SitesBLAST
Comparing WP_012116647.1 NCBI__GCF_000017645.1:WP_012116647.1 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)
4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
40% identity, 97% coverage: 6:336/342 of query aligns to 38:369/486 of 4pcuA
- active site: K77 (= K43), S105 (≠ A71), D237 (= D209), S305 (= S278)
- binding protoporphyrin ix containing fe: A182 (≠ V154), P185 (≠ R157), L186 (≠ Q158), Y189 (≠ I161), R222 (≠ I194), T269 (≠ A242)
- binding pyridoxal-5'-phosphate: K77 (= K43), N107 (= N73), G212 (= G184), T213 (= T185), G214 (= G186), T216 (= T188), G261 (= G234), S305 (= S278), P331 (≠ C304), D332 (= D305)
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
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
40% identity, 97% coverage: 6:336/342 of query aligns to 40:375/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ V154), P189 (≠ R157), L190 (≠ Q158), Y193 (≠ I161), R226 (≠ I194)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K43), T106 (= T70), S107 (≠ A71), N109 (= N73), T110 (= T74), Q182 (= Q150), G216 (= G184), T217 (= T185), G218 (= G186), T220 (= T188), G265 (= G234), S309 (= S278), P335 (≠ C304), D336 (= D305)
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, 97% coverage: 6:336/342 of query aligns to 39:374/507 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)
40% identity, 97% coverage: 6:336/342 of query aligns to 80:415/551 of P35520
- G85 (= G11) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T13) 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 (≠ A33) 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 (≠ G49) 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 (≠ I50) to V: in CBSD; loss of activity
- E131 (≠ V55) 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 pyridoxal 5'-phosphate
- 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 (≠ T89) 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 (≠ Q97) 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 (= E100) 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 (≠ M104) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (≠ V115) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ A134) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ V154) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N156) 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 (= A159) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ E162) 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 184:188) binding pyridoxal 5'-phosphate
- T257 (= T185) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (≠ A190) 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 (≠ I194) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (= K197) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ N200) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ I203) 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 (≠ G206) 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 (= D209) to N: in CBSD; loss of activity
- A288 (≠ Y216) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ S230) 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 (= G234) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G236) 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 (≠ I249) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (= D250) to V: in CBSD; loss of activity
- R336 (≠ F265) 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 (= L267) 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 (= G276) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (= S278) 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 (≠ N282) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ T298) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D305) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (≠ T308) 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 (= K313) 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
1jbqA Structure of human cystathionine beta-synthase: a unique pyridoxal 5'- phosphate dependent hemeprotein (see paper)
40% identity, 94% coverage: 6:325/342 of query aligns to 38:347/348 of 1jbqA
- active site: K77 (= K43), S105 (≠ A71), D232 (= D209), S236 (≠ A213), L238 (= L215), S300 (= S278), P326 (≠ C304)
- binding protoporphyrin ix containing fe: A177 (≠ V154), P180 (≠ R157), L181 (≠ Q158), Y184 (≠ I161), R217 (≠ I194)
- binding pyridoxal-5'-phosphate: K77 (= K43), N107 (= N73), V206 (= V183), G207 (= G184), T208 (= T185), G209 (= G186), G210 (= G187), T211 (= T188), G256 (= G234), S300 (= S278), P326 (≠ C304), D327 (= D305)
Sites not aligning to the query:
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
41% identity, 89% coverage: 9:312/342 of query aligns to 6:297/302 of 2efyA
- active site: K40 (= K43), S70 (≠ A71), E200 (≠ D209), S204 (≠ Y216), S263 (= S278)
- binding 5-oxohexanoic acid: T69 (= T70), G71 (= G72), T73 (= T74), Q141 (= Q150), G175 (= G184), G219 (= G234), M220 (≠ I235), P222 (≠ Q237)
- binding pyridoxal-5'-phosphate: K40 (= K43), N72 (= N73), Y172 (≠ C181), G175 (= G184), T176 (= T185), G177 (= G186), T179 (= T188), G219 (= G234), S263 (= S278), P289 (≠ C304), D290 (= D305)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
41% identity, 89% coverage: 9:312/342 of query aligns to 6:297/302 of 2ecqA
