SitesBLAST
Comparing WP_012589229.1 NCBI__GCF_000021745.1:WP_012589229.1 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, 94% coverage: 22:331/331 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)
61% identity, 92% coverage: 23:328/331 of query aligns to 3:305/310 of P9WP55
- K44 (= K66) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N97) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 201:205) binding pyridoxal 5'-phosphate
- S266 (= S289) 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)
61% identity, 92% coverage: 23:328/331 of query aligns to 3:305/306 of 2q3dA
- active site: K44 (= K66), S266 (= S289), P293 (= P316)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K66), T71 (= T94), S72 (= S95), N74 (= N97), T75 (= T98), Q144 (= Q167), V177 (= V200), G178 (= G201), T179 (= T202), G180 (= G203), T182 (= T205), G222 (= G245), I223 (= I246), S266 (= S289), P293 (= P316), D294 (≠ S317)
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
61% identity, 93% coverage: 23:329/331 of query aligns to 3:309/310 of 4lmbA
- active site: K46 (= K66), S269 (= S289)
- binding cysteine: K46 (= K66), T74 (= T94), S75 (= S95), N77 (= N97), T78 (= T98), M101 (= M121), M125 (= M145), M125 (= M145), Q147 (= Q167), F148 (= F168), Q224 (= Q244), G225 (= G245), G225 (= G245), I226 (= I246), A228 (= A248)
- binding pyridoxal-5'-phosphate: K46 (= K66), N77 (= N97), V180 (= V200), G181 (= G201), T182 (= T202), G183 (= G203), T185 (= T205), G225 (= G245), S269 (= S289), P296 (= P316)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
61% identity, 91% coverage: 23:323/331 of query aligns to 3:300/300 of 3zeiA
- active site: K44 (= K66), S266 (= S289), P293 (= P316)
- 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 (= T94), S72 (= S95), I126 (= I149), Q144 (= Q167), F145 (= F168), K215 (≠ A238), G222 (= G245), A225 (= A248), F227 (= F250)
- binding pyridoxal-5'-phosphate: K44 (= K66), N74 (= N97), V177 (= V200), G178 (= G201), T179 (= T202), G180 (= G203), T182 (= T205), G222 (= G245), S266 (= S289), P293 (= P316), D294 (≠ S317)
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)
61% identity, 91% coverage: 23:323/331 of query aligns to 3:300/300 of 2q3cA
- active site: K44 (= K66), S266 (= S289), P293 (= P316)
- binding : T71 (= T94), S72 (= S95), G73 (= G96), T75 (= T98), M122 (= M145), Q144 (= Q167), K215 (≠ A238), G222 (= G245), A225 (= A248)
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
57% identity, 94% coverage: 22:331/331 of query aligns to 12:319/323 of 4aecA
- active site: K54 (= K66), S277 (= S289)
- binding pyridoxal-5'-phosphate: K54 (= K66), N85 (= N97), I188 (≠ V200), G189 (= G201), T190 (= T202), G191 (= G203), G192 (= G204), T193 (= T205), G233 (= G245), S277 (= S289), P304 (= P316)
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)
58% identity, 93% coverage: 23:331/331 of query aligns to 75:381/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
60% identity, 95% coverage: 16:331/331 of query aligns to 1:309/310 of 5xoqA
- binding : T72 (= T94), S73 (= S95), G74 (= G96), T76 (= T98), M123 (= M145), Q144 (= Q167), R218 (≠ P240), H219 (= H241), Q222 (= Q244), G223 (= G245), A226 (= A248)
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
59% identity, 93% coverage: 23:329/331 of query aligns to 3:307/309 of 7n2tA
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, 93% coverage: 22:329/331 of query aligns to 4:309/322 of P47998
- K46 (= K66) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T94) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S95) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N97) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T98) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q167) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H177) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (≠ A182) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 201:205) binding pyridoxal 5'-phosphate
- T182 (= T202) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T205) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ Q237) mutation to A: Impaired interaction with SAT1.
- H221 (= H241) mutation to A: Impaired interaction with SAT1.
- K222 (= K242) mutation to A: Impaired interaction with SAT1.
