SitesBLAST
Comparing 16513 FitnessBrowser__Keio:16513 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)
100% identity, 100% coverage: 1:323/323 of query aligns to 1:323/323 of P0ABK5
- M1 (= M1) modified: Initiator methionine, Removed
- K42 (= K42) 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)
97% identity, 100% coverage: 1:323/323 of query aligns to 1:323/323 of P0A1E3
- M1 (= M1) modified: Initiator methionine, Removed
- N72 (= N72) binding
- S273 (= S273) binding
1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
97% identity, 100% coverage: 2:323/323 of query aligns to 1:322/322 of 1d6sA
- active site: A41 (≠ K42), G228 (= G229)
- binding methionine: T68 (= T69), N69 (≠ S70), N71 (= N72), T72 (= T73), Q142 (= Q143), F143 (= F144), G176 (= G177), G228 (= G229)
- binding pyridoxal-5'-phosphate: N71 (= N72), G176 (= G177), T177 (= T178), G178 (= G179), T180 (= T181), G228 (= G229), S272 (= S273), P299 (= P300)
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
97% identity, 99% coverage: 1:320/323 of query aligns to 2:321/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K42), N73 (= N72), V177 (= V176), G178 (= G177), T179 (= T178), G180 (= G179), T182 (= T181), G230 (= G229), S274 (= S273), P301 (= P300)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K42), T70 (= T69), G72 (= G71), N73 (= N72), T74 (= T73), Q144 (= Q143), F145 (= F144), Q229 (= Q228), G230 (= G229), I231 (= I230), A233 (= A232)
1fcjA Crystal structure of oass complexed with chloride and sulfate (see paper)
97% identity, 93% coverage: 2:303/323 of query aligns to 1:302/302 of 1fcjA
- active site: K41 (= K42), G228 (= G229), S272 (= S273)
- binding pyridoxal-5'-phosphate: K41 (= K42), N71 (= N72), V175 (= V176), G176 (= G177), T177 (= T178), G178 (= G179), T180 (= T181), G228 (= G229), S272 (= S273), P299 (= P300)
- binding sulfate ion: G70 (= G71), T72 (= T73), Q142 (= Q143)
1y7lA O-acetylserine sulfhydrylase complex (see paper)
71% identity, 96% coverage: 4:312/323 of query aligns to 2:310/310 of 1y7lA
5dbhX Crystal structure of o-acetylserine sulfhydrylase from haemophilus influenzae in complex with reaction intermediate alpha-aminoacrylate
71% identity, 96% coverage: 4:312/323 of query aligns to 2:310/312 of 5dbhX
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: K41 (= K42), T68 (= T69), S69 (= S70), N71 (= N72), T72 (= T73), Q142 (= Q143), G176 (= G177), T177 (= T178), G178 (= G179), S180 (≠ T181), G227 (= G229), S271 (= S273), P298 (= P300)
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
70% identity, 96% coverage: 4:312/323 of query aligns to 3:309/309 of 4zu6X
- binding o-acetylserine: T69 (= T69), S70 (= S70), T73 (= T73), Q141 (= Q143), G175 (= G177), G226 (= G229)
- binding pyridoxal-5'-phosphate: K42 (= K42), N72 (= N72), V174 (= V176), G175 (= G177), T176 (= T178), G177 (= G179), G178 (= G180), S179 (≠ T181), G226 (= G229), S270 (= S273), P297 (= P300)
- binding : S70 (= S70), T95 (= T95), M96 (= M96), K118 (= K118), G119 (= G119), P221 (= P224), H222 (= H225), K223 (= K226), A229 (= A232)
4oreX Cyrstal structure of o-acetylserine sulfhydrylase ternary complex from haemophilus influenzae at 2.2 a
70% identity, 96% coverage: 4:312/323 of query aligns to 2:308/308 of 4oreX
- binding o-acetylserine: K115 (= K118), G116 (= G119), M117 (= M120)
- binding : K41 (= K42), T68 (= T69), G69 (= G71), T71 (= T73), P91 (= P93), M117 (= M120), F141 (= F144), G219 (= G223), P220 (= P224), H221 (= H225), G225 (= G229), A228 (= A232)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
64% identity, 97% coverage: 4:315/323 of query aligns to 4:309/310 of 5xoqA
- binding : T72 (= T69), S73 (= S70), G74 (= G71), T76 (= T73), M123 (= M120), Q144 (= Q143), R218 (≠ E218), H219 (= H225), Q222 (= Q228), G223 (= G229), A226 (= A232)
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
58% identity, 98% coverage: 4:318/323 of query aligns to 13:322/323 of 4aecA
- active site: K54 (= K42), S277 (= S273)
- binding pyridoxal-5'-phosphate: K54 (= K42), N85 (= N72), I188 (≠ V176), G189 (= G177), T190 (= T178), G191 (= G179), G192 (= G180), T193 (= T181), G233 (= G229), S277 (= S273), P304 (= P300)
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, 99% coverage: 4:323/323 of query aligns to 75:389/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
