SitesBLAST
Comparing WP_013420517.1 NCBI__GCF_000166055.1:WP_013420517.1 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)
39% identity, 96% coverage: 13:348/351 of query aligns to 37:383/486 of 4pcuA
- active site: K77 (= K51), S105 (≠ A79), D237 (= D217), S305 (= S286)
- binding protoporphyrin ix containing fe: A182 (≠ I162), P185 (≠ R165), L186 (≠ R166), Y189 (≠ V169), R222 (≠ L202), T269 (≠ A250)
- binding pyridoxal-5'-phosphate: K77 (= K51), N107 (= N81), G212 (= G192), T213 (= T193), G214 (= G194), T216 (= T196), G261 (= G242), S305 (= S286), P331 (≠ C312), D332 (= D313)
- binding s-adenosylmethionine: P376 (= P342)
Sites not aligning to the query:
- binding protoporphyrin ix containing fe: 8, 9, 10, 11, 12, 20, 21, 22, 23
- binding s-adenosylmethionine: 396, 397, 398, 399, 476, 478, 479
P35520 Cystathionine beta-synthase; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Homo sapiens (Human) (see 40 papers)
40% identity, 91% coverage: 13:333/351 of query aligns to 79:396/551 of P35520
- G85 (= G19) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T21) 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 (≠ A41) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P46) 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 (= K51) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ F57) 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 (≠ I58) to V: in CBSD; loss of activity
- E131 (≠ V63) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G71) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (≠ V75) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (= E76) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G80) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N81) binding pyridoxal 5'-phosphate
- L154 (≠ I86) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (= A87) 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 (≠ A97) 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 (≠ Q105) 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 (= E108) 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 (≠ A112) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (≠ V123) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ A142) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ I162) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N164) 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 (= A167) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ E170) 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 192:196) binding pyridoxal 5'-phosphate
- T257 (= T193) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (≠ A198) 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 (≠ L202) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (= K205) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ R208) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ V211) 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 (≠ A214) 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 (= D217) to N: in CBSD; loss of activity
- A288 (≠ Y224) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ S238) 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 (= G242) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G244) 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 (= V257) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (= D258) to V: in CBSD; loss of activity
- R336 (≠ F273) 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 (= L275) 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 (= G284) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (= S286) 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 (≠ N290) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ T306) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D313) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (≠ T316) 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 (= K321) 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
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
40% identity, 91% coverage: 13:333/351 of query aligns to 39:356/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ I162), P189 (≠ R165), L190 (≠ R166), Y193 (≠ V169), R226 (≠ L202)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K51), T106 (= T78), S107 (≠ A79), N109 (= N81), T110 (= T82), Q182 (= Q158), G216 (= G192), T217 (= T193), G218 (= G194), T220 (= T196), G265 (= G242), S309 (= S286), P335 (≠ C312), D336 (= D313)
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, 91% coverage: 13:333/351 of query aligns to 38:355/507 of 8s5hA
Sites not aligning to the query:
1jbqA Structure of human cystathionine beta-synthase: a unique pyridoxal 5'- phosphate dependent hemeprotein (see paper)
40% identity, 91% coverage: 13:333/351 of query aligns to 37:347/348 of 1jbqA
- active site: K77 (= K51), S105 (≠ A79), D232 (= D217), S236 (= S221), L238 (≠ I223), S300 (= S286), P326 (≠ C312)
- binding protoporphyrin ix containing fe: A177 (≠ I162), P180 (≠ R165), L181 (≠ R166), Y184 (≠ V169), R217 (≠ L202)
- binding pyridoxal-5'-phosphate: K77 (= K51), N107 (= N81), V206 (= V191), G207 (= G192), T208 (= T193), G209 (= G194), G210 (= G195), T211 (= T196), G256 (= G242), S300 (= S286), P326 (≠ C312), D327 (= D313)
Sites not aligning to the query:
6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
36% identity, 93% coverage: 8:333/351 of query aligns to 6:329/477 of 6xwlC
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
36% identity, 93% coverage: 8:333/351 of query aligns to 6:329/468 of 6xylA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K51), T82 (= T82), Q154 (= Q158), G188 (= G192), T189 (= T193), G190 (= G194), T192 (= T196), G238 (= G242), I239 (= I243), Y241 (≠ Q245), S282 (= S286), P308 (≠ C312), D309 (= D313)
