SitesBLAST
Comparing WP_015931650.1 NCBI__GCF_000022085.1:WP_015931650.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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, 94% coverage: 19:327/327 of query aligns to 2:311/318 of 4lmaA
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
61% identity, 92% coverage: 23:324/327 of query aligns to 6:308/310 of 4lmbA
- active site: K46 (= K63), S269 (= S285)
- binding cysteine: K46 (= K63), T74 (= T90), S75 (= S91), N77 (= N93), T78 (= T94), M101 (= M117), M125 (= M141), M125 (= M141), Q147 (= Q163), F148 (= F164), Q224 (= Q240), G225 (= G241), G225 (= G241), I226 (≠ L242), A228 (= A244)
- binding pyridoxal-5'-phosphate: K46 (= K63), N77 (= N93), V180 (= V196), G181 (= G197), T182 (= T198), G183 (= G199), T185 (= T201), G225 (= G241), S269 (= S285), P296 (= P312)
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, 92% coverage: 23:324/327 of query aligns to 6:305/306 of 2q3dA
- active site: K44 (= K63), S266 (= S285), P293 (= P312)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K63), T71 (= T90), S72 (= S91), N74 (= N93), T75 (= T94), Q144 (= Q163), V177 (= V196), G178 (= G197), T179 (= T198), G180 (= G199), T182 (= T201), G222 (= G241), I223 (≠ L242), S266 (= S285), P293 (= P312), D294 (≠ S313)
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)
62% identity, 92% coverage: 23:324/327 of query aligns to 6:305/310 of P9WP55
- K44 (= K63) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N93) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 197:201) binding pyridoxal 5'-phosphate
- S266 (= S285) binding pyridoxal 5'-phosphate
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
61% identity, 95% coverage: 17:327/327 of query aligns to 1:309/310 of 5xoqA
- binding : T72 (= T90), S73 (= S91), G74 (= G92), T76 (= T94), M123 (= M141), Q144 (= Q163), R218 (≠ P236), H219 (= H237), Q222 (= Q240), G223 (= G241), A226 (= A244)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
62% identity, 91% coverage: 23:319/327 of query aligns to 6:300/300 of 3zeiA
- active site: K44 (= K63), S266 (= S285), P293 (= P312)
- 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 (= T90), S72 (= S91), I126 (≠ L145), Q144 (= Q163), F145 (= F164), K215 (≠ P234), G222 (= G241), A225 (= A244), F227 (= F246)
- binding pyridoxal-5'-phosphate: K44 (= K63), N74 (= N93), V177 (= V196), G178 (= G197), T179 (= T198), G180 (= G199), T182 (= T201), G222 (= G241), S266 (= S285), P293 (= P312), D294 (≠ S313)
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, 91% coverage: 23:319/327 of query aligns to 6:300/300 of 2q3cA
- active site: K44 (= K63), S266 (= S285), P293 (= P312)
- binding : T71 (= T90), S72 (= S91), G73 (= G92), T75 (= T94), M122 (= M141), Q144 (= Q163), K215 (≠ P234), G222 (= G241), A225 (= A244)
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
57% identity, 93% coverage: 23:327/327 of query aligns to 16:319/323 of 4aecA
- active site: K54 (= K63), S277 (= S285)
- binding pyridoxal-5'-phosphate: K54 (= K63), N85 (= N93), I188 (≠ V196), G189 (= G197), T190 (= T198), G191 (= G199), G192 (= G200), T193 (= T201), G233 (= G241), S277 (= S285), P304 (= P312)
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)
57% identity, 92% coverage: 26:327/327 of query aligns to 81:381/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
54% identity, 93% coverage: 23:327/327 of query aligns to 12:314/329 of 8b9wA
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
56% identity, 93% coverage: 24:327/327 of query aligns to 7:309/309 of 7n2tA
2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
55% identity, 94% coverage: 19:325/327 of query aligns to 2:307/320 of 2isqA
- active site: K44 (= K63), S267 (= S285)
- binding pyridoxal-5'-phosphate: K44 (= K63), N75 (= N93), G177 (= G195), G179 (= G197), T180 (= T198), G181 (= G199), T183 (= T201), G223 (= G241), S267 (= S285), P294 (= P312)
- binding : T72 (= T90), S73 (= S91), G74 (= G92), T76 (= T94), G122 (= G140), M123 (= M141), K124 (= K142), G217 (= G235), P218 (= P236), H219 (= H237), Q222 (= Q240), G223 (= G241)
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)
55% identity, 94% coverage: 19:325/327 of query aligns to 4:309/322 of P47998
- K46 (= K63) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T90) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S91) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N93) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T94) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q163) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H173) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (≠ A178) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 197:201) binding pyridoxal 5'-phosphate
- T182 (= T198) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T201) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ N233) mutation to A: Impaired interaction with SAT1.
