SitesBLAST
Comparing WP_011802813.1 NCBI__GCF_000015505.1:WP_011802813.1 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)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
51% identity, 98% coverage: 3:302/305 of query aligns to 4:308/318 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)
53% identity, 98% coverage: 3:302/305 of query aligns to 4:305/306 of 2q3dA
- active site: K44 (= K42), S266 (= S264), P293 (≠ Y290)
- 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 (= Q142), V177 (= V175), G178 (= G176), T179 (= T177), G180 (= G178), T182 (≠ H180), G222 (= G220), I223 (= I221), S266 (= S264), P293 (≠ Y290), D294 (= D291)
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)
53% identity, 98% coverage: 3:302/305 of query aligns to 4:305/310 of P9WP55
- K44 (= K42) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N72) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (≠ GTGGH 176:180) binding pyridoxal 5'-phosphate
- S266 (= S264) binding pyridoxal 5'-phosphate
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
53% identity, 97% coverage: 3:297/305 of query aligns to 4:300/300 of 3zeiA
- active site: K44 (= K42), S266 (= S264), P293 (≠ Y290)
- 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 (= Q142), F145 (= F143), K215 (≠ P213), G222 (= G220), A225 (= A223), F227 (= F225)
- binding pyridoxal-5'-phosphate: K44 (= K42), N74 (= N72), V177 (= V175), G178 (= G176), T179 (= T177), G180 (= G178), T182 (≠ H180), G222 (= G220), S266 (= S264), P293 (≠ Y290), D294 (= D291)
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)
53% identity, 97% coverage: 3:297/305 of query aligns to 4:300/300 of 2q3cA
- active site: K44 (= K42), S266 (= S264), P293 (≠ Y290)
- binding : T71 (= T69), S72 (= S70), G73 (= G71), T75 (= T73), M122 (= M120), Q144 (= Q142), K215 (≠ P213), G222 (= G220), A225 (= A223)
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
51% identity, 98% coverage: 3:302/305 of query aligns to 4:308/310 of 4lmbA
- active site: K46 (= K42), S269 (= S264)
- binding cysteine: K46 (= K42), T74 (= T69), S75 (= S70), N77 (= N72), T78 (= T73), M101 (= M96), M125 (= M120), M125 (= M120), Q147 (= Q142), F148 (= F143), Q224 (= Q219), G225 (= G220), G225 (= G220), I226 (= I221), A228 (= A223)
- binding pyridoxal-5'-phosphate: K46 (= K42), N77 (= N72), V180 (= V175), G181 (= G176), T182 (= T177), G183 (= G178), T185 (≠ H180), G225 (= G220), S269 (= S264), P296 (≠ Y290)
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)
51% identity, 98% coverage: 3:302/305 of query aligns to 6:308/322 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 pyridoxal 5'-phosphate; 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 (= Q142) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H152) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (≠ A157) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (≠ GTGGH 176:180) binding pyridoxal 5'-phosphate
- T182 (= T177) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (≠ H180) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ A212) mutation to A: Impaired interaction with SAT1.
- H221 (= H216) mutation to A: Impaired interaction with SAT1.
- K222 (≠ P217) mutation to A: Impaired interaction with SAT1.
- S269 (= S264) binding pyridoxal 5'-phosphate; mutation to A: Strong reduction of cysteine synthase activity.; mutation to T: Reduction of cysteine synthase activity.