- S269 (= S289) 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, 93% coverage: 22:329/331 of query aligns to 2:307/320 of 2isqA
- active site: K44 (= K66), S267 (= S289)
- binding pyridoxal-5'-phosphate: K44 (= K66), N75 (= N97), G177 (= G199), G179 (= G201), T180 (= T202), G181 (= G203), T183 (= T205), G223 (= G245), S267 (= S289), P294 (= P316)
- binding : T72 (= T94), S73 (= S95), G74 (= G96), T76 (= T98), G122 (= G144), M123 (= M145), K124 (= K146), G217 (= G239), P218 (= P240), H219 (= H241), Q222 (= Q244), G223 (= G245)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
58% identity, 93% coverage: 22:329/331 of query aligns to 2:307/320 of 1z7yA
- active site: A44 (≠ K66), S267 (= S289)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G96), N75 (= N97), T76 (= T98), Q145 (= Q167), I178 (≠ V200), G179 (= G201), T180 (= T202), G181 (= G203), T183 (= T205), G223 (= G245), S267 (= S289), P294 (= P316), S295 (= S317)
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
55% identity, 92% coverage: 26:328/331 of query aligns to 12:311/329 of 8b9wA
3t4pA Crystal structure of o-acetyl serine sulfhydrylase from leishmania donovani in complex with designed tetrapeptide (see paper)
54% identity, 94% coverage: 22:331/331 of query aligns to 9:315/319 of 3t4pA
- active site: K50 (= K66), S273 (= S289)
- binding : S78 (≠ T94), S79 (= S95), G80 (= G96), T82 (= T98), M129 (= M145), Q151 (= Q167), F152 (= F168), G223 (= G239), P224 (= P240), H225 (= H241), G229 (= G245), G231 (= G247), P232 (≠ A248)
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
51% identity, 94% coverage: 22:331/331 of query aligns to 10:317/329 of 3vbeC
- active site: K52 (= K66), S81 (= S95), E212 (= E226), S216 (= S230), S275 (= S289), P302 (= P316)
- binding pyridoxal-5'-phosphate: K52 (= K66), N83 (= N97), M184 (≠ A198), G187 (= G201), S188 (≠ T202), G189 (= G203), T191 (= T205), G231 (= G245), S275 (= S289), P302 (= P316)
8b9yC Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
53% identity, 94% coverage: 20:331/331 of query aligns to 7:315/330 of 8b9yC
3vc3A Crystal structure of beta-cyanoalanine synthase k95a mutant in soybean (see paper)
51% identity, 94% coverage: 22:331/331 of query aligns to 3:310/322 of 3vc3A
- active site: A45 (≠ K66), S268 (= S289), P295 (= P316)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-cysteine: T73 (= T94), S74 (= S95), N76 (= N97), M77 (≠ T98), Q146 (= Q167), M177 (≠ A198), G180 (= G201), S181 (≠ T202), G182 (= G203), T184 (= T205), G224 (= G245), S268 (= S289), P295 (= P316)
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)
57% identity, 94% coverage: 22:331/331 of query aligns to 3:315/323 of P0A1E3
- N72 (= N97) binding pyridoxal 5'-phosphate
- S273 (= S289) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
57% identity, 94% coverage: 22:331/331 of query aligns to 4:316/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K66), N73 (= N97), V177 (= V200), G178 (= G201), T179 (= T202), G180 (= G203), T182 (= T205), G230 (= G245), S274 (= S289), P301 (= P316)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K66), T70 (= T94), G72 (= G96), N73 (= N97), T74 (= T98), Q144 (= Q167), F145 (= F168), Q229 (= Q244), G230 (= G245), I231 (= I246), A233 (= A248)
Query Sequence
>WP_012589229.1 NCBI__GCF_000021745.1:WP_012589229.1
MAQSAVRPAEAAVTEHVPGRGRIYDSITETIGDTPLVRLSKIEKEKGLKAHLLAKLEFFN
PLASVKDRIGEHMISTLEAEGKITPGKTTLIEPTSGNTGIALAFVAAARGYKLILVMPES
MSIERRKMLALLGAELVLTPAAQGMKGAIAKAQELVDSTPNSWIPKQFDNPANVEIHKKT
TAEEIWNDTKGEIDIFVAGVGTGGTITGVGTVLKPRRPGLKIVAVEPEDSPVLSGGQAGP
HKIQGIGAGFVPSILDRSVIDEVVTVGNQTAFDTARLLARLEGIPVGISSGAAVAAAVEI
ALRPESEGKTIVIIIPSFAERYLSTALFEGL
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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