SitesBLAST
Comparing Dsui_2043 FitnessBrowser__PS:Dsui_2043 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)
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
34% identity, 88% coverage: 52:493/501 of query aligns to 41:491/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ P194), P189 (= P197), L190 (≠ K198), Y193 (≠ E201), R226 (= R234)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K87), T106 (= T114), S107 (≠ A115), N109 (= N117), T110 (= T118), Q182 (= Q190), G216 (= G224), T217 (≠ S225), G218 (= G226), T220 (= T228), G265 (= G274), S309 (= S318), P335 (≠ C344), D336 (= D345)
Sites not aligning to the query:
7qgtA Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
34% identity, 88% coverage: 52:493/501 of query aligns to 41:491/500 of 7qgtA
- binding protoporphyrin ix containing fe: A186 (≠ P194), P189 (= P197), L190 (≠ K198), Y193 (≠ E201), R226 (= R234)
- binding pyridoxal-5'-phosphate: K79 (= K87), N109 (= N117), G216 (= G224), T217 (≠ S225), G218 (= G226), T220 (= T228), G265 (= G274), S309 (= S318), P335 (≠ C344), D336 (= D345)
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)
38% identity, 88% coverage: 53:495/501 of query aligns to 9:457/464 of P9WP51
- K428 (≠ P466) 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)
38% identity, 88% coverage: 53:495/501 of query aligns to 7:455/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
38% identity, 88% coverage: 53:495/501 of query aligns to 7:455/458 of 7xnzB
4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
34% identity, 88% coverage: 52:493/501 of query aligns to 39:482/486 of 4pcuA
- active site: K77 (= K87), S105 (≠ A115), D237 (= D249), S305 (= S318)
- binding protoporphyrin ix containing fe: A182 (≠ P194), P185 (= P197), L186 (≠ K198), Y189 (≠ E201), R222 (= R234), T269 (≠ P282)
- binding pyridoxal-5'-phosphate: K77 (= K87), N107 (= N117), G212 (= G224), T213 (≠ S225), G214 (= G226), T216 (= T228), G261 (= G274), S305 (= S318), P331 (≠ C344), D332 (= D345)
- binding s-adenosylmethionine: P376 (≠ V387), G396 (≠ D407), F397 (≠ V408), D398 (≠ S409), Q399 (= Q410), T476 (= T487), I478 (= I489), D479 (= D490)
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, 97% coverage: 8:493/501 of query aligns to 14:541/551 of P35520
- R18 (= R12) to C: results in 1/3 to 2/3 the enzyme activity of the wild-type; dbSNP:rs201827340
- P49 (= P24) to L: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs148865119
- C52 (≠ F25) binding axial binding residue
- R58 (= R31) to W: in CBSD; linked with V-114; 18% of activity; dbSNP:rs555959266
- H65 (≠ A38) binding axial binding residue; to R: in CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs1191141364
- A69 (= A42) to P: in dbSNP:rs17849313
- P78 (= P48) to R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
- G85 (= G56) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T58) 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 (≠ P70) 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 (≠ L77) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P82) 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 (= K87) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ S93) 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 (= M94) to V: in CBSD; loss of activity
- E131 (= E99) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G107) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (≠ V111) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (= E112) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G116) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N117) binding
- L154 (= L122) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (≠ T123) 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 (≠ V133) 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 (= M141) 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 (= E144) 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 (≠ A148) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (= T159) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ A179) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ P194) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N196) 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 (= A199) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ T202) 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 224:228) binding
