SitesBLAST
Comparing WP_012067744.1 NCBI__GCF_000017145.1:WP_012067744.1 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)
60% identity, 96% coverage: 11:320/322 of query aligns to 2:311/318 of 4lmaA
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, 94% coverage: 15:317/322 of query aligns to 6:305/310 of P9WP55
- K44 (= K55) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N86) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 190:194) binding pyridoxal 5'-phosphate
- S266 (= S278) 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)
62% identity, 94% coverage: 15:317/322 of query aligns to 6:305/306 of 2q3dA
- active site: K44 (= K55), S266 (= S278), P293 (= P305)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K55), T71 (= T83), S72 (= S84), N74 (= N86), T75 (= T87), Q144 (= Q156), V177 (≠ I189), G178 (= G190), T179 (= T191), G180 (= G192), T182 (= T194), G222 (= G234), I223 (= I235), S266 (= S278), P293 (= P305), D294 (≠ S306)
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
62% identity, 94% coverage: 15:318/322 of query aligns to 6:309/310 of 4lmbA
- active site: K46 (= K55), S269 (= S278)
- binding cysteine: K46 (= K55), T74 (= T83), S75 (= S84), N77 (= N86), T78 (= T87), M101 (= M110), M125 (= M134), M125 (= M134), Q147 (= Q156), F148 (= F157), Q224 (= Q233), G225 (= G234), G225 (= G234), I226 (= I235), A228 (= A237)
- binding pyridoxal-5'-phosphate: K46 (= K55), N77 (= N86), V180 (≠ I189), G181 (= G190), T182 (= T191), G183 (= G192), T185 (= T194), G225 (= G234), S269 (= S278), P296 (= P305)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
62% identity, 93% coverage: 15:312/322 of query aligns to 6:300/300 of 3zeiA
- active site: K44 (= K55), 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 (= T83), S72 (= S84), I126 (= I138), Q144 (= Q156), F145 (= F157), K215 (≠ P227), G222 (= G234), A225 (= A237), F227 (= F239)
- binding pyridoxal-5'-phosphate: K44 (= K55), N74 (= N86), V177 (≠ I189), G178 (= G190), T179 (= T191), G180 (= G192), T182 (= T194), G222 (= G234), S266 (= S278), P293 (= P305), D294 (≠ S306)
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, 93% coverage: 15:312/322 of query aligns to 6:300/300 of 2q3cA
- active site: K44 (= K55), S266 (= S278), P293 (= P305)
- binding : T71 (= T83), S72 (= S84), G73 (= G85), T75 (= T87), M122 (= M134), Q144 (= Q156), K215 (≠ P227), G222 (= G234), A225 (= A237)
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
59% identity, 96% coverage: 11:320/322 of query aligns to 12:319/323 of 4aecA
- active site: K54 (= K55), S277 (= S278)
- binding pyridoxal-5'-phosphate: K54 (= K55), N85 (= N86), I188 (= I189), G189 (= G190), T190 (= T191), G191 (= G192), G192 (= G193), T193 (= T194), G233 (= G234), S277 (= S278), P304 (= P305)
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)
60% identity, 94% coverage: 18:320/322 of query aligns to 81:381/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
60% identity, 95% coverage: 15:320/322 of query aligns to 6:309/309 of 7n2tA
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
58% identity, 96% coverage: 12:320/322 of query aligns to 4:309/310 of 5xoqA
- binding : T72 (= T83), S73 (= S84), G74 (= G85), T76 (= T87), M123 (= M134), Q144 (= Q156), R218 (≠ P229), H219 (= H230), Q222 (= Q233), G223 (= G234), A226 (= A237)
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)
58% identity, 96% coverage: 11:318/322 of query aligns to 4:309/322 of P47998
- K46 (= K55) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T83) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S84) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N86) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T87) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q156) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H166) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (≠ A171) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 190:194) binding pyridoxal 5'-phosphate
- T182 (= T191) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T194) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ A226) 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 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)
58% identity, 96% coverage: 11:318/322 of query aligns to 2:307/320 of 2isqA
- active site: K44 (= K55), S267 (= S278)
- binding pyridoxal-5'-phosphate: K44 (= K55), N75 (= N86), G177 (= G188), G179 (= G190), T180 (= T191), G181 (= G192), T183 (= T194), G223 (= G234), S267 (= S278), P294 (= P305)
- binding : T72 (= T83), S73 (= S84), G74 (= G85), T76 (= T87), G122 (= G133), M123 (= M134), K124 (= K135), G217 (= G228), P218 (= P229), H219 (= H230), Q222 (= Q233), G223 (= G234)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
58% identity, 96% coverage: 11:318/322 of query aligns to 2:307/320 of 1z7yA
- active site: A44 (≠ K55), S267 (= S278)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G85), N75 (= N86), T76 (= T87), Q145 (= Q156), I178 (= I189), G179 (= G190), T180 (= T191), G181 (= G192), T183 (= T194), G223 (= G234), S267 (= S278), P294 (= P305), S295 (= S306)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
56% identity, 93% coverage: 20:317/322 of query aligns to 15:310/341 of Q93244
- P75 (= P82) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A95) mutation to V: In n5522; severe loss of protein stability.
