SitesBLAST
Comparing WP_013819405.1 NCBI__GCF_000214665.1:WP_013819405.1 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)
61% identity, 99% coverage: 1:299/301 of query aligns to 1:301/310 of P9WP55
- K44 (= K44) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N74) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 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)
61% identity, 99% coverage: 1:299/301 of query aligns to 1:301/306 of 2q3dA
- active site: K44 (= K44), S266 (= S265), P293 (≠ H291)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K44), T71 (= T71), S72 (= S72), N74 (= N74), T75 (= T75), Q144 (= Q143), V177 (= V176), G178 (= G177), T179 (= T178), G180 (= G179), T182 (= T181), G222 (= G221), I223 (= I222), S266 (= S265), P293 (≠ H291), D294 (= D292)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
61% identity, 99% coverage: 1:298/301 of query aligns to 1:300/300 of 3zeiA
- active site: K44 (= K44), S266 (= S265), P293 (≠ H291)
- 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 (= T71), S72 (= S72), I126 (= I126), Q144 (= Q143), F145 (= F144), K215 (≠ H214), G222 (= G221), A225 (= A224), F227 (= F226)
- binding pyridoxal-5'-phosphate: K44 (= K44), N74 (= N74), V177 (= V176), G178 (= G177), T179 (= T178), G180 (= G179), T182 (= T181), G222 (= G221), S266 (= S265), P293 (≠ H291), D294 (= D292)
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)
61% identity, 99% coverage: 1:298/301 of query aligns to 1:300/300 of 2q3cA
- active site: K44 (= K44), S266 (= S265), P293 (≠ H291)
- binding : T71 (= T71), S72 (= S72), G73 (= G73), T75 (= T75), M122 (= M122), Q144 (= Q143), K215 (≠ H214), G222 (= G221), A225 (= A224)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
58% identity, 99% coverage: 1:299/301 of query aligns to 1:304/318 of 4lmaA
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
58% identity, 97% coverage: 8:299/301 of query aligns to 9:302/310 of 5xoqA
- binding : T72 (= T71), S73 (= S72), G74 (= G73), T76 (= T75), M123 (= M122), Q144 (= Q143), R218 (≠ P216), H219 (= H217), Q222 (= Q220), G223 (= G221), A226 (= A224)
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
56% identity, 99% coverage: 1:299/301 of query aligns to 1:304/310 of 4lmbA
- active site: K46 (= K44), S269 (= S265)
- binding cysteine: K46 (= K44), T74 (= T71), S75 (= S72), N77 (= N74), T78 (= T75), M101 (= M98), M125 (= M122), M125 (= M122), Q147 (= Q143), F148 (= F144), Q224 (= Q220), G225 (= G221), G225 (= G221), I226 (= I222), A228 (= A224)
- binding pyridoxal-5'-phosphate: K46 (= K44), N77 (= N74), V180 (= V176), G181 (= G177), T182 (= T178), G183 (= G179), T185 (= T181), G225 (= G221), S269 (= S265), P296 (≠ H291)
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, 96% coverage: 11:299/301 of query aligns to 12:308/323 of P0ABK5
- K42 (= K44) 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)
55% identity, 96% coverage: 11:299/301 of query aligns to 12:308/323 of P0A1E3
- N72 (= N74) binding pyridoxal 5'-phosphate
- S273 (= S265) 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)
55% identity, 96% coverage: 11:299/301 of query aligns to 13:309/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K44), N73 (= N74), V177 (= V176), G178 (= G177), T179 (= T178), G180 (= G179), T182 (= T181), G230 (= G221), S274 (= S265), P301 (≠ H291)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K44), T70 (= T71), G72 (= G73), N73 (= N74), T74 (= T75), Q144 (= Q143), F145 (= F144), Q229 (= Q220), G230 (= G221), I231 (= I222), A233 (= A224)
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
55% identity, 98% coverage: 4:299/301 of query aligns to 14:312/323 of 4aecA
- active site: K54 (= K44), S277 (= S265)
- binding pyridoxal-5'-phosphate: K54 (= K44), N85 (= N74), I188 (≠ V176), G189 (= G177), T190 (= T178), G191 (= G179), G192 (= G180), T193 (= T181), G233 (= G221), S277 (= S265), P304 (≠ H291)
1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
54% identity, 97% coverage: 11:301/301 of query aligns to 11:309/322 of 1d6sA
- active site: A41 (≠ K44), G228 (= G221)
