SitesBLAST
Comparing WP_012567166.1 NCBI__GCF_000016185.1:WP_012567166.1 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)
36% identity, 97% coverage: 11:456/461 of query aligns to 36:484/486 of 4pcuA
- active site: K77 (= K49), S105 (≠ A77), D237 (= D211), S305 (= S280)
- binding protoporphyrin ix containing fe: A182 (≠ P156), P185 (= P159), L186 (≠ R160), Y189 (≠ E163), R222 (≠ A196), T269 (≠ P244)
- binding pyridoxal-5'-phosphate: K77 (= K49), N107 (= N79), G212 (= G186), T213 (≠ S187), G214 (= G188), T216 (= T190), G261 (= G236), S305 (= S280), P331 (≠ C306), D332 (= D307)
- binding s-adenosylmethionine: P376 (≠ V349), G396 (≠ D369), F397 (≠ V370), D398 (≠ S371), Q399 (= Q372), T476 (= T448), I478 (≠ M450), D479 (= D451)
Sites not aligning to the query:
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
35% identity, 97% coverage: 11:459/461 of query aligns to 38:496/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ P156), P189 (= P159), L190 (≠ R160), Y193 (≠ E163), R226 (≠ A196)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K49), T106 (= T76), S107 (≠ A77), N109 (= N79), T110 (= T80), Q182 (= Q152), G216 (= G186), T217 (≠ S187), G218 (= G188), T220 (= T190), G265 (= G236), S309 (= S280), P335 (≠ C306), D336 (= D307)
Sites not aligning to the query:
8s5hA Full-length human cystathionine beta-synthase with c-terminal 6xhis- tag, basal state, helical reconstruction (see paper)
35% identity, 97% coverage: 11:459/461 of query aligns to 37:505/507 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)
35% identity, 97% coverage: 11:459/461 of query aligns to 78:546/551 of P35520
- P78 (= P11) to R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
- G85 (= G18) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T20) 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 (≠ P32) 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 (≠ L39) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P44) 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 (= K49) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ K55) 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 (= M56) to V: in CBSD; loss of activity
- E131 (= E61) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G69) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (= I73) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (= E74) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G78) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N79) binding pyridoxal 5'-phosphate
- L154 (= L84) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (= A85) 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 (≠ L95) 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 (= M103) 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 (= E106) 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 (≠ H110) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (= T121) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ A141) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ P156) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N158) 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 (= A161) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ E164) 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 (≠ GSGGT 186:190) binding pyridoxal 5'-phosphate
- T257 (≠ S187) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (= T192) 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 (≠ A196) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (≠ A199) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ S202) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ T205) 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 (≠ V208) 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 (= D211) to N: in CBSD; loss of activity
- A288 (= A218) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ V233) 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 (= G236) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G238) 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 (≠ A251) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (≠ K252) to V: in CBSD; loss of activity
