SitesBLAST
Comparing WP_004514479.1 NCBI__GCF_000012925.1:WP_004514479.1 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)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
59% identity, 100% coverage: 1:307/307 of query aligns to 2:307/310 of 5xoqA
- binding : T72 (= T73), S73 (= S74), G74 (= G75), T76 (= T77), M123 (= M124), Q144 (= Q145), R218 (≠ P219), H219 (= H220), Q222 (= Q223), G223 (= G224), A226 (= A227)
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)
59% identity, 98% coverage: 6:306/307 of query aligns to 4:305/306 of 2q3dA
- active site: K44 (= K46), S266 (= S268), P293 (≠ C294)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K46), T71 (= T73), S72 (= S74), N74 (= N76), T75 (= T77), Q144 (= Q145), V177 (= V179), G178 (= G180), T179 (= T181), G180 (= G182), T182 (= T184), G222 (= G224), I223 (= I225), S266 (= S268), P293 (≠ C294), 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)
59% identity, 98% coverage: 6:306/307 of query aligns to 4:305/310 of P9WP55
- K44 (= K46) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N76) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 180:184) binding pyridoxal 5'-phosphate
- S266 (= S268) binding pyridoxal 5'-phosphate
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
59% identity, 96% coverage: 6:301/307 of query aligns to 4:300/300 of 3zeiA
- active site: K44 (= K46), S266 (= S268), P293 (≠ C294)
- 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 (= T73), S72 (= S74), I126 (≠ V128), Q144 (= Q145), F145 (= F146), K215 (≠ P217), G222 (= G224), A225 (= A227), F227 (= F229)
- binding pyridoxal-5'-phosphate: K44 (= K46), N74 (= N76), V177 (= V179), G178 (= G180), T179 (= T181), G180 (= G182), T182 (= T184), G222 (= G224), S266 (= S268), P293 (≠ C294), 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)
59% identity, 96% coverage: 6:301/307 of query aligns to 4:300/300 of 2q3cA
- active site: K44 (= K46), S266 (= S268), P293 (≠ C294)
- binding : T71 (= T73), S72 (= S74), G73 (= G75), T75 (= T77), M122 (= M124), Q144 (= Q145), K215 (≠ P217), G222 (= G224), A225 (= A227)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
56% identity, 98% coverage: 6:307/307 of query aligns to 4:309/318 of 4lmaA
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)
56% identity, 97% coverage: 9:307/307 of query aligns to 9:309/322 of P47998
- K46 (= K46) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T73) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S74) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N76) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T77) 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 (= G160) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 180:184) binding pyridoxal 5'-phosphate
- T182 (= T181) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T184) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ Q216) mutation to A: Impaired interaction with SAT1.
- H221 (= H220) mutation to A: Impaired interaction with SAT1.
- K222 (= K221) mutation to A: Impaired interaction with SAT1.
- S269 (= S268) 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)
56% identity, 97% coverage: 9:307/307 of query aligns to 7:307/320 of 2isqA
- active site: K44 (= K46), S267 (= S268)
- binding pyridoxal-5'-phosphate: K44 (= K46), N75 (= N76), G177 (= G178), G179 (= G180), T180 (= T181), G181 (= G182), T183 (= T184), G223 (= G224), S267 (= S268), P294 (≠ C294)
- binding : T72 (= T73), S73 (= S74), G74 (= G75), T76 (= T77), G122 (= G123), M123 (= M124), K124 (≠ R125), G217 (= G218), P218 (= P219), H219 (= H220), Q222 (= Q223), G223 (= G224)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
55% identity, 97% coverage: 9:307/307 of query aligns to 7:307/320 of 1z7yA
- active site: A44 (≠ K46), S267 (= S268)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G75), N75 (= N76), T76 (= T77), Q145 (= Q145), I178 (≠ V179), G179 (= G180), T180 (= T181), G181 (= G182), T183 (= T184), G223 (= G224), S267 (= S268), P294 (≠ C294), S295 (≠ D295)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
56% identity, 96% coverage: 13:306/307 of query aligns to 15:310/341 of Q93244
- P75 (= P72) mutation to L: In n5537; severe loss of protein stability.
- A88 (≠ C85) mutation to V: In n5522; severe loss of protein stability.
- S144 (≠ H140) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (= G178) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G180) mutation to R: In n5515; severe loss of protein stability.
