SitesBLAST
Comparing WP_007692184.1 NCBI__GCF_000336675.1:WP_007692184.1 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)
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
49% identity, 88% coverage: 8:288/319 of query aligns to 6:292/302 of 2efyA
- active site: K40 (= K38), S70 (= S66), E200 (= E195), S204 (≠ N199), S263 (= S258)
- binding 5-oxohexanoic acid: T69 (= T65), G71 (= G67), T73 (= T69), Q141 (= Q135), G175 (= G170), G219 (= G214), M220 (= M215), P222 (= P217)
- binding pyridoxal-5'-phosphate: K40 (= K38), N72 (= N68), Y172 (≠ A167), G175 (= G170), T176 (= T171), G177 (= G172), T179 (= T174), G219 (= G214), S263 (= S258), P289 (≠ T285), D290 (= D286)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
49% identity, 88% coverage: 8:288/319 of query aligns to 6:292/302 of 2ecqA
- active site: K40 (= K38), S70 (= S66), E200 (= E195), S204 (≠ N199), S263 (= S258)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K38), G71 (= G67), T73 (= T69), Q141 (= Q135), G219 (= G214)
- binding pyridoxal-5'-phosphate: K40 (= K38), N72 (= N68), Y172 (≠ A167), G173 (≠ A168), G175 (= G170), T176 (= T171), T179 (= T174), G219 (= G214), S263 (= S258), P289 (≠ T285)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
49% identity, 88% coverage: 8:288/319 of query aligns to 6:292/302 of 2ecoA
- active site: K40 (= K38), S70 (= S66), E200 (= E195), S204 (≠ N199), S263 (= S258)
- binding 4-methyl valeric acid: K40 (= K38), T69 (= T65), G71 (= G67), T73 (= T69), Q141 (= Q135), G175 (= G170), T176 (= T171), G219 (= G214)
- binding pyridoxal-5'-phosphate: K40 (= K38), N72 (= N68), Y172 (≠ A167), G175 (= G170), T176 (= T171), T179 (= T174), G219 (= G214), S263 (= S258), P289 (≠ T285), D290 (= D286)
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)
44% identity, 99% coverage: 3:318/319 of query aligns to 5:305/310 of P9WP55
- K44 (= K38) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N68) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 170:174) binding pyridoxal 5'-phosphate
- S266 (= S258) 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)
44% identity, 99% coverage: 3:318/319 of query aligns to 5:305/306 of 2q3dA
- active site: K44 (= K38), S266 (= S258), P293 (≠ W306)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K38), T71 (= T65), S72 (= S66), N74 (= N68), T75 (= T69), Q144 (= Q135), V177 (= V169), G178 (= G170), T179 (= T171), G180 (= G172), T182 (= T174), G222 (= G214), I223 (≠ M215), S266 (= S258), P293 (≠ W306), D294 (= D307)
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)
42% identity, 100% coverage: 1:319/319 of query aligns to 3:304/324 of D2Z027
- K43 (= K38) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Loss of catalytic activity, no longer binds N6-(pyridoxal phosphate)lysine.
- V74 (≠ T69) mutation to T: KM for OAS is 61 mM, KM for H(2)S is unchanged.
- Y97 (≠ K92) 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 (≠ E116) 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.
3x43A Crystal structure of o-ureido-l-serine synthase (see paper)
42% identity, 100% coverage: 1:319/319 of query aligns to 2:303/316 of 3x43A
- active site: K42 (= K38), S264 (= S258)
- binding pyridoxal-5'-phosphate: K42 (= K38), N72 (= N68), F175 (≠ V169), G176 (= G170), T177 (= T171), T178 (≠ G172), T180 (= T174), G220 (= G214), S264 (= S258), P290 (≠ W306), D291 (= D307)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
43% identity, 98% coverage: 7:319/319 of query aligns to 10:307/310 of 5xoqA
- binding : T72 (= T65), S73 (= S66), G74 (= G67), T76 (= T69), M123 (= M114), Q144 (= Q135), R218 (≠ T209), H219 (≠ D210), Q222 (≠ E213), G223 (= G214), A226 (≠ P217)
3x44A Crystal structure of o-ureido-l-serine-bound k43a mutant of o-ureido- l-serine synthase (see paper)
42% identity, 100% coverage: 1:319/319 of query aligns to 2:303/321 of 3x44A
- active site: A42 (≠ K38), S264 (= S258)
- binding (E)-O-(carbamoylamino)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: T69 (= T65), S70 (= S66), N72 (= N68), V73 (≠ T69), S120 (≠ E116), Q141 (= Q135), F175 (≠ V169), G176 (= G170), T177 (= T171), T178 (≠ G172), T180 (= T174), G220 (= G214), L221 (≠ M215), P223 (= P217), S264 (= S258), P290 (≠ W306), D291 (= D307)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
44% identity, 97% coverage: 3:313/319 of query aligns to 5:300/300 of 3zeiA
- active site: K44 (= K38), S266 (= S258), P293 (≠ W306)
- 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 (= T65), S72 (= S66), I126 (≠ K118), Q144 (= Q135), F145 (= F136), K215 (≠ A207), G222 (= G214), A225 (≠ P217), F227 (= F219)
- binding pyridoxal-5'-phosphate: K44 (= K38), N74 (= N68), V177 (= V169), G178 (= G170), T179 (= T171), G180 (= G172), T182 (= T174), G222 (= G214), S266 (= S258), P293 (≠ W306), D294 (= D307)
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)
44% identity, 97% coverage: 3:313/319 of query aligns to 5:300/300 of 2q3cA
- active site: K44 (= K38), S266 (= S258), P293 (≠ W306)
- binding : T71 (= T65), S72 (= S66), G73 (= G67), T75 (= T69), M122 (= M114), Q144 (= Q135), K215 (≠ A207), G222 (= G214), A225 (≠ P217)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
45% identity, 94% coverage: 20:318/319 of query aligns to 31:310/341 of Q93244
- P75 (= P64) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A77) mutation to V: In n5522; severe loss of protein stability.