- T257 (≠ S225) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (= T230) 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 (= R234) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (≠ R237) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ S240) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ V243) 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 (≠ V246) 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 (= D249) to N: in CBSD; loss of activity
- A288 (= A256) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ L271) 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 (= G274) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G276) 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 (= V289) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (≠ R290) to V: in CBSD; loss of activity
- R336 (= R305) 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 (= L307) 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 (= G316) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (= S318) 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 (≠ L322) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ H338) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D345) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (≠ N348) 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 (= K353) to E: in CBSD; severe form; dbSNP:rs121964967
- P422 (≠ V387) to L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
- P427 (= P392) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
- I435 (≠ Y400) to T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
- R439 (≠ K404) to Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
- D444 (≠ S409) to N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
- V449 (≠ T414) to G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- L456 (≠ V421) to P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- S466 (≠ L431) to L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
- S500 (≠ L465) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
- Q526 (≠ D478) to K: in CBSD; has significantly decreased levels of enzyme activity
- L539 (= L491) to S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
- L540 (= L492) to Q: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
Sites not aligning to the query:
- 548 R → Q: presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; dbSNP:rs150828989
6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
36% identity, 91% coverage: 43:498/501 of query aligns to 4:476/477 of 6xwlC
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
33% identity, 94% coverage: 28:497/501 of query aligns to 5:494/504 of Q2V0C9
- C12 (≠ T35) binding axial binding residue
- H23 (≠ S44) binding axial binding residue
- K78 (= K87) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N117) binding
- GTGGT 215:219 (≠ GSGGT 224:228) binding
- S307 (= S318) binding
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
35% identity, 91% coverage: 43:498/501 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 (= K87), T82 (= T118), Q154 (= Q190), G188 (= G224), T189 (≠ S225), G190 (= G226), T192 (= T228), G238 (= G274), I239 (= I275), Y241 (≠ E277), S282 (= S318), P308 (≠ C344), D309 (= D345)
5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
33% identity, 94% coverage: 28:497/501 of query aligns to 1:487/488 of 5ohxA
- binding protoporphyrin ix containing fe: R4 (= R31), Y7 (≠ M34), C8 (≠ T35), T9 (vs. gap), W10 (vs. gap), A14 (= A39), N16 (≠ L41), S17 (≠ A42), P18 (= P43), H19 (≠ S44), P181 (= P194), P184 (= P197), Y188 (≠ E201), R221 (= R234)
- binding pyridoxal-5'-phosphate: K74 (= K87), N104 (= N117), G209 (= G222), G211 (= G224), T212 (≠ S225), G213 (= G226), G214 (= G227), T215 (= T228), G256 (= G274), S300 (= S318), P326 (≠ C344), D327 (= D345)
6c4pA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex (see paper)
38% identity, 64% coverage: 52:370/501 of query aligns to 11:340/344 of 6c4pA
- binding calcium ion: N179 (vs. gap), D182 (≠ G214), N183 (≠ R215)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (= K87), N80 (= N117), A191 (≠ V223), G192 (= G224), T193 (≠ S225), G194 (= G226), T196 (= T228), G241 (= G274), S285 (= S318), P314 (≠ C344), D315 (= D345)