- active site: K40 (= K43), S70 (≠ A71), E200 (≠ D209), S204 (≠ Y216), S263 (= S278)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K43), G71 (= G72), T73 (= T74), Q141 (= Q150), G219 (= G234)
- binding pyridoxal-5'-phosphate: K40 (= K43), N72 (= N73), Y172 (≠ C181), G173 (≠ A182), G175 (= G184), T176 (= T185), T179 (= T188), G219 (= G234), S263 (= S278), P289 (≠ C304)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
41% identity, 89% coverage: 9:312/342 of query aligns to 6:297/302 of 2ecoA
- active site: K40 (= K43), S70 (≠ A71), E200 (≠ D209), S204 (≠ Y216), S263 (= S278)
- binding 4-methyl valeric acid: K40 (= K43), T69 (= T70), G71 (= G72), T73 (= T74), Q141 (= Q150), G175 (= G184), T176 (= T185), G219 (= G234)
- binding pyridoxal-5'-phosphate: K40 (= K43), N72 (= N73), Y172 (≠ C181), G175 (= G184), T176 (= T185), T179 (= T188), G219 (= G234), S263 (= S278), P289 (≠ C304), D290 (= D305)
6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
35% identity, 93% coverage: 2:320/342 of query aligns to 8:324/477 of 6xwlC
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
35% identity, 93% coverage: 2:320/342 of query aligns to 8:324/468 of 6xylA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K43), T82 (= T74), Q154 (= Q150), G188 (= G184), T189 (= T185), G190 (= G186), T192 (= T188), G238 (= G234), I239 (= I235), Y241 (≠ Q237), S282 (= S278), P308 (≠ C304), D309 (= D305)
6c2zA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-aminoacrylate intermediate (see paper)
34% identity, 94% coverage: 3:325/342 of query aligns to 8:336/345 of 6c2zA
- binding calcium ion: N180 (vs. gap), D183 (≠ G174), N184 (≠ K175)
- 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 (= Q150), A192 (≠ V183), G193 (= G184), T194 (= T185), G195 (= G186), T197 (= T188), G242 (= G234), S286 (= S278), P315 (≠ C304), D316 (= D305)
6c2qA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-l-serine intermediate (see paper)
34% identity, 94% coverage: 3:325/342 of query aligns to 8:336/345 of 6c2qA
- binding calcium ion: N180 (vs. gap), D183 (≠ G174), N184 (≠ K175)
- 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 (= Q150), A192 (≠ V183), G193 (= G184), T194 (= T185), G195 (= G186), T197 (= T188), G242 (= G234), Y245 (≠ Q237), S286 (= S278), P315 (≠ C304), D316 (= D305)
6c2hA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the catalytic core (see paper)
34% identity, 94% coverage: 3:325/342 of query aligns to 8:336/345 of 6c2hA
- binding calcium ion: N180 (vs. gap), D183 (≠ G174), N184 (≠ K175)
- binding pyridoxal-5'-phosphate: K50 (= K43), N81 (= N73), A192 (≠ V183), G193 (= G184), T194 (= T185), G195 (= G186), T197 (= T188), G242 (= G234), S286 (= S278), P315 (≠ C304), D316 (= D305)
6c4pA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex (see paper)
34% identity, 94% coverage: 3:325/342 of query aligns to 7:335/344 of 6c4pA
- binding calcium ion: N179 (vs. gap), D182 (≠ G174), N183 (≠ K175)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (= K43), N80 (= N73), A191 (≠ V183), G192 (= G184), T193 (= T185), G194 (= G186), T196 (= T188), G241 (= G234), S285 (= S278), P314 (≠ C304), D315 (= D305)
7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
39% identity, 92% coverage: 10:322/342 of query aligns to 9:311/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
39% identity, 92% coverage: 10:322/342 of query aligns to 9:311/458 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)
39% identity, 92% coverage: 10:322/342 of query aligns to 11:313/464 of P9WP51
Sites not aligning to the query:
- 428 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
39% identity, 94% coverage: 6:328/342 of query aligns to 39:357/504 of Q2V0C9
- K78 (= K43) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N73) binding pyridoxal 5'-phosphate
- GTGGT 215:219 (= GTGGT 184:188) binding pyridoxal 5'-phosphate
- S307 (= S278) binding pyridoxal 5'-phosphate
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)
39% identity, 94% coverage: 6:328/342 of query aligns to 35:350/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (≠ V154), P184 (≠ R157), Y188 (≠ I161), R221 (≠ I194)
- binding pyridoxal-5'-phosphate: K74 (= K43), N104 (= N73), G209 (≠ A182), G211 (= G184), T212 (= T185), G213 (= G186), G214 (= G187), T215 (= T188), G256 (= G234), S300 (= S278), P326 (≠ C304), D327 (= D305)
Sites not aligning to the query:
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
37% identity, 90% coverage: 6:312/342 of query aligns to 4:288/294 of 2bhtA
- active site: K41 (= K43), S69 (≠ A71), Q199 (≠ L224), G203 (= G228), S255 (= S278), C280 (= C304)
- binding pyridoxal-5'-phosphate: K41 (= K43), N71 (= N73), M173 (≠ V183), G174 (= G184), T175 (= T185), T176 (≠ G186), T178 (= T188), G208 (= G234), S255 (= S278), C280 (= C304)
Query Sequence
>WP_012116647.1 NCBI__GCF_000017645.1:WP_012116647.1
MIRNGLVDSIGNTPLIRLKRASEETGCEILGKAEFLNPGQSVKDRAALGIIKDAVARGAL
KPGGVIVEGTAGNTGIGLALVAAPLGFRTVIVIPETQSQEKKDMLKLAGAILVEVPAVAY
ANPNNYVKVSGRLAEALAKTEPNGAIWANQFDNVANRQAHIETTGPEIWEQTCGKLDGFI
CAVGTGGTLAGIAIALKARNPNIRIGLADPMGAALYSYYTTGELKAEGSSITEGIGQGRI
TANLVDAPIDTAFQIPDEEALPVVFDLLQHEGLCLGGSSGVNVAGAIRLAKEMGPGHTIV
TILCDYGTRYQSKLFNPEFLRSKNLPVPEWLERKVEVPNVLV
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