- R336 (= R267) 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 (= L269) 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 (= G278) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (= S280) 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 (≠ L284) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (= R300) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D307) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (≠ N310) 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 (= K315) to E: in CBSD; severe form; dbSNP:rs121964967
- P422 (≠ V349) to L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
- P427 (= P354) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
- I435 (≠ Y362) to T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
- R439 (= R366) to Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
- D444 (≠ S371) to N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
- V449 (≠ M376) to G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- L456 (≠ I382) to P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- S466 (≠ L392) to L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
- S500 (≠ T426) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
- Q526 (= Q439) to K: in CBSD; has significantly decreased levels of enzyme activity
- L539 (= L452) to S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
- L540 (= L453) 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
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
35% identity, 97% coverage: 11:459/461 of query aligns to 37:495/504 of Q2V0C9
- K78 (= K49) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N79) binding pyridoxal 5'-phosphate
- GTGGT 215:219 (≠ GSGGT 186:190) binding pyridoxal 5'-phosphate
- S307 (= S280) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 12 binding axial binding residue
- 23 binding axial binding residue
6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
35% identity, 97% coverage: 12:456/461 of query aligns to 11:473/477 of 6xwlC
5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
35% identity, 97% coverage: 11:459/461 of query aligns to 33:488/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (= P156), P184 (= P159), Y188 (≠ E163), R221 (≠ A196)
- binding pyridoxal-5'-phosphate: K74 (= K49), N104 (= N79), G209 (= G184), G211 (= G186), T212 (≠ S187), G213 (= G188), G214 (= G189), T215 (= T190), G256 (= G236), S300 (= S280), P326 (≠ C306), D327 (= D307)
Sites not aligning to the query:
1jbqA Structure of human cystathionine beta-synthase: a unique pyridoxal 5'- phosphate dependent hemeprotein (see paper)
42% identity, 69% coverage: 11:328/461 of query aligns to 36:348/348 of 1jbqA
- active site: K77 (= K49), S105 (≠ A77), D232 (= D211), S236 (= S215), L238 (≠ I217), S300 (= S280), P326 (≠ C306)
- binding protoporphyrin ix containing fe: A177 (≠ P156), P180 (= P159), L181 (≠ R160), Y184 (≠ E163), R217 (≠ A196)
- binding pyridoxal-5'-phosphate: K77 (= K49), N107 (= N79), V206 (= V185), G207 (= G186), T208 (≠ S187), G209 (= G188), G210 (= G189), T211 (= T190), G256 (= G236), S300 (= S280), P326 (≠ C306), D327 (= D307)
Sites not aligning to the query:
P9WP51 Probable cystathionine beta-synthase Rv1077; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
37% identity, 97% coverage: 13:461/461 of query aligns to 7:462/464 of P9WP51
- K428 (≠ P427) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
37% identity, 96% coverage: 13:456/461 of query aligns to 5:455/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
37% identity, 96% coverage: 13:456/461 of query aligns to 5:455/458 of 7xnzB
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
35% identity, 97% coverage: 12:456/461 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 (= K49), T82 (= T80), Q154 (= Q152), G188 (= G186), T189 (≠ S187), G190 (= G188), T192 (= T190), G238 (= G236), I239 (≠ V237), Y241 (≠ E239), S282 (= S280), P308 (≠ C306), D309 (= D307)
6c4pA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex (see paper)
40% identity, 67% coverage: 13:322/461 of query aligns to 10:330/344 of 6c4pA