- S144 (≠ M130) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (≠ A168) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G170) mutation to R: In n5515; severe loss of protein stability.
- G229 (= G216) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (= R246) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S259) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (= T303) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
43% identity, 93% coverage: 24:319/319 of query aligns to 30:307/320 of 2isqA
- active site: K44 (= K38), S267 (= S258)
- binding pyridoxal-5'-phosphate: K44 (= K38), N75 (= N68), G177 (≠ A168), G179 (= G170), T180 (= T171), G181 (= G172), T183 (= T174), G223 (= G214), S267 (= S258), P294 (≠ W306)
- binding : T72 (= T65), S73 (= S66), G74 (= G67), T76 (= T69), G122 (vs. gap), M123 (= M114), K124 (≠ T115), G217 (= G208), P218 (≠ T209), H219 (≠ D210), Q222 (≠ E213), G223 (= G214)
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)
43% identity, 93% coverage: 24:319/319 of query aligns to 32:309/322 of P47998
- K46 (= K38) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T65) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S66) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N68) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T69) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q135) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H145) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (= G150) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 170:174) binding pyridoxal 5'-phosphate
- T182 (= T171) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T174) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ E206) mutation to A: Impaired interaction with SAT1.
- H221 (≠ D210) mutation to A: Impaired interaction with SAT1.
- K222 (≠ E211) mutation to A: Impaired interaction with SAT1.
- S269 (= S258) binding pyridoxal 5'-phosphate; mutation to A: Strong reduction of cysteine synthase activity.; mutation to T: Reduction of cysteine synthase activity.
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
42% identity, 99% coverage: 3:319/319 of query aligns to 15:317/323 of 4aecA
- active site: K54 (= K38), S277 (= S258)
- binding pyridoxal-5'-phosphate: K54 (= K38), N85 (= N68), I188 (≠ V169), G189 (= G170), T190 (= T171), G191 (= G172), G192 (= G173), T193 (= T174), G233 (= G214), S277 (= S258), P304 (≠ W306)
P16703 Cysteine synthase B; CSase B; O-acetylserine (thiol)-lyase B; OAS-TL B; O-acetylserine sulfhydrylase B; EC 2.5.1.47 from Escherichia coli (strain K12) (see paper)
40% identity, 97% coverage: 11:318/319 of query aligns to 11:292/303 of P16703
- N71 (= N68) binding pyridoxal 5'-phosphate
- S255 (= S258) binding pyridoxal 5'-phosphate
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)
43% identity, 93% coverage: 23:319/319 of query aligns to 101:379/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
40% identity, 97% coverage: 11:318/319 of query aligns to 11:292/294 of 2bhtA
- active site: K41 (= K38), S69 (= S66), Q199 (≠ E195), G203 (≠ N199), S255 (= S258), C280 (≠ W306)
- binding pyridoxal-5'-phosphate: K41 (= K38), N71 (= N68), M173 (≠ V169), G174 (= G170), T175 (= T171), T176 (≠ G172), T178 (= T174), G208 (≠ T204), S255 (= S258), C280 (≠ W306)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
42% identity, 93% coverage: 24:319/319 of query aligns to 30:307/320 of 1z7yA
- active site: A44 (≠ K38), S267 (= S258)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G67), N75 (= N68), T76 (= T69), Q145 (= Q135), I178 (≠ V169), G179 (= G170), T180 (= T171), G181 (= G172), T183 (= T174), G223 (= G214), S267 (= S258), P294 (≠ W306), S295 (≠ D307)
8s5hA Full-length human cystathionine beta-synthase with c-terminal 6xhis- tag, basal state, helical reconstruction (see paper)
42% identity, 85% coverage: 5:275/319 of query aligns to 39:325/507 of 8s5hA
Sites not aligning to the query:
Query Sequence
>WP_007692184.1 NCBI__GCF_000336675.1:WP_007692184.1
MDDSILDAIGSPLVRVASPPGTTVAAKVESKNPGGSAKDRPAAAMVKAAEEAGLLEPGDH
IVEPTSGNTGIGLAVVAAVRGYDCTIVMPASKSEERQRVMAAYGAELELVDGEMTEAKDR
ADELEAGKGMVQLRQFENPANAQAHYDTTGPEILDQVGDRTVDALVAAVGTGGTITGIGR
RLREEFPEMTVVAVEPETNAVLSTGEAGTDEFEGMGPGFVSDILDRDLIDSVETVDLEES
EAECRRLAREEGILVGQSSGASNLVARRVASRLADDASPATELQTDGGAGADTGDTDDPL
VVTVFWDSGERYMSTGMFD
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