SitesBLAST
Comparing WP_017598059.1 NCBI__GCF_000341125.1:WP_017598059.1 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)
P9WP51 Probable cystathionine beta-synthase Rv1077; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
65% identity, 100% coverage: 1:454/455 of query aligns to 1:458/464 of P9WP51
- K428 (≠ R424) 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)
65% identity, 99% coverage: 3:454/455 of query aligns to 1:456/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
65% identity, 99% coverage: 3:454/455 of query aligns to 1:456/458 of 7xnzB
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
38% identity, 100% coverage: 2:455/455 of query aligns to 35:495/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ Q151), P189 (= P154), L190 (≠ E155), Y193 (= Y158), R226 (= R191)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K44), T106 (= T71), S107 (= S72), N109 (= N74), T110 (= T75), Q182 (= Q147), G216 (= G181), T217 (= T182), G218 (= G183), T220 (= T185), G265 (= G225), S309 (= S269), P335 (= P295), D336 (= D296)
Sites not aligning to the query:
8s5hA Full-length human cystathionine beta-synthase with c-terminal 6xhis- tag, basal state, helical reconstruction (see paper)
40% identity, 88% coverage: 2:402/455 of query aligns to 34:438/507 of 8s5hA
Sites not aligning to the query:
4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
37% identity, 100% coverage: 2:455/455 of query aligns to 33:486/486 of 4pcuA
- active site: K77 (= K44), S105 (= S72), D237 (= D207), S305 (= S269)
- binding protoporphyrin ix containing fe: A182 (≠ Q151), P185 (= P154), L186 (≠ E155), Y189 (= Y158), R222 (= R191), T269 (≠ G233)
- binding pyridoxal-5'-phosphate: K77 (= K44), N107 (= N74), G212 (= G181), T213 (= T182), G214 (= G183), T216 (= T185), G261 (= G225), S305 (= S269), P331 (= P295), D332 (= D296)
- binding s-adenosylmethionine: P376 (≠ F340), G396 (= G360), F397 (≠ V361), D398 (≠ S362), Q399 (= Q363), T476 (= T445), I478 (≠ Q447), D479 (= D448)
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)
40% identity, 88% coverage: 2:402/455 of query aligns to 75:479/551 of P35520
- P78 (≠ D5) to R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
- 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 (= L26) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
- K102 (≠ A27) 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 (≠ V34) 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 (= R50) 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 (= M51) 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 pyridoxal 5'-phosphate
- 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 (≠ V98) 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 (≠ D101) 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 (= V105) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (≠ C116) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ A136) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ Q151) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N153) 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 (≠ S156) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ H159) 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 181:185) binding pyridoxal 5'-phosphate
- T257 (= T182) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (≠ S187) 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 (= R191) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (= K194) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ S197) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ G201) 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 (= I204) 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 (vs. gap) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ L222) 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 (= G225) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G227) 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 (≠ C240) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (= D241) to V: in CBSD; loss of activity
- R336 (= R256) 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 (= L258) 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 (= G267) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (= S269) 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 (≠ A273) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ V289) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D296) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (= R299) 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 (= K304) to E: in CBSD; severe form; dbSNP:rs121964967
- P422 (≠ F340) to L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
- P427 (= P345) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
- I435 (≠ V353) to T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
- R439 (= R357) to Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
- D444 (≠ S362) to N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
- V449 (≠ M367) to G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- L456 (≠ V379) to P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- S466 (≠ D389) to L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
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
- 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
1jbqA Structure of human cystathionine beta-synthase: a unique pyridoxal 5'- phosphate dependent hemeprotein (see paper)
44% identity, 69% coverage: 2:317/455 of query aligns to 33:348/348 of 1jbqA
- active site: K77 (= K44), S105 (= S72), D232 (= D207), S236 (= S211), L238 (vs. gap), S300 (= S269), P326 (= P295)
- binding protoporphyrin ix containing fe: A177 (≠ Q151), P180 (= P154), L181 (≠ E155), Y184 (= Y158), R217 (= R191)
- binding pyridoxal-5'-phosphate: K77 (= K44), N107 (= N74), V206 (≠ I180), G207 (= G181), T208 (= T182), G209 (= G183), G210 (= G184), T211 (= T185), G256 (= G225), S300 (= S269), P326 (= P295), D327 (= D296)
