SitesBLAST
Comparing WP_013419965.1 NCBI__GCF_000166055.1:WP_013419965.1 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)
63% identity, 96% coverage: 13:322/322 of query aligns to 3:309/310 of P9WP55
- K44 (= K56) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N87) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 191:195) binding pyridoxal 5'-phosphate
- S266 (= S279) 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)
64% identity, 95% coverage: 13:318/322 of query aligns to 3:305/306 of 2q3dA
- active site: K44 (= K56), S266 (= S279), P293 (= P306)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K56), T71 (= T84), S72 (= S85), N74 (= N87), T75 (= T88), Q144 (= Q157), V177 (≠ I190), G178 (= G191), T179 (= T192), G180 (= G193), T182 (= T195), G222 (= G235), I223 (= I236), S266 (= S279), P293 (= P306), D294 (≠ S307)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
59% identity, 96% coverage: 12:321/322 of query aligns to 2:311/318 of 4lmaA
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
63% identity, 93% coverage: 13:313/322 of query aligns to 3:300/300 of 3zeiA
- active site: K44 (= K56), S266 (= S279), P293 (= P306)
- 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 (= T84), S72 (= S85), I126 (≠ V139), Q144 (= Q157), F145 (= F158), K215 (≠ P228), G222 (= G235), A225 (= A238), F227 (= F240)
- binding pyridoxal-5'-phosphate: K44 (= K56), N74 (= N87), V177 (≠ I190), G178 (= G191), T179 (= T192), G180 (= G193), T182 (= T195), G222 (= G235), S266 (= S279), P293 (= P306), D294 (≠ S307)
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)
63% identity, 93% coverage: 13:313/322 of query aligns to 3:300/300 of 2q3cA
- active site: K44 (= K56), S266 (= S279), P293 (= P306)
- binding : T71 (= T84), S72 (= S85), G73 (= G86), T75 (= T88), M122 (= M135), Q144 (= Q157), K215 (≠ P228), G222 (= G235), A225 (= A238)
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
61% identity, 95% coverage: 13:319/322 of query aligns to 3:309/310 of 4lmbA
- active site: K46 (= K56), S269 (= S279)
- binding cysteine: K46 (= K56), T74 (= T84), S75 (= S85), N77 (= N87), T78 (= T88), M101 (= M111), M125 (= M135), M125 (= M135), Q147 (= Q157), F148 (= F158), Q224 (= Q234), G225 (= G235), G225 (= G235), I226 (= I236), A228 (= A238)
- binding pyridoxal-5'-phosphate: K46 (= K56), N77 (= N87), V180 (≠ I190), G181 (= G191), T182 (= T192), G183 (= G193), T185 (= T195), G225 (= G235), S269 (= S279), P296 (= P306)
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
59% identity, 96% coverage: 13:321/322 of query aligns to 13:319/323 of 4aecA
- active site: K54 (= K56), S277 (= S279)
- binding pyridoxal-5'-phosphate: K54 (= K56), N85 (= N87), I188 (= I190), G189 (= G191), T190 (= T192), G191 (= G193), G192 (= G194), T193 (= T195), G233 (= G235), S277 (= S279), P304 (= P306)
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: 19:321/322 of query aligns to 81:381/392 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
59% identity, 96% coverage: 13:321/322 of query aligns to 4:309/310 of 5xoqA
- binding : T72 (= T84), S73 (= S85), G74 (= G86), T76 (= T88), M123 (= M135), Q144 (= Q157), R218 (≠ P230), H219 (= H231), Q222 (= Q234), G223 (= G235), A226 (= A238)
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)
60% identity, 96% coverage: 12:319/322 of query aligns to 4:309/322 of P47998
- K46 (= K56) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T84) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S85) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N87) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T88) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q157) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H167) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (≠ A172) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 191:195) binding pyridoxal 5'-phosphate
- T182 (= T192) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T195) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ N227) mutation to A: Impaired interaction with SAT1.
- H221 (= H231) mutation to A: Impaired interaction with SAT1.
- K222 (= K232) mutation to A: Impaired interaction with SAT1.
