SitesBLAST
Comparing WP_005351659.1 NCBI__GCF_000173975.1:WP_005351659.1 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)
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)
60% identity, 97% coverage: 11:310/310 of query aligns to 10:307/310 of P9WP55
- K44 (= K47) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N77) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 181:185) binding pyridoxal 5'-phosphate
- S266 (= S269) 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)
60% identity, 96% coverage: 11:308/310 of query aligns to 10:305/306 of 2q3dA
- active site: K44 (= K47), S266 (= S269), P293 (= P296)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K47), T71 (= T74), S72 (= S75), N74 (= N77), T75 (= T78), Q144 (= Q147), V177 (= V180), G178 (= G181), T179 (= T182), G180 (= G183), T182 (= T185), G222 (= G225), I223 (= I226), S266 (= S269), P293 (= P296), D294 (= D297)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
60% identity, 94% coverage: 11:302/310 of query aligns to 10:299/300 of 3zeiA
- active site: K44 (= K47), S266 (= S269), P293 (= P296)
- 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 (= T74), S72 (= S75), I126 (= I129), Q144 (= Q147), F145 (= F148), K215 (≠ A218), G222 (= G225), A225 (= A228), F227 (= F230)
- binding pyridoxal-5'-phosphate: K44 (= K47), N74 (= N77), V177 (= V180), G178 (= G181), T179 (= T182), G180 (= G183), T182 (= T185), G222 (= G225), S266 (= S269), P293 (= P296), D294 (= D297)
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)
60% identity, 94% coverage: 11:302/310 of query aligns to 10:299/300 of 2q3cA
- active site: K44 (= K47), S266 (= S269), P293 (= P296)
- binding : T71 (= T74), S72 (= S75), G73 (= G76), T75 (= T78), M122 (= M125), Q144 (= Q147), K215 (≠ A218), G222 (= G225), A225 (= A228)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
59% identity, 98% coverage: 4:308/310 of query aligns to 4:306/310 of 5xoqA
- binding : T72 (= T74), S73 (= S75), G74 (= G76), T76 (= T78), M123 (= M125), Q144 (= Q147), R218 (≠ P220), H219 (= H221), Q222 (= Q224), G223 (= G225), A226 (= A228)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
57% identity, 96% coverage: 11:308/310 of query aligns to 10:308/318 of 4lmaA
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
58% identity, 99% coverage: 2:308/310 of query aligns to 1:306/309 of 7n2tA
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
58% identity, 97% coverage: 11:310/310 of query aligns to 14:312/341 of Q93244
- P75 (= P73) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A86) mutation to V: In n5522; severe loss of protein stability.
- S144 (= S142) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (= G179) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G181) mutation to R: In n5515; severe loss of protein stability.
- G229 (= G227) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (≠ L257) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S270) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (≠ A293) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
55% identity, 99% coverage: 4:310/310 of query aligns to 3:310/310 of 4lmbA
- active site: K46 (= K47), S269 (= S269)
- binding cysteine: K46 (= K47), T74 (= T74), S75 (= S75), N77 (= N77), T78 (= T78), M101 (= M101), M125 (= M125), M125 (= M125), Q147 (= Q147), F148 (= F148), Q224 (= Q224), G225 (= G225), G225 (= G225), I226 (= I226), A228 (= A228)
- binding pyridoxal-5'-phosphate: K46 (= K47), N77 (= N77), V180 (= V180), G181 (= G181), T182 (= T182), G183 (= G183), T185 (= T185), G225 (= G225), S269 (= S269), P296 (= P296)
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
57% identity, 99% coverage: 3:308/310 of query aligns to 12:316/323 of 4aecA
- active site: K54 (= K47), S277 (= S269)
- binding pyridoxal-5'-phosphate: K54 (= K47), N85 (= N77), I188 (≠ V180), G189 (= G181), T190 (= T182), G191 (= G183), G192 (= G184), T193 (= T185), G233 (= G225), S277 (= S269), P304 (= P296)
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)
57% identity, 99% coverage: 3:308/310 of query aligns to 74:378/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
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, 99% coverage: 2:308/310 of query aligns to 3:308/322 of P47998
- K46 (= K47) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T74) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S75) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N77) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T78) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q147) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H157) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (= G162) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 181:185) binding pyridoxal 5'-phosphate
- T182 (= T182) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T185) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (= K217) mutation to A: Impaired interaction with SAT1.
- H221 (= H221) mutation to A: Impaired interaction with SAT1.
- K222 (= K222) mutation to A: Impaired interaction with SAT1.