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)
51% identity, 98% coverage: 3:302/305 of query aligns to 76:378/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
51% identity, 98% coverage: 3:302/305 of query aligns to 4:306/320 of 2isqA
- active site: K44 (= K42), S267 (= S264)
- binding pyridoxal-5'-phosphate: K44 (= K42), N75 (= N72), G177 (= G174), G179 (= G176), T180 (= T177), G181 (= G178), T183 (≠ H180), G223 (= G220), S267 (= S264), P294 (≠ Y290)
- binding : T72 (= T69), S73 (= S70), G74 (= G71), T76 (= T73), G122 (= G119), M123 (= M120), K124 (= K121), G217 (≠ A214), P218 (= P215), H219 (= H216), Q222 (= Q219), G223 (= G220)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
52% identity, 96% coverage: 9:302/305 of query aligns to 11:306/310 of 5xoqA
- binding : T72 (= T69), S73 (= S70), G74 (= G71), T76 (= T73), M123 (= M120), Q144 (= Q142), R218 (≠ P215), H219 (= H216), Q222 (= Q219), G223 (= G220), A226 (= A223)
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
51% identity, 98% coverage: 3:302/305 of query aligns to 4:306/309 of 7n2tA
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
51% identity, 98% coverage: 3:302/305 of query aligns to 4:306/320 of 1z7yA
- active site: A44 (≠ K42), S267 (= S264)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G71), N75 (= N72), T76 (= T73), Q145 (= Q142), I178 (≠ V175), G179 (= G176), T180 (= T177), G181 (= G178), T183 (≠ H180), G223 (= G220), S267 (= S264), P294 (≠ Y290), S295 (≠ D291)
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
49% identity, 98% coverage: 3:302/305 of query aligns to 14:316/323 of 4aecA
- active site: K54 (= K42), S277 (= S264)
- binding pyridoxal-5'-phosphate: K54 (= K42), N85 (= N72), I188 (≠ V175), G189 (= G176), T190 (= T177), G191 (= G178), G192 (= G179), T193 (≠ H180), G233 (= G220), S277 (= S264), P304 (≠ Y290)
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
51% identity, 95% coverage: 10:298/305 of query aligns to 7:297/302 of 2efyA
- active site: K40 (= K42), S70 (= S70), E200 (= E201), S204 (= S205), S263 (= S264)
- binding 5-oxohexanoic acid: T69 (= T69), G71 (= G71), T73 (= T73), Q141 (= Q142), G175 (= G176), G219 (= G220), M220 (≠ I221), P222 (≠ A223)
- binding pyridoxal-5'-phosphate: K40 (= K42), N72 (= N72), Y172 (≠ T173), G175 (= G176), T176 (= T177), G177 (= G178), T179 (≠ H180), G219 (= G220), S263 (= S264), P289 (≠ Y290), D290 (= D291)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
51% identity, 95% coverage: 10:298/305 of query aligns to 7:297/302 of 2ecqA
- active site: K40 (= K42), S70 (= S70), E200 (= E201), S204 (= S205), S263 (= S264)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K42), G71 (= G71), T73 (= T73), Q141 (= Q142), G219 (= G220)
- binding pyridoxal-5'-phosphate: K40 (= K42), N72 (= N72), Y172 (≠ T173), G173 (= G174), G175 (= G176), T176 (= T177), T179 (≠ H180), G219 (= G220), S263 (= S264), P289 (≠ Y290)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
51% identity, 95% coverage: 10:298/305 of query aligns to 7:297/302 of 2ecoA
- active site: K40 (= K42), S70 (= S70), E200 (= E201), S204 (= S205), S263 (= S264)
- binding 4-methyl valeric acid: K40 (= K42), T69 (= T69), G71 (= G71), T73 (= T73), Q141 (= Q142), G175 (= G176), T176 (= T177), G219 (= G220)