- S269 (= S279) 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)
60% identity, 96% coverage: 12:319/322 of query aligns to 2:307/320 of 2isqA
- active site: K44 (= K56), S267 (= S279)
- binding pyridoxal-5'-phosphate: K44 (= K56), N75 (= N87), G177 (= G189), G179 (= G191), T180 (= T192), G181 (= G193), T183 (= T195), G223 (= G235), S267 (= S279), P294 (= P306)
- binding : T72 (= T84), S73 (= S85), G74 (= G86), T76 (= T88), G122 (= G134), M123 (= M135), K124 (= K136), G217 (= G229), P218 (= P230), H219 (= H231), Q222 (= Q234), G223 (= G235)
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
59% identity, 95% coverage: 17:321/322 of query aligns to 7:309/309 of 7n2tA
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
59% identity, 96% coverage: 12:319/322 of query aligns to 2:307/320 of 1z7yA
- active site: A44 (≠ K56), S267 (= S279)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G86), N75 (= N87), T76 (= T88), Q145 (= Q157), I178 (= I190), G179 (= G191), T180 (= T192), G181 (= G193), T183 (= T195), G223 (= G235), S267 (= S279), P294 (= P306), S295 (= S307)
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
54% identity, 94% coverage: 16:318/322 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)
53% identity, 95% coverage: 16:321/322 of query aligns to 13:315/319 of 3t4pA
- active site: K50 (= K56), S273 (= S279)
- binding : S78 (≠ T84), S79 (= S85), G80 (= G86), T82 (= T88), M129 (= M135), Q151 (= Q157), F152 (= F158), G223 (= G229), P224 (= P230), H225 (= H231), G229 (= G235), G231 (= G237), P232 (≠ A238)
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)
55% identity, 96% coverage: 12:321/322 of query aligns to 3:315/323 of P0A1E3
- N72 (= N87) binding pyridoxal 5'-phosphate
- S273 (= S279) 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)
55% identity, 96% coverage: 12:321/322 of query aligns to 4:316/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K56), N73 (= N87), V177 (≠ I190), G178 (= G191), T179 (= T192), G180 (= G193), T182 (= T195), G230 (= G235), S274 (= S279), P301 (= P306)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K56), T70 (= T84), G72 (= G86), N73 (= N87), T74 (= T88), Q144 (= Q157), F145 (= F158), Q229 (= Q234), G230 (= G235), I231 (= I236), A233 (= A238)
8b9yC Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
51% identity, 97% coverage: 10:321/322 of query aligns to 7:315/330 of 8b9yC
1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
54% identity, 96% coverage: 12:321/322 of query aligns to 2:314/322 of 1d6sA
- active site: A41 (≠ K56), G228 (= G235)
- binding methionine: T68 (= T84), N69 (≠ S85), N71 (= N87), T72 (= T88), Q142 (= Q157), F143 (= F158), G176 (= G191), G228 (= G235)
- binding pyridoxal-5'-phosphate: N71 (= N87), G176 (= G191), T177 (= T192), G178 (= G193), T180 (= T195), G228 (= G235), S272 (= S279), P299 (= P306)
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
52% identity, 95% coverage: 17:321/322 of query aligns to 15:317/329 of 3vbeC
- active site: K52 (= K56), S81 (= S85), E212 (= E216), S216 (= S220), S275 (= S279), P302 (= P306)
- binding pyridoxal-5'-phosphate: K52 (= K56), N83 (= N87), M184 (≠ S188), G187 (= G191), S188 (≠ T192), G189 (= G193), T191 (= T195), G231 (= G235), S275 (= S279), P302 (= P306)
Query Sequence
>WP_013419965.1 NCBI__GCF_000166055.1:WP_013419965.1
MAEKNHAPGRGRIYGSITETIGDTPIVRLDKLAKEKGVKANLLAKLEFFNPIASVKDRIG
VSLIDALEKQGKIEPGKNTLIEPTSGNTGIALAFVAAARGYKLILVMPETMSIERRKMLA
LLGAELVLTPGAQGMKGAVAKANELLGEYPNAVVPQQFENPANPEIHRRTTAEEIWNDTE
HKVDIVVSGIGTGGTITGVGQVLKPRKPSLKIIAVEPEESPVLSGGNPGPHKIQGIGAGF
VPGVLDRDVIDEIVKVNSATALETARHVARLEGIPVGISSGAAIAAAIEVGSRPENAGKN
IVIIVPSFAERYLSTALFEGLA
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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