SitesBLAST
Comparing WP_085770473.1 NCBI__GCF_002117405.1:WP_085770473.1 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)
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, 94% coverage: 18:323/326 of query aligns to 3:305/310 of P9WP55
- K44 (= K61) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N92) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 196:200) binding pyridoxal 5'-phosphate
- S266 (= S284) 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)
63% identity, 94% coverage: 18:323/326 of query aligns to 3:305/306 of 2q3dA
- active site: K44 (= K61), S266 (= S284), P293 (= P311)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K61), T71 (= T89), S72 (= S90), N74 (= N92), T75 (= T93), Q144 (= Q162), V177 (= V195), G178 (= G196), T179 (= T197), G180 (= G198), T182 (= T200), G222 (= G240), I223 (= I241), S266 (= S284), P293 (= P311), D294 (≠ S312)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
59% identity, 95% coverage: 17:326/326 of query aligns to 2:311/318 of 4lmaA
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
63% identity, 92% coverage: 18:318/326 of query aligns to 3:300/300 of 3zeiA
- active site: K44 (= K61), S266 (= S284), P293 (= P311)
- 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 (= T89), S72 (= S90), I126 (≠ V144), Q144 (= Q162), F145 (= F163), K215 (≠ P233), G222 (= G240), A225 (= A243), F227 (= F245)
- binding pyridoxal-5'-phosphate: K44 (= K61), N74 (= N92), V177 (= V195), G178 (= G196), T179 (= T197), G180 (= G198), T182 (= T200), G222 (= G240), S266 (= S284), P293 (= P311), D294 (≠ S312)
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)
63% identity, 92% coverage: 18:318/326 of query aligns to 3:300/300 of 2q3cA
- active site: K44 (= K61), S266 (= S284), P293 (= P311)
- binding : T71 (= T89), S72 (= S90), G73 (= G91), T75 (= T93), M122 (= M140), Q144 (= Q162), K215 (≠ P233), G222 (= G240), A225 (= A243)
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
59% identity, 94% coverage: 18:324/326 of query aligns to 3:309/310 of 4lmbA
- active site: K46 (= K61), S269 (= S284)
- binding cysteine: K46 (= K61), T74 (= T89), S75 (= S90), N77 (= N92), T78 (= T93), M101 (= M116), M125 (= M140), M125 (= M140), Q147 (= Q162), F148 (= F163), Q224 (= Q239), G225 (= G240), G225 (= G240), I226 (= I241), A228 (= A243)
- binding pyridoxal-5'-phosphate: K46 (= K61), N77 (= N92), V180 (= V195), G181 (= G196), T182 (= T197), G183 (= G198), T185 (= T200), G225 (= G240), S269 (= S284), P296 (= P311)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
61% identity, 95% coverage: 18:326/326 of query aligns to 4:309/310 of 5xoqA
- binding : T72 (= T89), S73 (= S90), G74 (= G91), T76 (= T93), M123 (= M140), Q144 (= Q162), R218 (≠ P235), H219 (= H236), Q222 (= Q239), G223 (= G240), A226 (= A243)
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
58% identity, 95% coverage: 17:326/326 of query aligns to 12:319/323 of 4aecA
- active site: K54 (= K61), S277 (= S284)
- binding pyridoxal-5'-phosphate: K54 (= K61), N85 (= N92), I188 (≠ V195), G189 (= G196), T190 (= T197), G191 (= G198), G192 (= G199), T193 (= T200), G233 (= G240), S277 (= S284), P304 (= P311)
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)
58% identity, 95% coverage: 18:326/326 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, 95% coverage: 18:326/326 of query aligns to 3:309/309 of 7n2tA
2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
58% identity, 94% coverage: 17:324/326 of query aligns to 2:307/320 of 2isqA
- active site: K44 (= K61), S267 (= S284)
- binding pyridoxal-5'-phosphate: K44 (= K61), N75 (= N92), G177 (= G194), G179 (= G196), T180 (= T197), G181 (= G198), T183 (= T200), G223 (= G240), S267 (= S284), P294 (= P311)
- binding : T72 (= T89), S73 (= S90), G74 (= G91), T76 (= T93), G122 (= G139), M123 (= M140), K124 (= K141), G217 (= G234), P218 (= P235), H219 (= H236), Q222 (= Q239), G223 (= G240)
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, 94% coverage: 17:324/326 of query aligns to 4:309/322 of P47998
- K46 (= K61) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T89) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S90) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N92) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T93) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q162) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H172) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (≠ A177) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 196:200) binding pyridoxal 5'-phosphate
- T182 (= T197) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T200) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ P232) mutation to A: Impaired interaction with SAT1.
- H221 (= H236) mutation to A: Impaired interaction with SAT1.
- K222 (= K237) mutation to A: Impaired interaction with SAT1.
- S269 (= S284) 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)
58% identity, 94% coverage: 17:324/326 of query aligns to 2:307/320 of 1z7yA
- active site: A44 (≠ K61), S267 (= S284)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G91), N75 (= N92), T76 (= T93), Q145 (= Q162), I178 (≠ V195), G179 (= G196), T180 (= T197), G181 (= G198), T183 (= T200), G223 (= G240), S267 (= S284), P294 (= P311), S295 (= S312)
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
55% identity, 93% coverage: 21:323/326 of query aligns to 12:311/329 of 8b9wA
3t4pA Crystal structure of o-acetyl serine sulfhydrylase from leishmania donovani in complex with designed tetrapeptide (see paper)
54% identity, 95% coverage: 18:326/326 of query aligns to 10:315/319 of 3t4pA