SitesBLAST
Comparing WP_013553123.1 NCBI__GCF_000186245.1:WP_013553123.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
57% identity, 99% coverage: 2:302/303 of query aligns to 3:305/306 of 2q3dA
- active site: K44 (= K41), S266 (= S263), P293 (= P290)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K41), T71 (= T68), S72 (= S69), N74 (= N71), T75 (= T72), Q144 (= Q141), V177 (= V174), G178 (= G175), T179 (= T176), G180 (= G177), T182 (= T179), G222 (= G219), I223 (= I220), S266 (= S263), P293 (= P290), D294 (= D291)
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)
57% identity, 99% coverage: 2:302/303 of query aligns to 3:305/310 of P9WP55
- K44 (= K41) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N71) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 175:179) binding pyridoxal 5'-phosphate
- S266 (= S263) binding pyridoxal 5'-phosphate
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
57% identity, 98% coverage: 2:297/303 of query aligns to 3:300/300 of 3zeiA
- active site: K44 (= K41), S266 (= S263), P293 (= P290)
- 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 (= T68), S72 (= S69), I126 (= I123), Q144 (= Q141), F145 (= F142), K215 (≠ A212), G222 (= G219), A225 (= A222), F227 (= F224)
- binding pyridoxal-5'-phosphate: K44 (= K41), N74 (= N71), V177 (= V174), G178 (= G175), T179 (= T176), G180 (= G177), T182 (= T179), G222 (= G219), S266 (= S263), P293 (= P290), D294 (= D291)
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)
57% identity, 98% coverage: 2:297/303 of query aligns to 3:300/300 of 2q3cA
- active site: K44 (= K41), S266 (= S263), P293 (= P290)
- binding : T71 (= T68), S72 (= S69), G73 (= G70), T75 (= T72), M122 (= M119), Q144 (= Q141), K215 (≠ A212), G222 (= G219), A225 (= A222)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
55% identity, 100% coverage: 2:303/303 of query aligns to 4:307/310 of 5xoqA
- binding : T72 (= T68), S73 (= S69), G74 (= G70), T76 (= T72), M123 (= M119), Q144 (= Q141), R218 (≠ P214), H219 (= H215), Q222 (= Q218), G223 (= G219), A226 (= A222)
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
51% identity, 100% coverage: 2:303/303 of query aligns to 3:309/318 of 4lmaA
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, 99% coverage: 2:302/303 of query aligns to 4:312/323 of P0ABK5
- K42 (= K41) 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
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
51% identity, 100% coverage: 2:303/303 of query aligns to 13:317/323 of 4aecA
- active site: K54 (= K41), S277 (= S263)
- binding pyridoxal-5'-phosphate: K54 (= K41), N85 (= N71), I188 (≠ V174), G189 (= G175), T190 (= T176), G191 (= G177), G192 (= G178), T193 (= T179), G233 (= G219), S277 (= S263), P304 (= P290)
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
53% identity, 99% coverage: 2:302/303 of query aligns to 5:313/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K41), N73 (= N71), V177 (= V174), G178 (= G175), T179 (= T176), G180 (= G177), T182 (= T179), G230 (= G219), S274 (= S263), P301 (= P290)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K41), T70 (= T68), G72 (= G70), N73 (= N71), T74 (= T72), Q144 (= Q141), F145 (= F142), Q229 (= Q218), G230 (= G219), I231 (= I220), A233 (= A222)
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)
53% identity, 99% coverage: 2:302/303 of query aligns to 4:312/323 of P0A1E3
- N72 (= N71) binding pyridoxal 5'-phosphate
- S273 (= S263) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
52% identity, 100% coverage: 2:303/303 of query aligns to 75:379/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
52% identity, 99% coverage: 2:302/303 of query aligns to 3:311/322 of 1d6sA
- active site: A41 (≠ K41), G228 (= G219)
- binding methionine: T68 (= T68), N69 (≠ S69), N71 (= N71), T72 (= T72), Q142 (= Q141), F143 (= F142), G176 (= G175), G228 (= G219)
- binding pyridoxal-5'-phosphate: N71 (= N71), G176 (= G175), T177 (= T176), G178 (= G177), T180 (= T179), G228 (= G219), S272 (= S263), P299 (= P290)
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
52% identity, 100% coverage: 2:303/303 of query aligns to 3:307/309 of 7n2tA
3t4pA Crystal structure of o-acetyl serine sulfhydrylase from leishmania donovani in complex with designed tetrapeptide (see paper)
51% identity, 98% coverage: 6:302/303 of query aligns to 14:312/319 of 3t4pA
- active site: K50 (= K41), S273 (= S263)
- binding : S78 (≠ T68), S79 (= S69), G80 (= G70), T82 (= T72), M129 (= M119), Q151 (= Q141), F152 (= F142), G223 (= G213), P224 (= P214), H225 (= H215), G229 (= G219), G231 (= G221), P232 (≠ A222)
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)
51% identity, 100% coverage: 2:303/303 of query aligns to 5:309/322 of P47998
- K46 (= K41) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T68) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S69) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N71) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T72) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q141) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H151) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (≠ A156) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 175:179) binding pyridoxal 5'-phosphate
- T182 (= T176) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T179) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ E211) mutation to A: Impaired interaction with SAT1.
