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Comparing CCNA_03740 FitnessBrowser__Caulo:CCNA_03740 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)
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, 93% coverage: 21:325/328 of query aligns to 3:305/306 of 2q3dA
- active site: K44 (= K64), S266 (= S286), P293 (= P313)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K64), T71 (= T91), S72 (= S92), N74 (= N94), T75 (= T95), Q144 (= Q164), V177 (= V197), G178 (= G198), T179 (= T199), G180 (= G200), T182 (= T202), G222 (= G242), I223 (= I243), S266 (= S286), P293 (= P313), D294 (≠ S314)
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, 93% coverage: 21:325/328 of query aligns to 3:305/310 of P9WP55
- K44 (= K64) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N94) binding
- GTGGT 178:182 (= GTGGT 198:202) binding
- S266 (= S286) binding
4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
58% identity, 94% coverage: 20:328/328 of query aligns to 2:311/318 of 4lmaA
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
60% identity, 93% coverage: 21:325/328 of query aligns to 3:308/310 of 4lmbA
- active site: K46 (= K64), S269 (= S286)
- binding cysteine: K46 (= K64), T74 (= T91), S75 (= S92), N77 (= N94), T78 (= T95), M101 (= M118), M125 (= M142), M125 (= M142), Q147 (= Q164), F148 (= F165), Q224 (= Q241), G225 (= G242), G225 (= G242), I226 (= I243), A228 (= A245)
- binding pyridoxal-5'-phosphate: K46 (= K64), N77 (= N94), V180 (= V197), G181 (= G198), T182 (= T199), G183 (= G200), T185 (= T202), G225 (= G242), S269 (= S286), P296 (= P313)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
60% identity, 91% coverage: 21:320/328 of query aligns to 3:300/300 of 3zeiA
- active site: K44 (= K64), S266 (= S286), P293 (= P313)
- 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 (= T91), S72 (= S92), I126 (≠ V146), Q144 (= Q164), F145 (= F165), K215 (≠ P235), G222 (= G242), A225 (= A245), F227 (= F247)
- binding pyridoxal-5'-phosphate: K44 (= K64), N74 (= N94), V177 (= V197), G178 (= G198), T179 (= T199), G180 (= G200), T182 (= T202), G222 (= G242), S266 (= S286), P293 (= P313), D294 (≠ S314)
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, 91% coverage: 21:320/328 of query aligns to 3:300/300 of 2q3cA
- active site: K44 (= K64), S266 (= S286), P293 (= P313)
- binding : T71 (= T91), S72 (= S92), G73 (= G93), T75 (= T95), M122 (= M142), Q144 (= Q164), K215 (≠ P235), G222 (= G242), A225 (= A245)
5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
58% identity, 94% coverage: 21:328/328 of query aligns to 4:309/310 of 5xoqA
- binding : T72 (= T91), S73 (= S92), G74 (= G93), T76 (= T95), M123 (= M142), Q144 (= Q164), R218 (≠ P237), H219 (= H238), Q222 (= Q241), G223 (= G242), A226 (= A245)
2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
56% identity, 94% coverage: 20:326/328 of query aligns to 2:307/320 of 2isqA
- active site: K44 (= K64), S267 (= S286)
- binding pyridoxal-5'-phosphate: K44 (= K64), N75 (= N94), G177 (= G196), G179 (= G198), T180 (= T199), G181 (= G200), T183 (= T202), G223 (= G242), S267 (= S286), P294 (= P313)
- binding : T72 (= T91), S73 (= S92), G74 (= G93), T76 (= T95), G122 (= G141), M123 (= M142), K124 (≠ R143), G217 (= G236), P218 (= P237), H219 (= H238), Q222 (= Q241), G223 (= G242)
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)
56% identity, 94% coverage: 20:326/328 of query aligns to 4:309/322 of P47998
- K46 (= K64) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
- T74 (= T91) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
- S75 (= S92) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
- N77 (= N94) binding ; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
- T78 (= T95) mutation T->A,S: Reduction of cysteine synthase activity.
- Q147 (= Q164) mutation Q->A,E: Strong reduction of cysteine synthase activity.
- H157 (= H174) mutation H->Q,N: Slight reduction of cysteine synthase activity.
- G162 (≠ A179) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
- GTGGT 181:185 (= GTGGT 198:202) binding
- T182 (= T199) mutation T->A,S: Slight reduction of cysteine synthase activity.
- T185 (= T202) mutation T->A,S: Strong reduction of cysteine synthase activity.
- K217 (≠ A234) mutation to A: Impaired interaction with SAT1.
- H221 (= H238) mutation to A: Impaired interaction with SAT1.
- K222 (= K239) mutation to A: Impaired interaction with SAT1.
- S269 (= S286) binding ; mutation to A: Strong reduction of cysteine synthase activity.; mutation to T: Reduction of cysteine synthase activity.