- binding pyridoxal-5'-phosphate: K40 (= K42), N72 (= N72), Y172 (≠ T173), G175 (= G176), T176 (= T177), T179 (≠ H180), G219 (= G220), S263 (= S264), P289 (≠ Y290), D290 (= D291)
5xemA Crystal structure of a hydrogen sulfide-producing enzyme (fn1220) from fusobacterium nucleatum in complex with l-lanthionine-plp schiff base
47% identity, 97% coverage: 3:298/305 of query aligns to 3:301/302 of 5xemA
- binding (2R)-2-azanyl-3-[(2R)-2-azanyl-3-oxidanyl-3-oxidanylidene-propyl]sulfanyl-propanoic acid: K42 (= K42), T69 (= T69), S70 (= S70), N72 (= N72), T73 (= T73), M120 (= M120), Q142 (= Q142), G176 (= G176), T177 (= T177), G220 (= G220), M221 (≠ I221), G222 (= G222), S224 (vs. gap)
- binding calcium ion: L300 (= L297), S301 (= S298)
- binding pyridoxal-5'-phosphate: K42 (= K42), N72 (= N72), T175 (≠ V175), G176 (= G176), T177 (= T177), G178 (= G178), S180 (≠ H180), G220 (= G220), S266 (= S264), T293 (≠ Y290), D294 (= D291)
Sites not aligning to the query:
5xenA Crystal structure of a hydrogen sulfide-producing enzyme (fn1220) from fusobacterium nucleatum in complex with l-serine-plp schiff base
47% identity, 97% coverage: 3:297/305 of query aligns to 3:300/300 of 5xenA
- binding pyridoxal-5'-phosphate: K42 (= K42), K42 (= K42), N72 (= N72), N72 (= N72), T175 (≠ V175), T175 (≠ V175), G176 (= G176), G176 (= G176), T177 (= T177), T177 (= T177), G178 (= G178), G178 (= G178), S180 (≠ H180), S180 (≠ H180), G220 (= G220), G220 (= G220), S266 (= S264), S266 (= S264), T293 (≠ Y290), T293 (≠ Y290), D294 (= D291), D294 (= D291)
- binding serine: K42 (= K42), T69 (= T69), S70 (= S70), N72 (= N72), T73 (= T73), Q142 (= Q142)
3x43A Crystal structure of o-ureido-l-serine synthase (see paper)
49% identity, 98% coverage: 4:302/305 of query aligns to 4:302/316 of 3x43A
- active site: K42 (= K42), S264 (= S264)
- binding pyridoxal-5'-phosphate: K42 (= K42), N72 (= N72), F175 (≠ V175), G176 (= G176), T177 (= T177), T178 (≠ G178), T180 (≠ H180), G220 (= G220), S264 (= S264), P290 (≠ Y290), D291 (= D291)
D2Z027 O-ureido-L-serine synthase; Cysteine synthase homolog DscD; O-acetylserine sulfhydrylase; EC 2.6.99.3; EC 2.5.1.47 from Streptomyces lavendulae (see paper)
49% identity, 98% coverage: 4:302/305 of query aligns to 5:303/324 of D2Z027
- K43 (= K42) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Loss of catalytic activity, no longer binds N6-(pyridoxal phosphate)lysine.
- V74 (≠ T73) mutation to T: KM for OAS is 61 mM, KM for H(2)S is unchanged.
- Y97 (≠ M96) mutation to F: KM for OAS is unchanged, KM for H(2)S is 0.073 mM.; mutation to M: KM for OAS is 330 mM, KM for H(2)S is 0.084.
- S121 (≠ M120) mutation to A: KM for OAS is 140 mM, KM for H(2)S is 0.095 mM.; mutation to M: KM for OAS is 44 mM, KM for H(2)S is 0.20 mM.
Query Sequence
>WP_011802813.1 NCBI__GCF_000015505.1:WP_011802813.1
MKADSILATIGNTPHVRINRLFGPDAQVWIKSERANPGGSIKDRIALSMVEDAEKSGALK
PGGSIIEPTSGNTGIGLAMVAAVKGYKLVLVMPDSMSVERRRLMLAYGASFDLTPRANGM
KGAIARAQELIAATPGSWMPQQFENPANIDIHVRTTAQEILADFPDGLDVLITGVGTGGH
LTGCAKVLKAAWPQLKVFAVEPAASPVISGGAPAPHPIQGIGAGFIPKNLDTSLLDGVIQ
VDAEPAREMARRSASEEGMLVGISSGATLAAIAQKLAELPAGTRVLGFNYDTGERYLSVE
GFFPA
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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