- binding methionine: T68 (= T71), N69 (≠ S72), N71 (= N74), T72 (= T75), Q142 (= Q143), F143 (= F144), G176 (= G177), G228 (= G221)
- binding pyridoxal-5'-phosphate: N71 (= N74), G176 (= G177), T177 (= T178), G178 (= G179), T180 (= T181), G228 (= G221), S272 (= S265), P299 (≠ H291)
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
55% identity, 98% coverage: 4:299/301 of query aligns to 4:302/309 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)
53% identity, 98% coverage: 4:299/301 of query aligns to 6:304/322 of P47998
- K46 (= K44) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T71) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S72) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N74) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T75) 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 (= GTGGT 177:181) binding pyridoxal 5'-phosphate
- T182 (= T178) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T181) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ V213) 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)
53% identity, 98% coverage: 4:299/301 of query aligns to 4:302/320 of 2isqA
- active site: K44 (= K44), S267 (= S265)
- binding pyridoxal-5'-phosphate: K44 (= K44), N75 (= N74), G177 (= G175), G179 (= G177), T180 (= T178), G181 (= G179), T183 (= T181), G223 (= G221), S267 (= S265), P294 (≠ H291)
- binding : T72 (= T71), S73 (= S72), G74 (= G73), T76 (= T75), G122 (= G121), M123 (= M122), K124 (= K123), G217 (≠ S215), P218 (= P216), H219 (= H217), Q222 (= Q220), G223 (= G221)
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
54% identity, 96% coverage: 11:299/301 of query aligns to 7:297/302 of 2efyA
- active site: K40 (= K44), S70 (= S72), E200 (= E202), S204 (= S206), S263 (= S265)
- binding 5-oxohexanoic acid: T69 (= T71), G71 (= G73), T73 (= T75), Q141 (= Q143), G175 (= G177), G219 (= G221), M220 (≠ I222), P222 (≠ A224)
- binding pyridoxal-5'-phosphate: K40 (= K44), N72 (= N74), Y172 (≠ C174), G175 (= G177), T176 (= T178), G177 (= G179), T179 (= T181), G219 (= G221), S263 (= S265), P289 (≠ H291), D290 (= D292)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
54% identity, 96% coverage: 11:299/301 of query aligns to 7:297/302 of 2ecqA
- active site: K40 (= K44), S70 (= S72), E200 (= E202), S204 (= S206), S263 (= S265)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K44), G71 (= G73), T73 (= T75), Q141 (= Q143), G219 (= G221)
- binding pyridoxal-5'-phosphate: K40 (= K44), N72 (= N74), Y172 (≠ C174), G173 (= G175), G175 (= G177), T176 (= T178), T179 (= T181), G219 (= G221), S263 (= S265), P289 (≠ H291)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
54% identity, 96% coverage: 11:299/301 of query aligns to 7:297/302 of 2ecoA
- active site: K40 (= K44), S70 (= S72), E200 (= E202), S204 (= S206), S263 (= S265)
- binding 4-methyl valeric acid: K40 (= K44), T69 (= T71), G71 (= G73), T73 (= T75), Q141 (= Q143), G175 (= G177), T176 (= T178), G219 (= G221)
- binding pyridoxal-5'-phosphate: K40 (= K44), N72 (= N74), Y172 (≠ C174), G175 (= G177), T176 (= T178), T179 (= T181), G219 (= G221), S263 (= S265), P289 (≠ H291), D290 (= D292)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
53% identity, 98% coverage: 4:299/301 of query aligns to 4:302/320 of 1z7yA
- active site: A44 (≠ K44), S267 (= S265)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G73), N75 (= N74), T76 (= T75), Q145 (= Q143), I178 (≠ V176), G179 (= G177), T180 (= T178), G181 (= G179), T183 (= T181), G223 (= G221), S267 (= S265), P294 (≠ H291), S295 (≠ D292)
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)
54% identity, 98% coverage: 4:299/301 of query aligns to 76:374/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
Query Sequence
>WP_013819405.1 NCBI__GCF_000214665.1:WP_013819405.1
MANAINITQLIGNTPLVKLHRIVPDDSANVLVKLESRNPGGSVKDRIGLAMIQAAEKSGY
LKAGGSIVEPTSGNTGIALAMIAAARGYRCTLVMPDTMSIERRQLLALYGAEIVLTPGSE
GMKGAISKAHDIAAETGAFMPQQFENPANPEVHRQTTAQEIWSGTDGQIDAFVCGVGTGG
TITGVADVIKNRNPDFKAIAVEPAESPVISGGVHSPHKIQGIGAGFVPKNLDVDLLDGIE
LVSTEEAFAMRKRLIQEEGIMVGISSGASVCAALRVAARLGVGKTVVTIVHDTGERYLSM
S
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