SitesBLAST
Comparing CA265_RS04375 FitnessBrowser__Pedo557:CA265_RS04375 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)
7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
41% identity, 99% coverage: 4:452/453 of query aligns to 3:456/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
41% identity, 99% coverage: 4:452/453 of query aligns to 3:456/458 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)
41% identity, 99% coverage: 4:452/453 of query aligns to 5:458/464 of P9WP51
- K428 (≠ S421) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
37% identity, 99% coverage: 5:453/453 of query aligns to 39:495/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ L150), P189 (≠ S153), L190 (≠ Q154), Y193 (= Y157), R226 (≠ K190)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K43), T106 (= T70), S107 (= S71), N109 (= N73), T110 (= T74), Q182 (= Q146), G216 (= G180), T217 (= T181), G218 (= G182), T220 (= T184), G265 (= G232), S309 (= S276), P335 (≠ H302), D336 (= D303)
Sites not aligning to the query:
8s5hA Full-length human cystathionine beta-synthase with c-terminal 6xhis- tag, basal state, helical reconstruction (see paper)
37% identity, 99% coverage: 5:453/453 of query aligns to 38:504/507 of 8s5hA
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)
37% identity, 99% coverage: 5:453/453 of query aligns to 79:545/551 of P35520
- G85 (= G11) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T13) to N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
- L101 (≠ V25) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
- K102 (≠ P26) 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 (≠ I33) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P38) 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 (= K43) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ K49) 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 (= M50) to V: in CBSD; loss of activity
- E131 (= E55) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G63) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (= I67) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (= E68) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G72) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N73) binding pyridoxal 5'-phosphate
- L154 (= L78) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (= A79) 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 (= C89) 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 (≠ Q97) 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 (= E100) 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 (≠ A104) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (≠ C115) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ E135) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ L150) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N152) 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 (= A155) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ E158) 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 (= GTGGT 180:184) binding pyridoxal 5'-phosphate
- T257 (= T181) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (≠ S186) 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 (≠ K190) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (= K193) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ N196) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ I199) 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 (≠ W202) 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 (= D205) to N: in CBSD; loss of activity
- A288 (≠ K212) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ I229) 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 (≠ I247) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (= D248) 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 (≠ I265) 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 pyridoxal 5'-phosphate; 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 (≠ A280) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ V296) 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 (≠ S306) 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 (≠ Q349) to L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
- P427 (≠ E354) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
- I435 (vs. gap) to T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
- R439 (≠ K360) to Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
- D444 (≠ S365) to N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
- V449 (≠ T370) to G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- L456 (≠ V376) to P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- S466 (= S386) to L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
- S500 (= S420) 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 (≠ I447) to S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
- L540 (≠ I448) 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
- 78 P → R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
- 548 R → Q: presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; dbSNP:rs150828989
4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
36% identity, 99% coverage: 5:453/453 of query aligns to 37:486/486 of 4pcuA
- active site: K77 (= K43), S105 (= S71), D237 (= D205), S305 (= S276)
- binding protoporphyrin ix containing fe: A182 (≠ L150), P185 (≠ S153), L186 (≠ Q154), Y189 (= Y157), R222 (≠ K190), T269 (≠ A240)
- binding pyridoxal-5'-phosphate: K77 (= K43), N107 (= N73), G212 (= G180), T213 (= T181), G214 (= G182), T216 (= T184), G261 (= G232), S305 (= S276), P331 (≠ H302), D332 (= D303)
- binding s-adenosylmethionine: P376 (≠ Q349), G396 (≠ N363), F397 (≠ I364), D398 (≠ S365), Q399 (= Q366), T476 (= T443), I478 (≠ Y445), D479 (= D446)
Sites not aligning to the query:
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
36% identity, 99% coverage: 5:453/453 of query aligns to 42:500/504 of 3pc4A
- active site: K82 (= K43), S312 (= S276)
- binding protoporphyrin ix containing fe: A189 (≠ L150), P192 (≠ S153), L193 (≠ Q154), Y196 (= Y157), R229 (≠ K190), T276 (≠ A240)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K43), T109 (= T70), S110 (= S71), N112 (= N73), T113 (= T74), Q185 (= Q146), A218 (≠ V179), G219 (= G180), T220 (= T181), A221 (≠ G182), T223 (= T184), G268 (= G232), I269 (= I233), Y271 (≠ E235), S312 (= S276), P338 (≠ H302), D339 (= D303)
Sites not aligning to the query:
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
36% identity, 99% coverage: 5:453/453 of query aligns to 42:500/504 of 3pc3A
- active site: K82 (= K43), S312 (= S276)
- binding protoporphyrin ix containing fe: A189 (≠ L150), P192 (≠ S153), L193 (≠ Q154), Y196 (= Y157), R229 (≠ K190)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K43), T109 (= T70), S110 (= S71), N112 (= N73), T113 (= T74), Q185 (= Q146), A218 (≠ V179), G219 (= G180), T220 (= T181), A221 (≠ G182), T223 (= T184), G268 (= G232), I269 (= I233), S312 (= S276), P338 (≠ H302), D339 (= D303)
Sites not aligning to the query:
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
36% identity, 99% coverage: 5:453/453 of query aligns to 40:498/500 of 3pc2A