SitesBLAST
Comparing WP_011384252.1 NCBI__GCF_000009985.1:WP_011384252.1 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)
34% identity, 98% coverage: 6:449/455 of query aligns to 37:484/486 of 4pcuA
- active site: K77 (= K43), S105 (≠ A71), D237 (= D204), S305 (= S273)
- binding protoporphyrin ix containing fe: A182 (≠ P149), P185 (= P152), L186 (≠ A153), Y189 (≠ E156), R222 (= R189), T269 (≠ M237)
- binding pyridoxal-5'-phosphate: K77 (= K43), N107 (= N73), G212 (= G179), T213 (≠ S180), G214 (= G181), T216 (= T183), G261 (= G229), S305 (= S273), P331 (≠ C299), D332 (= D300)
- binding s-adenosylmethionine: P376 (≠ A342), G396 (≠ D362), F397 (≠ V363), D398 (≠ S364), Q399 (= Q365), T476 (= T441), I478 (≠ M443), D479 (= D444)
Sites not aligning to the query:
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
33% identity, 98% coverage: 6:449/455 of query aligns to 39:493/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ P149), P189 (= P152), L190 (≠ A153), Y193 (≠ E156), R226 (= R189)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K43), T106 (= T70), S107 (≠ A71), N109 (= N73), T110 (= T74), Q182 (= Q145), G216 (= G179), T217 (≠ S180), G218 (= G181), T220 (= T183), G265 (= G229), S309 (= S273), P335 (≠ C299), D336 (= D300)
Sites not aligning to the query:
7qgtA Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
33% identity, 98% coverage: 6:449/455 of query aligns to 39:493/500 of 7qgtA
- binding protoporphyrin ix containing fe: A186 (≠ P149), P189 (= P152), L190 (≠ A153), Y193 (≠ E156), R226 (= R189)
- binding pyridoxal-5'-phosphate: K79 (= K43), N109 (= N73), G216 (= G179), T217 (≠ S180), G218 (= G181), T220 (= T183), G265 (= G229), S309 (= S273), P335 (≠ C299), D336 (= D300)
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)
32% identity, 98% coverage: 6:449/455 of query aligns to 79:543/551 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 (≠ 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 (≠ L33) 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 (≠ S49) 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 (≠ V67) 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
- 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 (≠ L89) 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 (≠ A97) 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 (≠ D100) 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 (≠ H104) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (≠ A115) 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 (≠ P149) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N151) 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 (= A154) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (= D157) 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 179:183) binding
- T257 (≠ S180) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (= T185) 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 (= R189) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (≠ A192) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ S195) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ T198) 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 (≠ V201) 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 (= D204) to N: in CBSD; loss of activity
- A288 (= A211) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ L226) 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 (= G229) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G231) 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 (= V244) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (≠ T245) to V: in CBSD; loss of activity
- R336 (= R260) 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 (≠ V262) 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 (= G271) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (= S273) 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 (≠ L277) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (= R293) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D300) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (≠ N303) 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 (≠ R308) to E: in CBSD; severe form; dbSNP:rs121964967
- P422 (≠ A342) to L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
- P427 (= P347) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
- I435 (≠ Y355) to T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
- R439 (= R359) to Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
- D444 (≠ S364) to N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
- V449 (= V369) to G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- L456 (≠ I375) to P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- S466 (≠ I385) to L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
- S500 (≠ L419) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
- Q526 (≠ D432) to K: in CBSD; has significantly decreased levels of enzyme activity
- L539 (= L445) to S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
- L540 (= L446) 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
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
35% identity, 99% coverage: 2:452/455 of query aligns to 4:467/468 of 6xylA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K43), T82 (= T74), Q154 (= Q145), G188 (= G179), T189 (≠ S180), G190 (= G181), T192 (= T183), G238 (= G229), I239 (= I230), Y241 (≠ G232), S282 (= S273), P308 (≠ C299), D309 (= D300)
6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
34% identity, 99% coverage: 2:452/455 of query aligns to 4:476/477 of 6xwlC
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
40% identity, 70% coverage: 6:322/455 of query aligns to 38:356/504 of Q2V0C9
- K78 (= K43) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N73) binding