- binding calcium ion: N179 (vs. gap), D182 (≠ G176), N183 (≠ D177)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (= K49), N80 (= N79), A191 (≠ V185), G192 (= G186), T193 (≠ S187), G194 (= G188), T196 (= T190), G241 (= G236), S285 (= S280), P314 (≠ C306), D315 (= D307)
6c2zA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-aminoacrylate intermediate (see paper)
40% identity, 67% coverage: 13:322/461 of query aligns to 11:331/345 of 6c2zA
- binding calcium ion: N180 (vs. gap), D183 (≠ G176), N184 (≠ D177)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K50 (= K49), T78 (= T76), S79 (≠ A77), N81 (= N79), T82 (= T80), Q154 (= Q152), A192 (≠ V185), G193 (= G186), T194 (≠ S187), G195 (= G188), T197 (= T190), G242 (= G236), S286 (= S280), P315 (≠ C306), D316 (= D307)
6c2qA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-l-serine intermediate (see paper)
40% identity, 67% coverage: 13:322/461 of query aligns to 11:331/345 of 6c2qA
- binding calcium ion: N180 (vs. gap), D183 (≠ G176), N184 (≠ D177)
- binding L-Serine, N-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]: K50 (= K49), T78 (= T76), S79 (≠ A77), N81 (= N79), T82 (= T80), Q154 (= Q152), A192 (≠ V185), G193 (= G186), T194 (≠ S187), G195 (= G188), T197 (= T190), G242 (= G236), Y245 (≠ E239), S286 (= S280), P315 (≠ C306), D316 (= D307)
6c2hA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the catalytic core (see paper)
40% identity, 67% coverage: 13:322/461 of query aligns to 11:331/345 of 6c2hA
- binding calcium ion: N180 (vs. gap), D183 (≠ G176), N184 (≠ D177)
- binding pyridoxal-5'-phosphate: K50 (= K49), N81 (= N79), A192 (≠ V185), G193 (= G186), T194 (≠ S187), G195 (= G188), T197 (= T190), G242 (= G236), S286 (= S280), P315 (≠ C306), D316 (= D307)
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
34% identity, 93% coverage: 11:438/461 of query aligns to 41:475/504 of 3pc4A
- active site: K82 (= K49), S312 (= S280)
- binding protoporphyrin ix containing fe: A189 (≠ P156), P192 (= P159), L193 (≠ R160), Y196 (≠ E163), R229 (≠ A196), T276 (≠ P244)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K49), T109 (= T76), S110 (≠ A77), N112 (= N79), T113 (= T80), Q185 (= Q152), A218 (≠ V185), G219 (= G186), T220 (≠ S187), A221 (≠ G188), T223 (= T190), G268 (= G236), I269 (≠ V237), Y271 (≠ E239), S312 (= S280), P338 (≠ C306), D339 (= D307)
Sites not aligning to the query:
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
34% identity, 93% coverage: 11:438/461 of query aligns to 41:475/504 of 3pc3A
- active site: K82 (= K49), S312 (= S280)
- binding protoporphyrin ix containing fe: A189 (≠ P156), P192 (= P159), L193 (≠ R160), Y196 (≠ E163), R229 (≠ A196)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K49), T109 (= T76), S110 (≠ A77), N112 (= N79), T113 (= T80), Q185 (= Q152), A218 (≠ V185), G219 (= G186), T220 (≠ S187), A221 (≠ G188), T223 (= T190), G268 (= G236), I269 (≠ V237), S312 (= S280), P338 (≠ C306), D339 (= D307)
Sites not aligning to the query:
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
34% identity, 93% coverage: 11:438/461 of query aligns to 39:473/500 of 3pc2A
- active site: K80 (= K49), S310 (= S280)
- binding protoporphyrin ix containing fe: A187 (≠ P156), P190 (= P159), L191 (≠ R160), Y194 (≠ E163), R227 (≠ A196)
- binding pyridoxal-5'-phosphate: K80 (= K49), N110 (= N79), A216 (≠ V185), G217 (= G186), T218 (≠ S187), A219 (≠ G188), T221 (= T190), G266 (= G236), S310 (= S280), P336 (≠ C306), D337 (= D307)
Sites not aligning to the query:
6vjuB Crystal structure of cystathionine beta synthase from legionella pneumophila with llp, plp, and homocysteine
42% identity, 69% coverage: 11:328/461 of query aligns to 5:317/317 of 6vjuB
Query Sequence
>WP_012567166.1 NCBI__GCF_000016185.1:WP_012567166.1
MPDTLSAAKAPAILSMIGGTPVIRVSTFDTGPCELYLKLENQNPGGSIKDRIGLKMIEAA
EAEGRLKPGGTVIEATAGNTGLGLALVCAAKGYRLILVIPDKMAVEKINHLRALGAEIHI
TRSDVGKGHPDYYQDIAERLAADIPGSVYMNQFANPANPRAHEEWTGPELLRQMDGDVDA
VVVGVGSGGTMTGLGAFFAKASPKTKMVIADPAGSIIADLVNKGTHEEPGSWVVEGVGED
FVPPNCDLRYAKAAYYVSDAESLTAARDLLRREGILGGSSSGTLLAGALKYCRDQTTRQR
VVTFVCDTGNKYLSKMFNDAWMADQGFLPLEKHGDLRDLMTRRHDKGQVVTVSPQDTLLT
AYKRMRISDVSQLPVMEGERVIGILDESDLLLHVEKDPVRFKDKVYTAMVNRLETLPATA
PIAALTPLFERNLVAIIMQDGRFLGLLTRMDLLNHLRRQMG
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