- S144 (≠ A151) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (= G188) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G190) mutation to R: In n5515; severe loss of protein stability.
- G229 (= G236) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (≠ L266) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (≠ A279) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (≠ V302) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
52% identity, 95% coverage: 15:320/322 of query aligns to 14:317/329 of 3vbeC
- active site: K52 (= K55), S81 (= S84), E212 (= E215), S216 (= S219), S275 (= S278), P302 (= P305)
- binding pyridoxal-5'-phosphate: K52 (= K55), N83 (= N86), M184 (≠ S187), G187 (= G190), S188 (≠ T191), G189 (= G192), T191 (= T194), G231 (= G234), S275 (= S278), P302 (= P305)
3vc3A Crystal structure of beta-cyanoalanine synthase k95a mutant in soybean (see paper)
52% identity, 95% coverage: 15:320/322 of query aligns to 7:310/322 of 3vc3A
- active site: A45 (≠ K55), S268 (= S278), P295 (= P305)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-cysteine: T73 (= T83), S74 (= S84), N76 (= N86), M77 (≠ T87), Q146 (= Q156), M177 (≠ S187), G180 (= G190), S181 (≠ T191), G182 (= G192), T184 (= T194), G224 (= G234), S268 (= S278), P295 (= P305)
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, 96% coverage: 11:320/322 of query aligns to 3:315/323 of P0ABK5
- K42 (= K55) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Still stimulates tRNase activity of CdiA-CT in vitro and in vivo.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
54% identity, 96% coverage: 11:320/322 of query aligns to 4:316/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K55), N73 (= N86), V177 (≠ I189), G178 (= G190), T179 (= T191), G180 (= G192), T182 (= T194), G230 (= G234), S274 (= S278), P301 (= P305)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K55), T70 (= T83), G72 (= G85), N73 (= N86), T74 (= T87), Q144 (= Q156), F145 (= F157), Q229 (= Q233), G230 (= G234), I231 (= I235), A233 (= A237)
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, 96% coverage: 11:320/322 of query aligns to 3:315/323 of P0A1E3
- N72 (= N86) binding pyridoxal 5'-phosphate
- S273 (= S278) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
50% identity, 94% coverage: 15:317/322 of query aligns to 12:311/329 of 8b9wA
Query Sequence
>WP_012067744.1 NCBI__GCF_000017145.1:WP_012067744.1
MSEARKPGRGRVFSSITETIGDTPIVRLDKLAKEKGVKANLLAKLEFFNPIGSVKDRIGV
AMIESLEEQGKITPGRTTLVEPTSGNTGIALAFVAAAKGYRLILTMPETMSVERRKMLAL
LGAELVLTEGAKGMKGAIAKAQELTETLPDAIIPQQFENPANPEIHRQTTAEEIWNDTEG
AVDILVSGIGTGGTITGAGQVLKARKPSLRVIAVEPEESPILSGGAPGPHKIQGIGAGFA
PAILDTSVYDEVVTVNAGEAVETARLVARLEGVPVGISAGAALQAAIEIGQREENAGKNI
VVIIPSFAERYLSTVLFEGLGA
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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