- GTGGT 215:219 (≠ GSGGT 179:183) binding
- S307 (= S273) binding
Sites not aligning to the query:
- 12 binding axial binding residue
- 23 binding axial binding residue
5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
40% identity, 70% coverage: 6:322/455 of query aligns to 34:349/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (= P149), P184 (= P152), Y188 (≠ E156), R221 (= R189)
- binding pyridoxal-5'-phosphate: K74 (= K43), N104 (= N73), G209 (= G177), G211 (= G179), T212 (≠ S180), G213 (= G181), G214 (= G182), T215 (= T183), G256 (= G229), S300 (= S273), P326 (≠ C299), D327 (= D300)
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, 69% coverage: 11:324/455 of query aligns to 15:340/345 of 6c2zA
- binding calcium ion: N180 (vs. gap), D183 (≠ G169), N184 (≠ R170)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K50 (= K43), T78 (= T70), S79 (≠ A71), N81 (= N73), T82 (= T74), Q154 (= Q145), A192 (= A178), G193 (= G179), T194 (≠ S180), G195 (= G181), T197 (= T183), G242 (= G229), S286 (= S273), P315 (≠ C299), D316 (= D300)
6c2qA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-l-serine intermediate (see paper)
39% identity, 69% coverage: 11:324/455 of query aligns to 15:340/345 of 6c2qA
- binding calcium ion: N180 (vs. gap), D183 (≠ G169), N184 (≠ R170)
- binding L-Serine, N-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]: K50 (= K43), T78 (= T70), S79 (≠ A71), N81 (= N73), T82 (= T74), Q154 (= Q145), A192 (= A178), G193 (= G179), T194 (≠ S180), G195 (= G181), T197 (= T183), G242 (= G229), Y245 (≠ G232), S286 (= S273), P315 (≠ C299), D316 (= D300)
6c2hA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the catalytic core (see paper)
39% identity, 69% coverage: 11:324/455 of query aligns to 15:340/345 of 6c2hA
- binding calcium ion: N180 (vs. gap), D183 (≠ G169), N184 (≠ R170)
- binding pyridoxal-5'-phosphate: K50 (= K43), N81 (= N73), A192 (= A178), G193 (= G179), T194 (≠ S180), G195 (= G181), T197 (= T183), G242 (= G229), S286 (= S273), P315 (≠ C299), D316 (= D300)
6c4pA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex (see paper)
39% identity, 69% coverage: 11:324/455 of query aligns to 14:339/344 of 6c4pA
- binding calcium ion: N179 (vs. gap), D182 (≠ G169), N183 (≠ R170)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (= K43), N80 (= N73), A191 (= A178), G192 (= G179), T193 (≠ S180), G194 (= G181), T196 (= T183), G241 (= G229), S285 (= S273), P314 (≠ C299), D315 (= D300)
7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
36% identity, 96% coverage: 11:449/455 of query aligns to 9:455/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
36% identity, 96% coverage: 11:449/455 of query aligns to 9:455/458 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)
36% identity, 96% coverage: 11:449/455 of query aligns to 11:457/464 of P9WP51
- K428 (vs. gap) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
34% identity, 81% coverage: 6:372/455 of query aligns to 42:414/504 of 3pc4A
- active site: K82 (= K43), S312 (= S273)
- binding protoporphyrin ix containing fe: A189 (≠ P149), P192 (= P152), L193 (≠ A153), Y196 (≠ E156), R229 (= R189), T276 (≠ M237)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K43), T109 (= T70), S110 (≠ A71), N112 (= N73), T113 (= T74), Q185 (= Q145), A218 (= A178), G219 (= G179), T220 (≠ S180), A221 (≠ G181), T223 (= T183), G268 (= G229), I269 (= I230), Y271 (≠ G232), S312 (= S273), P338 (≠ C299), D339 (= D300)
Sites not aligning to the query:
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
34% identity, 81% coverage: 6:372/455 of query aligns to 42:414/504 of 3pc3A
- active site: K82 (= K43), S312 (= S273)
- binding protoporphyrin ix containing fe: A189 (≠ P149), P192 (= P152), L193 (≠ A153), Y196 (≠ E156), R229 (= R189)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K43), T109 (= T70), S110 (≠ A71), N112 (= N73), T113 (= T74), Q185 (= Q145), A218 (= A178), G219 (= G179), T220 (≠ S180), A221 (≠ G181), T223 (= T183), G268 (= G229), I269 (= I230), S312 (= S273), P338 (≠ C299), D339 (= D300)
Sites not aligning to the query:
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
34% identity, 81% coverage: 6:372/455 of query aligns to 40:412/500 of 3pc2A
- active site: K80 (= K43), S310 (= S273)
- binding protoporphyrin ix containing fe: A187 (≠ P149), P190 (= P152), L191 (≠ A153), Y194 (≠ E156), R227 (= R189)
- binding pyridoxal-5'-phosphate: K80 (= K43), N110 (= N73), A216 (= A178), G217 (= G179), T218 (≠ S180), A219 (≠ G181), T221 (= T183), G266 (= G229), S310 (= S273), P336 (≠ C299), D337 (= D300)
Sites not aligning to the query:
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)
39% identity, 65% coverage: 11:307/455 of query aligns to 8:288/303 of P16703
- N71 (= N73) binding
- S255 (= S273) binding
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
38% identity, 65% coverage: 11:307/455 of query aligns to 8:288/294 of 2bhtA
- active site: K41 (= K43), S69 (≠ A71), Q199 (≠ A203), G203 (= G207), S255 (= S273), C280 (= C299)
- binding pyridoxal-5'-phosphate: K41 (= K43), N71 (= N73), M173 (≠ A178), G174 (= G179), T175 (≠ S180), T176 (≠ G181), T178 (= T183), G208 (≠ D212), S255 (= S273), C280 (= C299)
Query Sequence
>WP_011384252.1 NCBI__GCF_000009985.1:WP_011384252.1
MPYDADLLCQIGNTPLIELTNLDTAPCRLFVKLESRNPSGSIKDRAALSMVRAAERDGLL
RPGGHLVEATAGNTGLALALLAAHRGYRLTLVIPDKAGLDKVSHLRAMGAEVVLARSDVP
RRHPEHYQNVASRLAGETGAHFIDQFNNPANPAAHEDGTGPELWEQMGGRVDAVVAGAGS
GGTLTGLSRFFARRSPATEMVLADPRGSVLADYVRTGRVGEAGSWLVEGIGGDSIPMVSD
FSRVTRAYSVSDRESFATARLVLRIEGLLVGSSSGTLLAAALRYCREQTAPKRVATLVCD
AGNRHLSRLHDESWLADQGLLQRDEHGDLRDLISRRHDEGAAITVRPDDTLSTAYNRMRV
NDVSQVPVVVGDRCIGLLDESDVLIALAEGKFGFDLPVRDAMTRKIETVTPQTPPERLLP
LFDRGWVAIVVDGERFLGLVTRMDLLNHLRRKLAA
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