SitesBLAST
Comparing Dsui_2521 FitnessBrowser__PS:Dsui_2521 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)
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)
68% identity, 98% coverage: 4:326/328 of query aligns to 1:321/323 of P0ABK5
- M1 (= M4) modified: Initiator methionine, Removed
- K42 (= K48) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Still stimulates tRNase activity of CdiA-CT in vitro and in vivo.
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)
68% identity, 98% coverage: 4:326/328 of query aligns to 1:321/323 of P0A1E3
- M1 (= M4) modified: Initiator methionine, Removed
- N72 (= N78) binding
- S273 (= S278) binding
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
68% identity, 98% coverage: 4:323/328 of query aligns to 2:319/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K48), N73 (= N78), V177 (= V182), G178 (= G183), T179 (= T184), G180 (= G185), T182 (= T187), G230 (= G234), S274 (= S278), P301 (= P305)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K48), T70 (= T75), G72 (= G77), N73 (= N78), T74 (= T79), Q144 (= Q149), F145 (= F150), Q229 (= Q233), G230 (= G234), I231 (= I235), A233 (= A237)
1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
67% identity, 98% coverage: 5:326/328 of query aligns to 1:320/322 of 1d6sA
- active site: A41 (≠ K48), G228 (= G234)
- binding methionine: T68 (= T75), N69 (≠ S76), N71 (= N78), T72 (= T79), Q142 (= Q149), F143 (= F150), G176 (= G183), G228 (= G234)
- binding pyridoxal-5'-phosphate: N71 (= N78), G176 (= G183), T177 (= T184), G178 (= G185), T180 (= T187), G228 (= G234), S272 (= S278), P299 (= P305)
1fcjA Crystal structure of oass complexed with chloride and sulfate (see paper)
68% identity, 93% coverage: 5:308/328 of query aligns to 1:302/302 of 1fcjA
- active site: K41 (= K48), G228 (= G234), S272 (= S278)
- binding pyridoxal-5'-phosphate: K41 (= K48), N71 (= N78), V175 (= V182), G176 (= G183), T177 (= T184), G178 (= G185), T180 (= T187), G228 (= G234), S272 (= S278), P299 (= P305)
- binding sulfate ion: G70 (= G77), T72 (= T79), Q142 (= Q149)
5dbhX Crystal structure of o-acetylserine sulfhydrylase from haemophilus influenzae in complex with reaction intermediate alpha-aminoacrylate
67% identity, 95% coverage: 8:319/328 of query aligns to 3:312/312 of 5dbhX
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: K41 (= K48), T68 (= T75), S69 (= S76), N71 (= N78), T72 (= T79), Q142 (= Q149), G176 (= G183), T177 (= T184), G178 (= G185), S180 (≠ T187), G227 (= G234), S271 (= S278), P298 (= P305)
1y7lA O-acetylserine sulfhydrylase complex (see paper)
67% identity, 95% coverage: 8:317/328 of query aligns to 3:310/310 of 1y7lA
4zu6X Crystal structure of o-acetylserine sulfhydrylase from haemophilus influenzae in complex with pre-reactive o-acetyl serine, alpha- aminoacrylate reaction intermediate and peptide inhibitor at the resolution of 2.25a
66% identity, 95% coverage: 8:317/328 of query aligns to 4:309/309 of 4zu6X
- binding o-acetylserine: T69 (= T75), S70 (= S76), T73 (= T79), Q141 (= Q149), G175 (= G183), G226 (= G234)
- binding pyridoxal-5'-phosphate: K42 (= K48), N72 (= N78), V174 (= V182), G175 (= G183), T176 (= T184), G177 (= G185), G178 (= G186), S179 (≠ T187), G226 (= G234), S270 (= S278), P297 (= P305)
- binding : S70 (= S76), T95 (= T101), M96 (= M102), K118 (= K124), G119 (= G125), P221 (= P229), H222 (= H230), K223 (= K231), A229 (= A237)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
65% identity, 95% coverage: 8:320/328 of query aligns to 5:309/310 of 5xoqA
- binding : T72 (= T75), S73 (= S76), G74 (= G77), T76 (= T79), M123 (= M126), Q144 (= Q149), R218 (≠ P229), H219 (= H230), Q222 (= Q233), G223 (= G234), A226 (= A237)
4oreX Cyrstal structure of o-acetylserine sulfhydrylase ternary complex from haemophilus influenzae at 2.2 a
66% identity, 95% coverage: 8:317/328 of query aligns to 3:308/308 of 4oreX
- binding o-acetylserine: K115 (= K124), G116 (= G125), M117 (= M126)
- binding : K41 (= K48), T68 (= T75), G69 (= G77), T71 (= T79), P91 (= P99), M117 (= M126), F141 (= F150), G219 (= G228), P220 (= P229), H221 (= H230), G225 (= G234), A228 (= A237)
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, 95% coverage: 10:320/328 of query aligns to 6:308/310 of P9WP55
- K44 (= K48) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N78) binding
- GTGGT 178:182 (= GTGGT 183:187) binding
- S266 (= S278) binding
