SitesBLAST
Comparing Pf1N1B4_4889 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4889 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)
4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
35% identity, 98% coverage: 7:453/458 of query aligns to 36:484/486 of 4pcuA
- active site: K77 (= K45), S105 (≠ A73), D237 (= D207), S305 (= S276)
- binding protoporphyrin ix containing fe: A182 (≠ P152), P185 (= P155), L186 (= L156), Y189 (≠ E159), R222 (= R192), T269 (≠ S240)
- binding pyridoxal-5'-phosphate: K77 (= K45), N107 (= N75), G212 (= G182), T213 (≠ S183), G214 (≠ A184), T216 (= T186), G261 (= G232), S305 (= S276), P331 (≠ C302), D332 (= D303)
- binding s-adenosylmethionine: P376 (vs. gap), G396 (≠ D365), F397 (≠ V366), D398 (≠ S367), Q399 (= Q368), T476 (= T445), I478 (≠ V447), D479 (= D448)
Sites not aligning to the query:
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
34% identity, 98% coverage: 7:453/458 of query aligns to 38:493/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ P152), P189 (= P155), L190 (= L156), Y193 (≠ E159), R226 (= R192)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K45), T106 (= T72), S107 (≠ A73), N109 (= N75), T110 (= T76), Q182 (= Q148), G216 (= G182), T217 (≠ S183), G218 (≠ A184), T220 (= T186), G265 (= G232), S309 (= S276), P335 (≠ C302), D336 (= D303)
Sites not aligning to the query:
7qgtA Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
34% identity, 98% coverage: 7:453/458 of query aligns to 38:493/500 of 7qgtA
- binding protoporphyrin ix containing fe: A186 (≠ P152), P189 (= P155), L190 (= L156), Y193 (≠ E159), R226 (= R192)
- binding pyridoxal-5'-phosphate: K79 (= K45), N109 (= N75), G216 (= G182), T217 (≠ S183), G218 (≠ A184), T220 (= T186), G265 (= G232), S309 (= S276), P335 (≠ C302), D336 (= D303)
Sites not aligning to the query:
P35520 Cystathionine beta-synthase; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Homo sapiens (Human) (see 40 papers)
34% identity, 97% coverage: 7:451/458 of query aligns to 78:541/551 of P35520
- P78 (= P7) to R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
- G85 (= G14) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T16) to N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
- L101 (vs. gap) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
- K102 (≠ P28) to N: in CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204609; to Q: in dbSNP:rs34040148
- C109 (≠ L35) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P40) to V: in CBSD; mild form; when linked with W-58 severe form; decreased cystathionine beta-synthase activity; decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs121964964
- K119 (= K45) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ A51) to Q: in CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs781444670; to W: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs886057100
- M126 (= M52) to V: in CBSD; loss of activity
- E131 (= E57) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G65) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (≠ V69) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (= E70) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G74) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N75) binding
- L154 (= L80) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (= A81) to T: in CBSD; complete loss of activity; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs1429138569; to V: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- C165 (≠ V91) to Y: in CBSD; severe form; protein expression is comparable to wild-type; loss of cystathionine beta-synthase activity; no effect on homotetramer formation; dbSNP:rs1347651454
- M173 (= M99) to V: in CBSD; presents 40% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; natural variant: Missing (in CBSD; loss of activity)
- E176 (= E102) to K: in CBSD; severe form; loss of cystathionine beta-synthase activity; inhibited by AdoMet; severely decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs762065361
- V180 (≠ H106) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (= T117) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ A137) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ P152) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N154) to K: in CBSD; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs1464223176; to S: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1555874803
- A231 (= A157) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ C160) to N: in CBSD; decreased cystathionine beta-synthase activity; changed localization; decreased interaction with pyridoxal 5'-phosphate; no effect on homotetramer formation; dbSNP:rs773734233; natural variant: Missing (in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity)
- GTGGT 256:260 (≠ GSAGT 182:186) binding
- T257 (≠ S183) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (= T188) to M: in CBSD; moderate form; dbSNP:rs149119723; to R: in CBSD; severe form; loss of cystathionine beta-synthase activity; loss of homotetramer formation
- R266 (= R192) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (≠ Q195) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ Q198) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ L201) to Y: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; mutation to S: Reduced heme content and cystathionine beta-synthase activity.