Sites not aligning to the query:
6c4pA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex (see paper)
46% identity, 67% coverage: 6:311/455 of query aligns to 9:330/344 of 6c4pA
- binding calcium ion: N179 (vs. gap), D182 (≠ G171), N183 (≠ R172)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (= K44), N80 (= N74), A191 (≠ I180), G192 (= G181), T193 (= T182), G194 (= G183), T196 (= T185), G241 (= G225), S285 (= S269), P314 (= P295), D315 (= D296)
6c2zA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-aminoacrylate intermediate (see paper)
46% identity, 67% coverage: 6:311/455 of query aligns to 10:331/345 of 6c2zA
- binding calcium ion: N180 (vs. gap), D183 (≠ G171), N184 (≠ R172)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K50 (= K44), T78 (= T71), S79 (= S72), N81 (= N74), T82 (= T75), Q154 (= Q147), A192 (≠ I180), G193 (= G181), T194 (= T182), G195 (= G183), T197 (= T185), G242 (= G225), S286 (= S269), P315 (= P295), D316 (= D296)
6c2qA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-l-serine intermediate (see paper)
46% identity, 67% coverage: 6:311/455 of query aligns to 10:331/345 of 6c2qA
- binding calcium ion: N180 (vs. gap), D183 (≠ G171), N184 (≠ R172)
- binding L-Serine, N-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]: K50 (= K44), T78 (= T71), S79 (= S72), N81 (= N74), T82 (= T75), Q154 (= Q147), A192 (≠ I180), G193 (= G181), T194 (= T182), G195 (= G183), T197 (= T185), G242 (= G225), Y245 (≠ E228), S286 (= S269), P315 (= P295), D316 (= D296)
6c2hA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the catalytic core (see paper)
46% identity, 67% coverage: 6:311/455 of query aligns to 10:331/345 of 6c2hA
- binding calcium ion: N180 (vs. gap), D183 (≠ G171), N184 (≠ R172)
- binding pyridoxal-5'-phosphate: K50 (= K44), N81 (= N74), A192 (≠ I180), G193 (= G181), T194 (= T182), G195 (= G183), T197 (= T185), G242 (= G225), S286 (= S269), P315 (= P295), D316 (= D296)
5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
37% identity, 100% coverage: 2:454/455 of query aligns to 30:486/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (≠ Q151), P184 (= P154), Y188 (= Y158), R221 (= R191)
- binding pyridoxal-5'-phosphate: K74 (= K44), N104 (= N74), G209 (= G179), G211 (= G181), T212 (= T182), G213 (= G183), G214 (= G184), T215 (= T185), G256 (= G225), S300 (= S269), P326 (= P295), D327 (= D296)
Sites not aligning to the query:
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
36% identity, 100% coverage: 2:454/455 of query aligns to 34:493/504 of Q2V0C9
- K78 (= K44) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N74) binding pyridoxal 5'-phosphate
- GTGGT 215:219 (= GTGGT 181:185) binding pyridoxal 5'-phosphate
- S307 (= S269) 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)
37% identity, 99% coverage: 3:454/455 of query aligns to 8:474/477 of 6xwlC
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
37% identity, 99% coverage: 3:454/455 of query aligns to 8:465/468 of 6xylA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K44), T82 (= T75), Q154 (= Q147), G188 (= G181), T189 (= T182), G190 (= G183), T192 (= T185), G238 (= G225), I239 (≠ V226), Y241 (≠ E228), S282 (= S269), P308 (= P295), D309 (= D296)
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
35% identity, 95% coverage: 2:435/455 of query aligns to 36:473/500 of 3pc2A
- active site: K80 (= K44), S310 (= S269)
- binding protoporphyrin ix containing fe: A187 (≠ Q151), P190 (= P154), L191 (≠ E155), Y194 (= Y158), R227 (= R191)
- binding pyridoxal-5'-phosphate: K80 (= K44), N110 (= N74), A216 (≠ I180), G217 (= G181), T218 (= T182), A219 (≠ G183), T221 (= T185), G266 (= G225), S310 (= S269), P336 (= P295), D337 (= D296)
Sites not aligning to the query:
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
35% identity, 95% coverage: 2:435/455 of query aligns to 38:475/504 of 3pc4A
- active site: K82 (= K44), S312 (= S269)
- binding protoporphyrin ix containing fe: A189 (≠ Q151), P192 (= P154), L193 (≠ E155), Y196 (= Y158), R229 (= R191), T276 (≠ G233)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K44), T109 (= T71), S110 (= S72), N112 (= N74), T113 (= T75), Q185 (= Q147), A218 (≠ I180), G219 (= G181), T220 (= T182), A221 (≠ G183), T223 (= T185), G268 (= G225), I269 (≠ V226), Y271 (≠ E228), S312 (= S269), P338 (= P295), D339 (= D296)
Sites not aligning to the query:
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
35% identity, 95% coverage: 2:435/455 of query aligns to 38:475/504 of 3pc3A
- active site: K82 (= K44), S312 (= S269)
- binding protoporphyrin ix containing fe: A189 (≠ Q151), P192 (= P154), L193 (≠ E155), Y196 (= Y158), R229 (= R191)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K44), T109 (= T71), S110 (= S72), N112 (= N74), T113 (= T75), Q185 (= Q147), A218 (≠ I180), G219 (= G181), T220 (= T182), A221 (≠ G183), T223 (= T185), G268 (= G225), I269 (≠ V226), S312 (= S269), P338 (= P295), D339 (= D296)
Sites not aligning to the query:
6vjuB Crystal structure of cystathionine beta synthase from legionella pneumophila with llp, plp, and homocysteine
44% identity, 69% coverage: 3:317/455 of query aligns to 3:317/317 of 6vjuB
Query Sequence
>WP_017598059.1 NCBI__GCF_000341125.1:WP_017598059.1
MRVHDSLIDLVGDTPLVRLRKVTEGLAPTILAKVEYFNPGGSVKDRIALRMVEAAEKSGE
LRAGGTIVEPTSGNTGIGLAMVAQEKGYRCVFVCPDKVGADKLAVLRAYGAEVVVCPTTV
APEHPDSYYSVSDRLAEEIPGAWKPNQYENQNNPESHYHSTGPEIWDQTEGRVTHFVAGI
GTGGTISGTGRYLKEVSDGRGKVIGADPEGSVYSGGSGRPYLVEGVGEDIWPGTYDTGIC
DDIVAVSDKESFLMTRRLAREEALLVGGSCGLAVEAALRVAEDAGPDDVIVVLLPDGGRG
YLGKIFNDEWMADYGFLSAETEEATAGQVLNGKGGEMPDFVHTHPHESIGTAVAIMREYG
VSQLPVMKEEPPVMAAEVVGSIAERDVLDALFDGRAQLDDSVETHMGKPLATVGTGTPVG
DCVRLLRGSGALVVLRDGRPVGILTRQDLLAHLSG
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