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, 94% coverage: 10:317/328 of query aligns to 6:305/306 of 2q3dA
- active site: K44 (= K48), S266 (= S278), P293 (= P305)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K48), T71 (= T75), S72 (= S76), N74 (= N78), T75 (= T79), Q144 (= Q149), V177 (= V182), G178 (= G183), T179 (= T184), G180 (= G185), T182 (= T187), G222 (= G234), I223 (= I235), S266 (= S278), P293 (= P305), D294 (= D306)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
62% identity, 92% coverage: 10:312/328 of query aligns to 6:300/300 of 3zeiA
- active site: K44 (= K48), S266 (= S278), P293 (= P305)
- 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 (= T75), S72 (= S76), I126 (= I130), Q144 (= Q149), F145 (= F150), K215 (≠ N221), G222 (= G234), A225 (= A237), F227 (= F239)
- binding pyridoxal-5'-phosphate: K44 (= K48), N74 (= N78), V177 (= V182), G178 (= G183), T179 (= T184), G180 (= G185), T182 (= T187), G222 (= G234), S266 (= S278), P293 (= P305), D294 (= D306)
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, 92% coverage: 10:312/328 of query aligns to 6:300/300 of 2q3cA
- active site: K44 (= K48), S266 (= S278), P293 (= P305)
- binding : T71 (= T75), S72 (= S76), G73 (= G77), T75 (= T79), M122 (= M126), Q144 (= Q149), K215 (≠ N221), G222 (= G234), A225 (= A237)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
57% identity, 95% coverage: 10:320/328 of query aligns to 6:311/318 of 4lmaA
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)
56% identity, 97% coverage: 6:324/328 of query aligns to 74:385/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
56% identity, 96% coverage: 8:323/328 of query aligns to 13:322/323 of 4aecA
- active site: K54 (= K48), S277 (= S278)
- binding pyridoxal-5'-phosphate: K54 (= K48), N85 (= N78), I188 (≠ V182), G189 (= G183), T190 (= T184), G191 (= G185), G192 (= G186), T193 (= T187), G233 (= G234), S277 (= S278), P304 (= P305)
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
58% identity, 94% coverage: 10:318/328 of query aligns to 6:309/310 of 4lmbA
- active site: K46 (= K48), S269 (= S278)
- binding cysteine: K46 (= K48), T74 (= T75), S75 (= S76), N77 (= N78), T78 (= T79), M101 (= M102), M125 (= M126), M125 (= M126), Q147 (= Q149), F148 (= F150), Q224 (= Q233), G225 (= G234), G225 (= G234), I226 (= I235), A228 (= A237)
- binding pyridoxal-5'-phosphate: K46 (= K48), N77 (= N78), V180 (= V182), G181 (= G183), T182 (= T184), G183 (= G185), T185 (= T187), G225 (= G234), S269 (= S278), P296 (= P305)
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)
57% identity, 96% coverage: 10:324/328 of query aligns to 8:315/322 of P47998
- K46 (= K48) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T75) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S76) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N78) binding ; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T79) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q149) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H159) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (= G164) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 183:187) binding
- T182 (= T184) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T187) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (= K226) mutation to A: Impaired interaction with SAT1.
- H221 (= H230) mutation to A: Impaired interaction with SAT1.
- K222 (= K231) mutation to A: Impaired interaction with SAT1.
- S269 (= S278) binding ; 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)
57% identity, 96% coverage: 10:324/328 of query aligns to 6:313/320 of 2isqA
- active site: K44 (= K48), S267 (= S278)
- binding pyridoxal-5'-phosphate: K44 (= K48), N75 (= N78), G177 (= G181), G179 (= G183), T180 (= T184), G181 (= G185), T183 (= T187), G223 (= G234), S267 (= S278), P294 (= P305)
- binding : T72 (= T75), S73 (= S76), G74 (= G77), T76 (= T79), G122 (= G125), M123 (= M126), K124 (≠ G127), G217 (= G228), P218 (= P229), H219 (= H230), Q222 (= Q233), G223 (= G234)
Query Sequence
>Dsui_2521 FitnessBrowser__PS:Dsui_2521
MKSMSNWFSDNSRSIGRTPLVRLNRVTDGAPATVLAKIEGRNPAYSVKCRIGAAMVWDAE
IRGLLGPGKELVEPTSGNTGIALAFVAAVYGIPLTLTMPETMSLERRKLLAAYGAKLVLT
EGTKGMGGAIAKAEEIAASDPGKYVLLQQFKNPANPAIHESTTGPEIWIDTDDKVDIFVS
GVGTGGTITGVSRYFKKTRGAKLWSVAVEPSASPVLTQTRNGEPVKPGPHKIQGIGAGFV
PQVLDLSLIDAIEQVSNEEAVAYARRLAREEGIISGISSGAAVAVASRLAQRRENAGKTI
VVILPDSGERYLSSVLFEGVFNEAGLPV
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