- I278 (≠ V204) to S: in CBSD; loss of activity; to T: in CBSD; mild to severe form; common mutation; decreased expression; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs5742905
- D281 (= D207) to N: in CBSD; loss of activity
- A288 (= A214) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ A229) to K: in CBSD; no effect on cystathionine beta-synthase activity; inhibited by AdoHcy and impaired activation by AdoMet; no effect on homotetramer formation; dbSNP:rs779270933
- G305 (= G232) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G234) to S: in CBSD; moderate to severe form; linked with D-534; common mutation; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; no effect on homotetramer formation; dbSNP:rs121964962
- V320 (= V247) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (≠ R248) to V: in CBSD; loss of activity
- R336 (= R263) to C: in CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure; dbSNP:rs398123151; to H: in CBSD; mild form; no effect on expression; exhibits an activity lower than 4% of the wild-type enzyme; altered stimulation by AdoMet; absent capacity to form multimeric quaternary structure; dbSNP:rs760417941
- L338 (= L265) to P: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- G347 (= G274) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (= S276) binding ; to N: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- T353 (≠ L280) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (= R296) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D303) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (≠ T306) to Q: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs763036586
- K384 (= K311) to E: in CBSD; severe form; dbSNP:rs121964967
- P422 (≠ V345) to L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
- P427 (= P350) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
- I435 (≠ F358) to T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
- R439 (= R362) to Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
- D444 (≠ S367) to N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
- V449 (≠ L372) to G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- L456 (≠ V379) to P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- S466 (≠ F389) to L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
- S500 (≠ E423) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
- Q526 (vs. gap) to K: in CBSD; has significantly decreased levels of enzyme activity
- L539 (≠ M449) to S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
- L540 (= L450) to Q: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
Sites not aligning to the query:
- 18 R → C: results in 1/3 to 2/3 the enzyme activity of the wild-type; dbSNP:rs201827340
- 49 P → L: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs148865119
- 52 binding axial binding residue
- 58 R → W: in CBSD; linked with V-114; 18% of activity; dbSNP:rs555959266
- 65 binding axial binding residue; H → R: in CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs1191141364
- 69 A → P: in dbSNP:rs17849313
- 548 R → Q: presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; dbSNP:rs150828989
7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
38% identity, 97% coverage: 9:453/458 of query aligns to 5:455/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
38% identity, 97% coverage: 9:453/458 of query aligns to 5:455/458 of 7xnzB
P9WP51 Probable cystathionine beta-synthase Rv1077; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
38% identity, 97% coverage: 9:453/458 of query aligns to 7:457/464 of P9WP51
- K428 (≠ A424) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
35% identity, 97% coverage: 8:453/458 of query aligns to 11:473/477 of 6xwlC
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
34% identity, 98% coverage: 7:456/458 of query aligns to 37:495/504 of Q2V0C9
- K78 (= K45) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N75) binding
- GTGGT 215:219 (≠ GSAGT 182:186) binding
- S307 (= S276) binding
Sites not aligning to the query:
- 12 binding axial binding residue
- 23 binding axial binding residue
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
35% identity, 97% coverage: 8:453/458 of query aligns to 11:464/468 of 6xylA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K45), T82 (= T76), Q154 (= Q148), G188 (= G182), T189 (≠ S183), G190 (≠ A184), T192 (= T186), G238 (= G232), I239 (= I233), Y241 (≠ E235), S282 (= S276), P308 (≠ C302), D309 (= D303)
5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
33% identity, 98% coverage: 7:456/458 of query aligns to 33:488/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (= P152), P184 (= P155), Y188 (≠ E159), R221 (= R192)
- binding pyridoxal-5'-phosphate: K74 (= K45), N104 (= N75), G209 (= G180), G211 (= G182), T212 (≠ S183), G213 (≠ A184), G214 (= G185), T215 (= T186), G256 (= G232), S300 (= S276), P326 (≠ C302), D327 (= D303)