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)
57% identity, 97% coverage: 4:315/323 of query aligns to 3:308/310 of P9WP55
- K44 (= K42) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N72) binding
- GTGGT 178:182 (= GTGGT 177:181) binding
- S266 (= S273) binding
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
57% identity, 99% coverage: 3:321/323 of query aligns to 2:316/318 of 4lmaA
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)
57% identity, 96% coverage: 4:313/323 of query aligns to 3:306/306 of 2q3dA
- active site: K44 (= K42), S266 (= S273), P293 (= P300)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K42), T71 (= T69), S72 (= S70), N74 (= N72), T75 (= T73), Q144 (= Q143), V177 (= V176), G178 (= G177), T179 (= T178), G180 (= G179), T182 (= T181), G222 (= G229), I223 (= I230), S266 (= S273), P293 (= P300), D294 (≠ S301)
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
56% identity, 96% coverage: 4:314/323 of query aligns to 3:310/310 of 4lmbA
- active site: K46 (= K42), S269 (= S273)
- binding cysteine: K46 (= K42), T74 (= T69), S75 (= S70), N77 (= N72), T78 (= T73), M101 (= M96), M125 (= M120), M125 (= M120), Q147 (= Q143), F148 (= F144), Q224 (= Q228), G225 (= G229), G225 (= G229), I226 (= I230), A228 (= A232)
- binding pyridoxal-5'-phosphate: K46 (= K42), N77 (= N72), V180 (= V176), G181 (= G177), T182 (= T178), G183 (= G179), T185 (= T181), G225 (= G229), S269 (= S273), P296 (= P300)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
57% identity, 94% coverage: 4:307/323 of query aligns to 3:300/300 of 3zeiA
- active site: K44 (= K42), S266 (= S273), P293 (= P300)
- 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 (= T69), S72 (= S70), I126 (= I124), Q144 (= Q143), F145 (= F144), K215 (≠ E219), G222 (= G229), A225 (= A232), F227 (= F234)
- binding pyridoxal-5'-phosphate: K44 (= K42), N74 (= N72), V177 (= V176), G178 (= G177), T179 (= T178), G180 (= G179), T182 (= T181), G222 (= G229), S266 (= S273), P293 (= P300), D294 (≠ S301)
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)
57% identity, 94% coverage: 4:307/323 of query aligns to 3:300/300 of 2q3cA
- active site: K44 (= K42), S266 (= S273), P293 (= P300)
- binding : T71 (= T69), S72 (= S70), G73 (= G71), T75 (= T73), M122 (= M120), Q144 (= Q143), K215 (≠ E219), G222 (= G229), A225 (= A232)
2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
55% identity, 96% coverage: 2:312/323 of query aligns to 1:306/320 of 2isqA
- active site: K44 (= K42), S267 (= S273)
- binding pyridoxal-5'-phosphate: K44 (= K42), N75 (= N72), G177 (= G175), G179 (= G177), T180 (= T178), G181 (= G179), T183 (= T181), G223 (= G229), S267 (= S273), P294 (= P300)
- binding : T72 (= T69), S73 (= S70), G74 (= G71), T76 (= T73), G122 (= G119), M123 (= M120), K124 (= K121), G217 (= G223), P218 (= P224), H219 (= H225), Q222 (= Q228), G223 (= G229)
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, 96% coverage: 2:312/323 of query aligns to 3:308/322 of P47998
- K46 (= K42) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T69) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S70) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N72) binding ; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T73) 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 (= G158) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 177:181) binding
- 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 (= K221) mutation to A: Impaired interaction with SAT1.
- H221 (= H225) mutation to A: Impaired interaction with SAT1.
- K222 (= K226) mutation to A: Impaired interaction with SAT1.
- S269 (= S273) binding ; mutation to A: Strong reduction of cysteine synthase activity.; mutation to T: Reduction of cysteine synthase activity.
Query Sequence
>16513 FitnessBrowser__Keio:16513
MSKIFEDNSLTIGHTPLVRLNRIGNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLK
PGVELVEPTSGNTGIALAYVAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGAKGM
KGAIQKAEEIVASNPEKYLLLQQFSNPANPEIHEKTTGPEIWEDTDGQVDVFIAGVGTGG
TLTGVSRYIKGTKGKTDLISVAVEPTDSPVIAQALAGEEIKPGPHKIQGIGAGFIPANLD
LKLVDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDESFTNKNIVVILP
SSGERYLSTALFADLFTEKELQQ
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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