SitesBLAST
Comparing RR42_RS11250 FitnessBrowser__Cup4G11:RR42_RS11250 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)
42% identity, 93% coverage: 11:323/336 of query aligns to 42:352/486 of 4pcuA
- active site: K77 (= K44), S105 (≠ A72), D237 (= D207), S305 (= S276)
- binding protoporphyrin ix containing fe: A182 (≠ L150), P185 (≠ R153), L186 (≠ Q154), Y189 (= Y157), R222 (= R190), T269 (≠ A240)
- binding pyridoxal-5'-phosphate: K77 (= K44), N107 (= N74), G212 (= G180), T213 (= T181), G214 (= G182), T216 (= T184), G261 (= G232), S305 (= S276), P331 (≠ C302), D332 (= D303)
Sites not aligning to the query:
- binding protoporphyrin ix containing fe: 8, 9, 10, 11, 12, 20, 21, 22, 23
- binding s-adenosylmethionine: 376, 396, 397, 398, 399, 476, 478, 479
P35520 Cystathionine beta-synthase; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Homo sapiens (Human) (see 40 papers)
42% identity, 93% coverage: 11:323/336 of query aligns to 84:396/551 of P35520
- G85 (= G12) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T14) 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 (vs. gap) 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 (≠ A34) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P39) 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 (= K44) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ Y50) 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 (≠ I51) to V: in CBSD; loss of activity
- E131 (= E56) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G64) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (≠ V68) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (= E69) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G73) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N74) binding
- L154 (= L79) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (= A80) 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 (= C90) 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 (≠ Q98) 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 (= E101) 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 (≠ R105) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (≠ V116) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ A135) 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
- 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 (≠ A186) 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 (= R190) 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 (≠ N198) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ V201) 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 (≠ Y214) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ S228) 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 (≠ Y263) 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 (≠ N280) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ T296) 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 (≠ D306) 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 (≠ R311) to E: in CBSD; severe form; dbSNP:rs121964967
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
- 422 P → L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
- 427 P → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
- 435 I → T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
- 439 R → Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
- 444 D → N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
- 449 V → G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- 456 L → P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- 466 S → L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
- 500 S → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
- 526 Q → K: in CBSD; has significantly decreased levels of enzyme activity
- 539 L → S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
- 540 L → Q: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- 548 R → Q: presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; dbSNP:rs150828989
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
42% identity, 93% coverage: 11:323/336 of query aligns to 44:356/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ L150), P189 (≠ R153), L190 (≠ Q154), Y193 (= Y157), R226 (= R190)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K44), T106 (= T71), S107 (≠ A72), N109 (= N74), T110 (= T75), Q182 (= Q146), G216 (= G180), T217 (= T181), G218 (= G182), T220 (= T184), 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)
42% identity, 93% coverage: 11:323/336 of query aligns to 44:356/500 of 7qgtA
- binding protoporphyrin ix containing fe: A186 (≠ L150), P189 (≠ R153), L190 (≠ Q154), Y193 (= Y157), R226 (= R190)
- binding pyridoxal-5'-phosphate: K79 (= K44), N109 (= N74), G216 (= G180), T217 (= T181), G218 (= G182), T220 (= T184), G265 (= G232), S309 (= S276), P335 (≠ C302), D336 (= D303)
Sites not aligning to the query:
7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
43% identity, 93% coverage: 11:323/336 of query aligns to 9:314/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
43% identity, 93% coverage: 11:323/336 of query aligns to 9:314/458 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)
43% identity, 93% coverage: 11:323/336 of query aligns to 11:316/464 of P9WP51
Sites not aligning to the query:
- 428 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
40% identity, 96% coverage: 3:326/336 of query aligns to 8:332/477 of 6xwlC
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
40% identity, 96% coverage: 3:326/336 of query aligns to 8:332/468 of 6xylA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K44), T82 (= T75), Q154 (= Q146), G188 (= G180), T189 (= T181), G190 (= G182), T192 (= T184), G238 (= G232), I239 (= I233), Y241 (≠ S235), S282 (= S276), P308 (≠ C302), D309 (= D303)