- G229 (= G226) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (= R256) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S269) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (= T291) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
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)
53% identity, 99% coverage: 3:306/307 of query aligns to 4:312/323 of P0ABK5
- K42 (= K46) 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
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
56% identity, 97% coverage: 9:307/307 of query aligns to 7:307/309 of 7n2tA
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)
53% identity, 96% coverage: 13:306/307 of query aligns to 12:312/323 of P0A1E3
- N72 (= N76) binding pyridoxal 5'-phosphate
- S273 (= S268) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
55% identity, 98% coverage: 6:306/307 of query aligns to 14:316/323 of 4aecA
- active site: K54 (= K46), S277 (= S268)
- binding pyridoxal-5'-phosphate: K54 (= K46), N85 (= N76), I188 (≠ V179), G189 (= G180), T190 (= T181), G191 (= G182), G192 (= G183), T193 (= T184), G233 (= G224), S277 (= S268), P304 (≠ C294)
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
53% identity, 96% coverage: 13:306/307 of query aligns to 13:313/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K46), N73 (= N76), V177 (= V179), G178 (= G180), T179 (= T181), G180 (= G182), T182 (= T184), G230 (= G224), S274 (= S268), P301 (≠ C294)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K46), T70 (= T73), G72 (= G75), N73 (= N76), T74 (= T77), Q144 (= Q145), F145 (= F146), Q229 (= Q223), G230 (= G224), I231 (= I225), A233 (= A227)
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
55% identity, 96% coverage: 13:306/307 of query aligns to 7:301/302 of 2efyA
- active site: K40 (= K46), S70 (= S74), E200 (= E205), S204 (= S209), S263 (= S268)
- binding 5-oxohexanoic acid: T69 (= T73), G71 (= G75), T73 (= T77), Q141 (= Q145), G175 (= G180), G219 (= G224), M220 (≠ I225), P222 (≠ A227)
- binding pyridoxal-5'-phosphate: K40 (= K46), N72 (= N76), Y172 (≠ A177), G175 (= G180), T176 (= T181), G177 (= G182), T179 (= T184), G219 (= G224), S263 (= S268), P289 (≠ C294), D290 (= D295)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
55% identity, 96% coverage: 13:306/307 of query aligns to 7:301/302 of 2ecqA
- active site: K40 (= K46), S70 (= S74), E200 (= E205), S204 (= S209), S263 (= S268)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K46), G71 (= G75), T73 (= T77), Q141 (= Q145), G219 (= G224)
- binding pyridoxal-5'-phosphate: K40 (= K46), N72 (= N76), Y172 (≠ A177), G173 (= G178), G175 (= G180), T176 (= T181), T179 (= T184), G219 (= G224), S263 (= S268), P289 (≠ C294)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
55% identity, 96% coverage: 13:306/307 of query aligns to 7:301/302 of 2ecoA
- active site: K40 (= K46), S70 (= S74), E200 (= E205), S204 (= S209), S263 (= S268)
- binding 4-methyl valeric acid: K40 (= K46), T69 (= T73), G71 (= G75), T73 (= T77), Q141 (= Q145), G175 (= G180), T176 (= T181), G219 (= G224)
- binding pyridoxal-5'-phosphate: K40 (= K46), N72 (= N76), Y172 (≠ A177), G175 (= G180), T176 (= T181), T179 (= T184), G219 (= G224), S263 (= S268), P289 (≠ C294), D290 (= D295)
1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
53% identity, 96% coverage: 13:306/307 of query aligns to 11:311/322 of 1d6sA
- active site: A41 (≠ K46), G228 (= G224)
- binding methionine: T68 (= T73), N69 (≠ S74), N71 (= N76), T72 (= T77), Q142 (= Q145), F143 (= F146), G176 (= G180), G228 (= G224)
- binding pyridoxal-5'-phosphate: N71 (= N76), G176 (= G180), T177 (= T181), G178 (= G182), T180 (= T184), G228 (= G224), S272 (= S268), P299 (≠ C294)
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)
55% identity, 98% coverage: 6:307/307 of query aligns to 76:379/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
Query Sequence
>WP_004514479.1 NCBI__GCF_000012925.1:WP_004514479.1
MPVFDSDKVIEQIGNTPLQRLAKLEAPGSAAVYGKAEFFNPGGSVKDRICLAMIEAAEKD
GSLKPGMTVVEPTSGNTGIGLSMICAIKGYKLVLTMPDTMTVERRRLLAAYGAELVLTPG
AQGMRGAVQKAEELAAQPGHIMMQQFKNGANPEAHRRTTGPEIVRALSGQSIDAFVAGVG
TGGTITGVGEVLKEHNAAVRIVAVEPDASPILSGGQPGPHKIQGIGAGFVPDVLNTKVYD
EVIRVTNEDAYETVRRLAQEEGVLVGISSGANVFAALQVAKRLGPGKNVVTILCDTGERY
LSTGVFD
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