- H221 (= H215) mutation to A: Impaired interaction with SAT1.
- K222 (= K216) mutation to A: Impaired interaction with SAT1.
- S269 (= S263) 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)
51% identity, 100% coverage: 2:303/303 of query aligns to 3:307/320 of 2isqA
- active site: K44 (= K41), S267 (= S263)
- binding pyridoxal-5'-phosphate: K44 (= K41), N75 (= N71), G177 (≠ A173), G179 (= G175), T180 (= T176), G181 (= G177), T183 (= T179), G223 (= G219), S267 (= S263), P294 (= P290)
- binding : T72 (= T68), S73 (= S69), G74 (= G70), T76 (= T72), G122 (= G118), M123 (= M119), K124 (≠ Q120), G217 (= G213), P218 (= P214), H219 (= H215), Q222 (= Q218), G223 (= G219)
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
50% identity, 100% coverage: 2:303/303 of query aligns to 3:307/320 of 1z7yA
- active site: A44 (≠ K41), S267 (= S263)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G70), N75 (= N71), T76 (= T72), Q145 (= Q141), I178 (≠ V174), G179 (= G175), T180 (= T176), G181 (= G177), T183 (= T179), G223 (= G219), S267 (= S263), P294 (= P290), S295 (≠ D291)
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
48% identity, 100% coverage: 1:303/303 of query aligns to 2:309/310 of 4lmbA
- active site: K46 (= K41), S269 (= S263)
- binding cysteine: K46 (= K41), T74 (= T68), S75 (= S69), N77 (= N71), T78 (= T72), M101 (= M95), M125 (= M119), M125 (= M119), Q147 (= Q141), F148 (= F142), Q224 (= Q218), G225 (= G219), G225 (= G219), I226 (= I220), A228 (= A222)
- binding pyridoxal-5'-phosphate: K46 (= K41), N77 (= N71), V180 (= V174), G181 (= G175), T182 (= T176), G183 (= G177), T185 (= T179), G225 (= G219), S269 (= S263), P296 (= P290)
8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
50% identity, 97% coverage: 10:302/303 of query aligns to 17:311/329 of 8b9wA
1fcjA Crystal structure of oass complexed with chloride and sulfate (see paper)
51% identity, 96% coverage: 2:292/303 of query aligns to 3:301/302 of 1fcjA
- active site: K41 (= K41), G228 (= G219), S272 (= S263)
- binding pyridoxal-5'-phosphate: K41 (= K41), N71 (= N71), V175 (= V174), G176 (= G175), T177 (= T176), G178 (= G177), T180 (= T179), G228 (= G219), S272 (= S263), P299 (= P290)
- binding sulfate ion: G70 (= G70), T72 (= T72), Q142 (= Q141)
Query Sequence
>WP_013553123.1 NCBI__GCF_000186245.1:WP_013553123.1
MIFDDIQQTIGQTPLIRLAYLSNNATILAKAEYFNPGSSIKDRVAKSMIDGAMERGELDA
ETVVIEPTSGNTGIGLALVCAVRGLRLILTMPESMSLERRKLLRHLGAELVLTPAAEGMQ
GAIEEARRLAASFEKSFIPDQFANPDNPAAHERGTAQEILEATGGAVNIFVAAVGTGGTL
SGNGRALKAANPKLRLVAVEPAASPAISRGEAGPHKIQGIGAGFVPDNLDLDLVDEVLTV
TDEEAIAFAREAARKAGLLVGISSGANLAAAYRLAQREENRGKTIVTVLPDTAERYLSTE
LFE
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