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
40% identity, 97% coverage: 3:328/336 of query aligns to 39:363/504 of 3pc4A
- active site: K82 (= K44), S312 (= S276)
- binding protoporphyrin ix containing fe: A189 (≠ L150), P192 (≠ R153), L193 (≠ Q154), Y196 (= Y157), R229 (= R190), T276 (≠ A240)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K44), T109 (= T71), S110 (≠ A72), N112 (= N74), T113 (= T75), Q185 (= Q146), A218 (≠ T179), G219 (= G180), T220 (= T181), A221 (≠ G182), T223 (= T184), G268 (= G232), I269 (= I233), Y271 (≠ S235), 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)
40% identity, 97% coverage: 3:328/336 of query aligns to 39:363/504 of 3pc3A
- active site: K82 (= K44), S312 (= S276)
- binding protoporphyrin ix containing fe: A189 (≠ L150), P192 (≠ R153), L193 (≠ Q154), Y196 (= Y157), R229 (= R190)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K44), T109 (= T71), S110 (≠ A72), N112 (= N74), T113 (= T75), Q185 (= Q146), A218 (≠ T179), G219 (= G180), T220 (= T181), A221 (≠ G182), T223 (= T184), G268 (= G232), I269 (= I233), S312 (= S276), P338 (≠ C302), D339 (= D303)
Sites not aligning to the query:
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
40% identity, 97% coverage: 3:328/336 of query aligns to 37:361/500 of 3pc2A
- active site: K80 (= K44), S310 (= S276)
- binding protoporphyrin ix containing fe: A187 (≠ L150), P190 (≠ R153), L191 (≠ Q154), Y194 (= Y157), R227 (= R190)
- binding pyridoxal-5'-phosphate: K80 (= K44), N110 (= N74), A216 (≠ T179), G217 (= G180), T218 (= T181), A219 (≠ G182), T221 (= T184), G266 (= G232), S310 (= S276), P336 (≠ C302), D337 (= D303)
Sites not aligning to the query:
5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
40% identity, 97% coverage: 11:335/336 of query aligns to 39:358/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (≠ L150), P184 (≠ R153), Y188 (= Y157), R221 (= R190)
- binding pyridoxal-5'-phosphate: K74 (= K44), N104 (= N74), G209 (≠ A178), G211 (= G180), T212 (= T181), G213 (= G182), G214 (= G183), T215 (= T184), G256 (= G232), S300 (= S276), P326 (≠ C302), D327 (= D303)
Sites not aligning to the query:
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
40% identity, 97% coverage: 11:335/336 of query aligns to 43:365/504 of Q2V0C9
- K78 (= K44) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N74) binding
- GTGGT 215:219 (= GTGGT 180:184) binding
- S307 (= S276) binding
Sites not aligning to the query:
- 12 binding axial binding residue
- 23 binding axial binding residue
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
43% identity, 89% coverage: 9:308/336 of query aligns to 5:295/302 of 2efyA
- active site: K40 (= K44), S70 (≠ A72), E200 (≠ D207), S204 (= S211), S263 (= S276)
- binding 5-oxohexanoic acid: T69 (= T71), G71 (= G73), T73 (= T75), Q141 (= Q146), G175 (= G180), G219 (= G232), M220 (≠ I233), P222 (≠ S235)
- binding pyridoxal-5'-phosphate: K40 (= K44), N72 (= N74), Y172 (≠ C177), G175 (= G180), T176 (= T181), G177 (= G182), T179 (= T184), G219 (= G232), S263 (= S276), P289 (≠ C302), D290 (= D303)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
43% identity, 89% coverage: 9:308/336 of query aligns to 5:295/302 of 2ecqA
- active site: K40 (= K44), S70 (≠ A72), E200 (≠ D207), S204 (= S211), S263 (= S276)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K44), G71 (= G73), T73 (= T75), Q141 (= Q146), G219 (= G232)
- binding pyridoxal-5'-phosphate: K40 (= K44), N72 (= N74), Y172 (≠ C177), G173 (≠ A178), G175 (= G180), T176 (= T181), T179 (= T184), G219 (= G232), S263 (= S276), P289 (≠ C302)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
43% identity, 89% coverage: 9:308/336 of query aligns to 5:295/302 of 2ecoA
- active site: K40 (= K44), S70 (≠ A72), E200 (≠ D207), S204 (= S211), S263 (= S276)
- binding 4-methyl valeric acid: K40 (= K44), T69 (= T71), G71 (= G73), T73 (= T75), Q141 (= Q146), G175 (= G180), T176 (= T181), G219 (= G232)
- binding pyridoxal-5'-phosphate: K40 (= K44), N72 (= N74), Y172 (≠ C177), G175 (= G180), T176 (= T181), T179 (= T184), G219 (= G232), S263 (= S276), P289 (≠ C302), D290 (= D303)
6vjuB Crystal structure of cystathionine beta synthase from legionella pneumophila with llp, plp, and homocysteine
37% identity, 94% coverage: 7:323/336 of query aligns to 7:316/317 of 6vjuB
6c4pA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex (see paper)
35% identity, 98% coverage: 2:331/336 of query aligns to 5:343/344 of 6c4pA
- binding calcium ion: N179 (≠ D167), D182 (≠ G170), N183 (≠ K171)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (= K44), N80 (= N74), A191 (≠ T179), G192 (= G180), T193 (= T181), G194 (= G182), T196 (= T184), G241 (= G232), S285 (= S276), P314 (≠ C302), D315 (= D303)
P16703 Cysteine synthase B; CSase B; O-acetylserine (thiol)-lyase B; OAS-TL B; O-acetylserine sulfhydrylase B; EC 2.5.1.47 from Escherichia coli (strain K12) (see paper)
37% identity, 89% coverage: 10:308/336 of query aligns to 7:286/303 of P16703
- N71 (= N74) binding
- S255 (= S276) binding
Query Sequence
>RR42_RS11250 FitnessBrowser__Cup4G11:RR42_RS11250
MDVKDGFVGTIGHTPLIRLAGLSEETGCEILGKAEFLNPGGSVKDRAALYIIRDAERRGA
LKPGGTVVEGTAGNTGIGLAHLCAARGYRCIVVIPDTQSPEKMDRLRLLGAEVRPVPAAP
YADPNNYQKVAGRLAQETENAIWANQFDNLANRQAHYETTGPEIWHDTAGKIDAFVCATG
TGGTLAGVARFLKEKERNPPVRIVLADPHGSGLYHFVKHHEVKAKGNSITEGIGSSRVTA
NLADTPIDDAVRIDDQACVDMVYRLLREEGLWVGGSSGINVAAAAWLAREMGPGHTIVTL
LCDRGDLYAGRLFNADWLAAKGLTPQPVVSRHVAQP
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