1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
56% identity, 94% coverage: 20:326/328 of query aligns to 2:307/320 of 1z7yA
- active site: A44 (≠ K64), S267 (= S286)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G93), N75 (= N94), T76 (= T95), Q145 (= Q164), I178 (≠ V197), G179 (= G198), T180 (= T199), G181 (= G200), T183 (= T202), G223 (= G242), S267 (= S286), P294 (= P313), S295 (= S314)
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, 94% coverage: 20:328/328 of query aligns to 3:315/323 of P0A1E3
- N72 (= N94) binding
- S273 (= S286) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6z4nAAA structure of oass complexed with upar inhibitor (see paper)
55% identity, 94% coverage: 20:328/328 of query aligns to 4:316/321 of 6z4nAAA
- binding pyridoxal-5'-phosphate: K43 (= K64), N73 (= N94), V177 (= V197), G178 (= G198), T179 (= T199), G180 (= G200), T182 (= T202), G230 (= G242), S274 (= S286), P301 (= P313)
- binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K64), T70 (= T91), G72 (= G93), N73 (= N94), T74 (= T95), Q144 (= Q164), F145 (= F165), Q229 (= Q241), G230 (= G242), I231 (= I243), A233 (= A245)
1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
54% identity, 94% coverage: 20:328/328 of query aligns to 2:314/322 of 1d6sA
- active site: A41 (≠ K64), G228 (= G242)
- binding methionine: T68 (= T91), N69 (≠ S92), N71 (= N94), T72 (= T95), Q142 (= Q164), F143 (= F165), G176 (= G198), G228 (= G242)
- binding pyridoxal-5'-phosphate: N71 (= N94), G176 (= G198), T177 (= T199), G178 (= G200), T180 (= T202), G228 (= G242), S272 (= S286), P299 (= P313)
7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
54% identity, 94% coverage: 21:328/328 of query aligns to 3:309/309 of 7n2tA
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)
53% identity, 94% coverage: 20:328/328 of query aligns to 3:315/323 of P0ABK5
- K42 (= K64) 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
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)
54% identity, 94% coverage: 21:328/328 of query aligns to 75:381/392 of P47999
Sites not aligning to the query:
- 61 modified: N-acetylalanine
4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
52% identity, 94% coverage: 21:328/328 of query aligns to 13:319/323 of 4aecA
- active site: K54 (= K64), S277 (= S286)
- binding pyridoxal-5'-phosphate: K54 (= K64), N85 (= N94), I188 (≠ V197), G189 (= G198), T190 (= T199), G191 (= G200), G192 (= G201), T193 (= T202), G233 (= G242), S277 (= S286), P304 (= P313)
3t4pA Crystal structure of o-acetyl serine sulfhydrylase from leishmania donovani in complex with designed tetrapeptide (see paper)
50% identity, 93% coverage: 20:325/328 of query aligns to 9:312/319 of 3t4pA
- active site: K50 (= K64), S273 (= S286)
- binding : S78 (≠ T91), S79 (= S92), G80 (= G93), T82 (= T95), M129 (= M142), Q151 (= Q164), F152 (= F165), G223 (= G236), P224 (= P237), H225 (= H238), G229 (= G242), G231 (= G244), P232 (≠ A245)
1fcjA Crystal structure of oass complexed with chloride and sulfate (see paper)
54% identity, 90% coverage: 20:314/328 of query aligns to 2:300/302 of 1fcjA
- active site: K41 (= K64), G228 (= G242), S272 (= S286)
- binding pyridoxal-5'-phosphate: K41 (= K64), N71 (= N94), V175 (= V197), G176 (= G198), T177 (= T199), G178 (= G200), T180 (= T202), G228 (= G242), S272 (= S286), P299 (= P313)
- binding sulfate ion: G70 (= G93), T72 (= T95), Q142 (= Q164)
Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
51% identity, 95% coverage: 16:325/328 of query aligns to 2:310/341 of Q93244
- P75 (= P90) mutation to L: In n5537; severe loss of protein stability.
- A88 (= A103) mutation to V: In n5522; severe loss of protein stability.
- S144 (≠ A159) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
- G181 (= G196) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
- G183 (= G198) mutation to R: In n5515; severe loss of protein stability.
- G229 (= G244) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
- R259 (= R274) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
- S272 (= S287) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
- T295 (≠ V310) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.
Query Sequence
>CCNA_03740 FitnessBrowser__Caulo:CCNA_03740
MDDASSLYDAARFKRAGRGKIYDSIIDTIGDTPLVRLPRLSAELNPKAEVLAKLEFFNPI
ASVKDRIGVSMIESLEAQGVLKPGATIIEPTSGNTGIALAFVAAAKGYKLTLVMPESMSI
ERRKMLLLLGAKLELTPAEKGMRGAVTRAQELIEATPGAVMPQQFENSANPLIHRVSTAE
EIWNDTAGAVDAVVSGVGTGGTITGVGQALKARKPSLKMVAVEPEASPVLSGGAPGPHKI
QGIGAGFVPGVLDRGVIDDIVQVSNDDAFAMARRAAATEGLPVGISSGAALTAAFDLALR
DAYKGKTIVVIIPSFAERYLSTALFDGL
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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