Sites not aligning to the query:
6c2zA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-aminoacrylate intermediate (see paper)
39% identity, 70% coverage: 4:323/458 of query aligns to 6:336/345 of 6c2zA
- binding calcium ion: N180 (vs. gap), D183 (≠ H172), N184 (≠ D173)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K50 (= K45), T78 (= T72), S79 (≠ A73), N81 (= N75), T82 (= T76), Q154 (= Q148), A192 (≠ V181), G193 (= G182), T194 (≠ S183), G195 (≠ A184), T197 (= T186), G242 (= G232), S286 (= S276), P315 (≠ C302), D316 (= D303)
6c2qA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-l-serine intermediate (see paper)
39% identity, 70% coverage: 4:323/458 of query aligns to 6:336/345 of 6c2qA
- binding calcium ion: N180 (vs. gap), D183 (≠ H172), N184 (≠ D173)
- binding L-Serine, N-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]: K50 (= K45), T78 (= T72), S79 (≠ A73), N81 (= N75), T82 (= T76), Q154 (= Q148), A192 (≠ V181), G193 (= G182), T194 (≠ S183), G195 (≠ A184), T197 (= T186), G242 (= G232), Y245 (≠ E235), S286 (= S276), P315 (≠ C302), D316 (= D303)
6c2hA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the catalytic core (see paper)
39% identity, 70% coverage: 4:323/458 of query aligns to 6:336/345 of 6c2hA
- binding calcium ion: N180 (vs. gap), D183 (≠ H172), N184 (≠ D173)
- binding pyridoxal-5'-phosphate: K50 (= K45), N81 (= N75), A192 (≠ V181), G193 (= G182), T194 (≠ S183), G195 (≠ A184), T197 (= T186), G242 (= G232), S286 (= S276), P315 (≠ C302), D316 (= D303)
6c4pA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex (see paper)
39% identity, 70% coverage: 4:323/458 of query aligns to 5:335/344 of 6c4pA
- binding calcium ion: N179 (vs. gap), D182 (≠ H172), N183 (≠ D173)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (= K45), N80 (= N75), A191 (≠ V181), G192 (= G182), T193 (≠ S183), G194 (≠ A184), T196 (= T186), G241 (= G232), S285 (= S276), P314 (≠ C302), D315 (= D303)
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
37% identity, 83% coverage: 7:388/458 of query aligns to 39:426/500 of 3pc2A
- active site: K80 (= K45), S310 (= S276)
- binding protoporphyrin ix containing fe: A187 (≠ P152), P190 (= P155), L191 (= L156), Y194 (≠ E159), R227 (= R192)
- binding pyridoxal-5'-phosphate: K80 (= K45), N110 (= N75), A216 (≠ V181), G217 (= G182), T218 (≠ S183), A219 (= A184), T221 (= T186), G266 (= G232), S310 (= S276), P336 (≠ C302), D337 (= D303)
Sites not aligning to the query:
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
37% identity, 83% coverage: 7:388/458 of query aligns to 41:428/504 of 3pc4A
- active site: K82 (= K45), S312 (= S276)
- binding protoporphyrin ix containing fe: A189 (≠ P152), P192 (= P155), L193 (= L156), Y196 (≠ E159), R229 (= R192), T276 (≠ S240)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K45), T109 (= T72), S110 (≠ A73), N112 (= N75), T113 (= T76), Q185 (= Q148), A218 (≠ V181), G219 (= G182), T220 (≠ S183), A221 (= A184), T223 (= T186), G268 (= G232), I269 (= I233), Y271 (≠ E235), S312 (= S276), P338 (≠ C302), D339 (= D303)
Sites not aligning to the query:
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
37% identity, 83% coverage: 7:388/458 of query aligns to 41:428/504 of 3pc3A
- active site: K82 (= K45), S312 (= S276)
- binding protoporphyrin ix containing fe: A189 (≠ P152), P192 (= P155), L193 (= L156), Y196 (≠ E159), R229 (= R192)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K45), T109 (= T72), S110 (≠ A73), N112 (= N75), T113 (= T76), Q185 (= Q148), A218 (≠ V181), G219 (= G182), T220 (≠ S183), A221 (= A184), T223 (= T186), G268 (= G232), I269 (= I233), S312 (= S276), P338 (≠ C302), D339 (= D303)
Sites not aligning to the query:
6vjuB Crystal structure of cystathionine beta synthase from legionella pneumophila with llp, plp, and homocysteine
39% identity, 69% coverage: 7:324/458 of query aligns to 5:317/317 of 6vjuB
G5EFH8 Cystathionine beta-synthase cbs-1; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Caenorhabditis elegans (see paper)
37% identity, 70% coverage: 3:324/458 of query aligns to 372:702/704 of G5EFH8
- K421 (= K45) mutation to A: Binds significantly less of the PLP cofactor. Altered fluorescence-based tryptophan spectra.
Query Sequence
>Pf1N1B4_4889 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4889
MPNDSRPAVLELIGNTPLVRISRFDTGPCTLFLKLESQNPGGSIKDRIGLAMIDTAERDG
RLRPGGTIVEATAGNTGLGLALVGRAKGYRVVLVVPDKMSTEKVLHLKAMGAEVHITRSD
VGKGHPDYYQDVAARLARDIPDAFFADQFNNPANPLAHECSTAPEIWAQTQHDVDAIVVG
VGSAGTLTGLTRFFQRVQPNLEMVLADPVGSVMAEYSRSGTLGTPGSWAVEGIGEDFIPS
IADLSSVRKAYSISDEESFDHARQLLRAEGILGGSSTGTLLAAALRYCREQTEPKRVVSF
VCDTGTRYLSKVYNDQWMNDQGLLARKRYGDLRDLIARRFEDGRVVSVGPDDTLLTAFQR
MRLADVSQLPVLVDGQRLVGVIDESDILFGVHEDATHFRMTVTSAMTDKLETLPPGASLA
ELEAVLDRGLVAIIADTSGFHGLITRVDMLNHLRRSLA
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