6c2zA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-aminoacrylate intermediate (see paper)
38% identity, 64% coverage: 52:370/501 of query aligns to 12:341/345 of 6c2zA
- binding calcium ion: N180 (vs. gap), D183 (≠ G214), N184 (≠ R215)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K50 (= K87), T78 (= T114), S79 (≠ A115), N81 (= N117), T82 (= T118), Q154 (= Q190), A192 (≠ V223), G193 (= G224), T194 (≠ S225), G195 (= G226), T197 (= T228), G242 (= G274), S286 (= S318), P315 (≠ C344), D316 (= D345)
6c2qA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-l-serine intermediate (see paper)
38% identity, 64% coverage: 52:370/501 of query aligns to 12:341/345 of 6c2qA
- binding calcium ion: N180 (vs. gap), D183 (≠ G214), N184 (≠ R215)
- binding L-Serine, N-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]: K50 (= K87), T78 (= T114), S79 (≠ A115), N81 (= N117), T82 (= T118), Q154 (= Q190), A192 (≠ V223), G193 (= G224), T194 (≠ S225), G195 (= G226), T197 (= T228), G242 (= G274), Y245 (≠ E277), S286 (= S318), P315 (≠ C344), D316 (= D345)
6c2hA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the catalytic core (see paper)
38% identity, 64% coverage: 52:370/501 of query aligns to 12:341/345 of 6c2hA
- binding calcium ion: N180 (vs. gap), D183 (≠ G214), N184 (≠ R215)
- binding pyridoxal-5'-phosphate: K50 (= K87), N81 (= N117), A192 (≠ V223), G193 (= G224), T194 (≠ S225), G195 (= G226), T197 (= T228), G242 (= G274), S286 (= S318), P315 (≠ C344), D316 (= D345)
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
34% identity, 81% coverage: 52:455/501 of query aligns to 44:453/504 of 3pc4A
- active site: K82 (= K87), S312 (= S318)
- binding protoporphyrin ix containing fe: A189 (≠ P194), P192 (= P197), L193 (≠ K198), Y196 (≠ E201), R229 (= R234), T276 (≠ P282)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K87), T109 (= T114), S110 (≠ A115), N112 (= N117), T113 (= T118), Q185 (= Q190), A218 (≠ V223), G219 (= G224), T220 (≠ S225), A221 (≠ G226), T223 (= T228), G268 (= G274), I269 (= I275), Y271 (≠ E277), S312 (= S318), P338 (≠ C344), D339 (= D345)
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: 52:455/501 of query aligns to 44:453/504 of 3pc3A
- active site: K82 (= K87), S312 (= S318)
- binding protoporphyrin ix containing fe: A189 (≠ P194), P192 (= P197), L193 (≠ K198), Y196 (≠ E201), R229 (= R234)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K87), T109 (= T114), S110 (≠ A115), N112 (= N117), T113 (= T118), Q185 (= Q190), A218 (≠ V223), G219 (= G224), T220 (≠ S225), A221 (≠ G226), T223 (= T228), G268 (= G274), I269 (= I275), S312 (= S318), P338 (≠ C344), D339 (= D345)
Sites not aligning to the query:
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
34% identity, 81% coverage: 52:455/501 of query aligns to 42:451/500 of 3pc2A
- active site: K80 (= K87), S310 (= S318)
- binding protoporphyrin ix containing fe: A187 (≠ P194), P190 (= P197), L191 (≠ K198), Y194 (≠ E201), R227 (= R234)
- binding pyridoxal-5'-phosphate: K80 (= K87), N110 (= N117), A216 (≠ V223), G217 (= G224), T218 (≠ S225), A219 (≠ G226), T221 (= T228), G266 (= G274), S310 (= S318), P336 (≠ C344), D337 (= D345)
Sites not aligning to the query:
6vjuB Crystal structure of cystathionine beta synthase from legionella pneumophila with llp, plp, and homocysteine
41% identity, 63% coverage: 52:366/501 of query aligns to 8:317/317 of 6vjuB
G5EFH8 Cystathionine beta-synthase cbs-1; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Caenorhabditis elegans (see paper)
38% identity, 68% coverage: 27:366/501 of query aligns to 371:702/704 of G5EFH8
- K421 (= K87) mutation to A: Binds significantly less of the PLP cofactor. Altered fluorescence-based tryptophan spectra.
Query Sequence
>Dsui_2043 FitnessBrowser__PS:Dsui_2043
MTAATGHGAPSRAGPNLHLSPPAPFVFQPNRDSMTDTAATLAPSATLPRSSLDLIGATPL
VEVTHFDTGPCRLFLKLESQNPGGSIKDRVARSMIDAAEKEGLIKPGSTLVEATAGNTGL
ALTLVGAQRGYKVVLVVPDKMSQEKIFALKALGARVVMTRSDVGVGHPEYYQDMAQRLAS
EIPGAWYVNQFGNPNNPKAHETGTGPELWSQLKGRIDAVVCGVGSGGTLTGLTRFFRQKS
PRVKMVLADPAGSVLADYVAHGYIKEAGSWLVEGIGEDFIPPICDLTGVREAYTVPDAES
FAAARELLRKEGIMGGSSTGTLLAAALRYCRTRTKPEHVVTFVCDHGNRYLSKMYNDFWM
ADQGFLPKDVRGDLRDIIGRRADEGAVVTVAPTDTVLTAYGRFKLYDVSQLPVTNDEGRI
VGLIDESDLLLAITKDEANFRQPVKKFMTSRLTTLPPTAPISDLLPLFDQGLVPIVVDGD
RFLGLVTRIDLLNHLRRKLKS
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