERYLSTALFEGLGS
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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