- S269 (= S269) 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)
57% identity, 99% coverage: 2:308/310 of query aligns to 1:306/320 of 2isqA
- active site: K44 (= K47), S267 (= S269)
- binding pyridoxal-5'-phosphate: K44 (= K47), N75 (= N77), G177 (= G179), G179 (= G181), T180 (= T182), G181 (= G183), T183 (= T185), G223 (= G225), S267 (= S269), P294 (= P296)
- binding : T72 (= T74), S73 (= S75), G74 (= G76), T76 (= T78), G122 (= G124), M123 (= M125), K124 (= K126), G217 (= G219), P218 (= P220), H219 (= H221), Q222 (= Q224), G223 (= G225)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
56% identity, 99% coverage: 2:308/310 of query aligns to 1:306/320 of 1z7yA
- active site: A44 (≠ K47), S267 (= S269)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G76), N75 (= N77), T76 (= T78), Q145 (= Q147), I178 (≠ V180), G179 (= G181), T180 (= T182), G181 (= G183), T183 (= T185), G223 (= G225), S267 (= S269), P294 (= P296), S295 (≠ D297)
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)
54% identity, 100% coverage: 1:310/310 of query aligns to 1:314/323 of P0ABK5
- M1 (= M1) modified: Initiator methionine, Removed
- K42 (= K47) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Still stimulates tRNase activity of CdiA-CT in vitro and in vivo.
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
54% identity, 100% coverage: 1:310/310 of query aligns to 2:315/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K47), N73 (= N77), V177 (= V180), G178 (= G181), T179 (= T182), G180 (= G183), T182 (= T185), G230 (= G225), S274 (= S269), P301 (= P296)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K47), T70 (= T74), G72 (= G76), N73 (= N77), T74 (= T78), Q144 (= Q147), F145 (= F148), Q229 (= Q224), G230 (= G225), I231 (= I226), A233 (= A228)
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)
54% identity, 100% coverage: 1:310/310 of query aligns to 1:314/323 of P0A1E3
- M1 (= M1) modified: Initiator methionine, Removed
- N72 (= N77) binding pyridoxal 5'-phosphate
- S273 (= S269) binding pyridoxal 5'-phosphate
1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
53% identity, 100% coverage: 2:310/310 of query aligns to 1:313/322 of 1d6sA
- active site: A41 (≠ K47), G228 (= G225)
- binding methionine: T68 (= T74), N69 (≠ S75), N71 (= N77), T72 (= T78), Q142 (= Q147), F143 (= F148), G176 (= G181), G228 (= G225)
- binding pyridoxal-5'-phosphate: N71 (= N77), G176 (= G181), T177 (= T182), G178 (= G183), T180 (= T185), G228 (= G225), S272 (= S269), P299 (= P296)
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
51% identity, 99% coverage: 3:310/310 of query aligns to 10:316/329 of 3vbeC
- active site: K52 (= K47), S81 (= S75), E212 (= E206), S216 (= S210), S275 (= S269), P302 (= P296)
- binding pyridoxal-5'-phosphate: K52 (= K47), N83 (= N77), M184 (≠ A178), G187 (= G181), S188 (≠ T182), G189 (= G183), T191 (= T185), G231 (= G225), S275 (= S269), P302 (= P296)
3vc3A Crystal structure of beta-cyanoalanine synthase k95a mutant in soybean (see paper)
50% identity, 99% coverage: 3:310/310 of query aligns to 3:309/322 of 3vc3A
- active site: A45 (≠ K47), S268 (= S269), P295 (= P296)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-cysteine: T73 (= T74), S74 (= S75), N76 (= N77), M77 (≠ T78), Q146 (= Q147), M177 (≠ A178), G180 (= G181), S181 (≠ T182), G182 (= G183), T184 (= T185), G224 (= G225), S268 (= S269), P295 (= P296)
Query Sequence
>WP_005351659.1 NCBI__GCF_000173975.1:WP_005351659.1
MANIYKGTLGLIGNTPLVEVANIEKELGLKARVLVKLEYFNPAGSVKDRIAKAMIEDAEK
KGILKEGSVIIEPTSGNTGIGLASIAAAKGYRIILTMPETMSVERRNILKAYGAEIVLTS
GAKGMKGAIAKANELSEEIEGSFIPGQFVNPANPAIHKATTGPEIWNDTDGEVDIFIAGV
GTGGTLTGTGQYLREQKPEVKIVALEPDTSPVLSEGKAGPHKIQGIGAGFVPDVLDTKIY
DEIFRATNEDAFATAKLLAKKEGILVGISSGASLHAAIEYAKKPENEGKTIVALLPDTGD
RYYSTALFTE
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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