5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
36% identity, 95% coverage: 2:336/351 of query aligns to 23:350/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (≠ I162), P184 (≠ R165), Y188 (≠ V169), R221 (≠ L202)
- binding pyridoxal-5'-phosphate: K74 (= K51), N104 (= N81), G209 (≠ S190), G211 (= G192), T212 (= T193), G213 (= G194), G214 (= G195), T215 (= T196), G256 (= G242), S300 (= S286), P326 (≠ C312), D327 (= D313)
Sites not aligning to the query:
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
36% identity, 95% coverage: 2:336/351 of query aligns to 27:357/504 of Q2V0C9
- K78 (= K51) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N81) binding pyridoxal 5'-phosphate
- GTGGT 215:219 (= GTGGT 192:196) binding pyridoxal 5'-phosphate
- S307 (= S286) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 12 binding axial binding residue
- 23 binding axial binding residue
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
39% identity, 87% coverage: 14:320/351 of query aligns to 3:297/302 of 2efyA
- active site: K40 (= K51), S70 (≠ A79), E200 (≠ D217), S204 (= S221), S263 (= S286)
- binding 5-oxohexanoic acid: T69 (= T78), G71 (= G80), T73 (= T82), Q141 (= Q158), G175 (= G192), G219 (= G242), M220 (≠ I243), P222 (≠ Q245)
- binding pyridoxal-5'-phosphate: K40 (= K51), N72 (= N81), Y172 (≠ C189), G175 (= G192), T176 (= T193), G177 (= G194), T179 (= T196), G219 (= G242), S263 (= S286), P289 (≠ C312), D290 (= D313)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
39% identity, 87% coverage: 14:320/351 of query aligns to 3:297/302 of 2ecqA
- active site: K40 (= K51), S70 (≠ A79), E200 (≠ D217), S204 (= S221), S263 (= S286)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K51), G71 (= G80), T73 (= T82), Q141 (= Q158), G219 (= G242)
- binding pyridoxal-5'-phosphate: K40 (= K51), N72 (= N81), Y172 (≠ C189), G173 (≠ S190), G175 (= G192), T176 (= T193), T179 (= T196), G219 (= G242), S263 (= S286), P289 (≠ C312)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
39% identity, 87% coverage: 14:320/351 of query aligns to 3:297/302 of 2ecoA
- active site: K40 (= K51), S70 (≠ A79), E200 (≠ D217), S204 (= S221), S263 (= S286)
- binding 4-methyl valeric acid: K40 (= K51), T69 (= T78), G71 (= G80), T73 (= T82), Q141 (= Q158), G175 (= G192), T176 (= T193), G219 (= G242)
- binding pyridoxal-5'-phosphate: K40 (= K51), N72 (= N81), Y172 (≠ C189), G175 (= G192), T176 (= T193), T179 (= T196), G219 (= G242), S263 (= S286), P289 (≠ C312), D290 (= D313)
7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
40% identity, 90% coverage: 18:333/351 of query aligns to 9:314/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
40% identity, 90% coverage: 18:333/351 of query aligns to 9:314/458 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)
40% identity, 90% coverage: 18:333/351 of query aligns to 11:316/464 of P9WP51
Sites not aligning to the query:
- 428 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)
36% identity, 92% coverage: 13:336/351 of query aligns to 42:362/504 of 3pc4A
- active site: K82 (= K51), S312 (= S286)
- binding protoporphyrin ix containing fe: A189 (≠ I162), P192 (≠ R165), L193 (≠ R166), Y196 (≠ V169), R229 (≠ L202), T276 (≠ A250)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K51), T109 (= T78), S110 (≠ A79), N112 (= N81), T113 (= T82), Q185 (= Q158), A218 (≠ V191), G219 (= G192), T220 (= T193), A221 (≠ G194), T223 (= T196), G268 (= G242), I269 (= I243), Y271 (≠ Q245), S312 (= S286), P338 (≠ C312), D339 (= D313)
Sites not aligning to the query:
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
36% identity, 92% coverage: 13:336/351 of query aligns to 42:362/504 of 3pc3A
- active site: K82 (= K51), S312 (= S286)
- binding protoporphyrin ix containing fe: A189 (≠ I162), P192 (≠ R165), L193 (≠ R166), Y196 (≠ V169), R229 (≠ L202)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K51), T109 (= T78), S110 (≠ A79), N112 (= N81), T113 (= T82), Q185 (= Q158), A218 (≠ V191), G219 (= G192), T220 (= T193), A221 (≠ G194), T223 (= T196), G268 (= G242), I269 (= I243), S312 (= S286), P338 (≠ C312), D339 (= D313)
Sites not aligning to the query:
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
36% identity, 92% coverage: 13:336/351 of query aligns to 40:360/500 of 3pc2A
- active site: K80 (= K51), S310 (= S286)
- binding protoporphyrin ix containing fe: A187 (≠ I162), P190 (≠ R165), L191 (≠ R166), Y194 (≠ V169), R227 (≠ L202)
- binding pyridoxal-5'-phosphate: K80 (= K51), N110 (= N81), A216 (≠ V191), G217 (= G192), T218 (= T193), A219 (≠ G194), T221 (= T196), G266 (= G242), S310 (= S286), P336 (≠ C312), D337 (= D313)
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)
37% identity, 92% coverage: 12:333/351 of query aligns to 2:303/303 of P16703
- N71 (= N81) binding pyridoxal 5'-phosphate
- S255 (= S286) binding pyridoxal 5'-phosphate
6vjuB Crystal structure of cystathionine beta synthase from legionella pneumophila with llp, plp, and homocysteine
37% identity, 91% coverage: 13:333/351 of query aligns to 6:316/317 of 6vjuB
Query Sequence
>WP_013420517.1 NCBI__GCF_000166055.1:WP_013420517.1
MTHANDTSALKSSVIAAIGNTPLIRLKRASEETGCEIYGKAEFMNPGQSVKDRAALFIVE
DAVKRGQLKPGGTIVEGTAGNTGIGIALVANALGYKAVIVIPETQSQEKKDALRLLGATL
VEVPAVPYKNANNYVKYSARLAHKLAAERPEGAVWANQFDNIANRRAHVETTAEEIWRQT
AGRVDGFICSVGTGGTLAGTSLGLKAKRPGVVVAVADPFGSAIYSHYAHGRLEATGSSIT
EGIGQGRITANLAGAGVDGAYQIPDEEALDVVFRLLSEEGLCVGGSTGINVAGAVRLARD
LGPGHTIVTILCDYGTRYQSKLFNPEFLRGKGLPVPPWLDAPQTLPTVFEG
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