- H221 (= H237) mutation to A: Impaired interaction with SAT1.
- K222 (= K238) mutation to A: Impaired interaction with SAT1.
- S269 (= S285) 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)
55% identity, 94% coverage: 19:325/327 of query aligns to 2:307/320 of 1z7yA
- active site: A44 (≠ K63), S267 (= S285)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G92), N75 (= N93), T76 (= T94), Q145 (= Q163), I178 (≠ V196), G179 (= G197), T180 (= T198), G181 (= G199), T183 (= T201), G223 (= G241), S267 (= S285), P294 (= P312), S295 (= S313)
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)
56% identity, 94% coverage: 19:324/327 of query aligns to 3:312/323 of P0ABK5
- K42 (= K63) 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
3t4pA Crystal structure of o-acetyl serine sulfhydrylase from leishmania donovani in complex with designed tetrapeptide (see paper)
52% identity, 93% coverage: 23:327/327 of query aligns to 13:315/319 of 3t4pA
- active site: K50 (= K63), S273 (= S285)
- binding : S78 (≠ T90), S79 (= S91), G80 (= G92), T82 (= T94), M129 (= M141), Q151 (= Q163), F152 (= F164), G223 (= G235), P224 (= P236), H225 (= H237), G229 (= G241), G231 (= G243), P232 (≠ A244)
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)
56% identity, 94% coverage: 19:324/327 of query aligns to 3:312/323 of P0A1E3
- N72 (= N93) binding pyridoxal 5'-phosphate
- S273 (= S285) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
56% identity, 94% coverage: 19:324/327 of query aligns to 4:313/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K63), N73 (= N93), V177 (= V196), G178 (= G197), T179 (= T198), G180 (= G199), T182 (= T201), G230 (= G241), S274 (= S285), P301 (= P312)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K63), T70 (= T90), G72 (= G92), N73 (= N93), T74 (= T94), Q144 (= Q163), F145 (= F164), Q229 (= Q240), G230 (= G241), I231 (≠ L242), A233 (= A244)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
56% identity, 92% coverage: 28:327/327 of query aligns to 15:313/341 of Q93244
- P75 (= P89) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A102) mutation to V: In n5522; severe loss of protein stability.
- S144 (= S158) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (= G195) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G197) mutation to R: In n5515; severe loss of protein stability.
- G229 (= G243) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (≠ L273) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (≠ T286) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (= T309) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
55% identity, 94% coverage: 19:324/327 of query aligns to 2:311/322 of 1d6sA
- active site: A41 (≠ K63), G228 (= G241)
- binding methionine: T68 (= T90), N69 (≠ S91), N71 (= N93), T72 (= T94), Q142 (= Q163), F143 (= F164), G176 (= G197), G228 (= G241)
- binding pyridoxal-5'-phosphate: N71 (= N93), G176 (= G197), T177 (= T198), G178 (= G199), T180 (= T201), G228 (= G241), S272 (= S285), P299 (= P312)
Query Sequence
>WP_015931650.1 NCBI__GCF_000022085.1:WP_015931650.1
MADAATTASDTGRKPGHGRVFGSITETIGNTPLVRLNRLPQERGVEAEILLKLEFFNPIA
SVKDRIGVSMIDALEASGTLKPGGTLVEPTSGNTGIALAFVAAARGYRLILVMPETMSIE
RRKMLLFLGAELVLTPGPQGMKGALAKAEELLGEIPGSIMPQQFNNPANPEIHRDTTAEE
IWNDTQGHLDAFVAGVGTGGTITGVGQVLKPRLPQLRVIAVEPEDSPVLSGGNPGPHKIQ
GLGAGFVPNVLDRSVIDEVVTVSNQTAFETARLLSRLEGIPGGISTGANVAAALEVAARP
EFRGKRIATVAPSFAERYISSALFDGI
Or try a new SitesBLAST search
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