SitesBLAST
Comparing WP_010875114.1 NCBI__GCF_000018545.1:WP_010875114.1 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)
8s5hA Full-length human cystathionine beta-synthase with c-terminal 6xhis- tag, basal state, helical reconstruction (see paper)
33% identity, 97% coverage: 6:330/336 of query aligns to 39:369/507 of 8s5hA
Sites not aligning to the query:
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
33% identity, 97% coverage: 6:330/336 of query aligns to 40:370/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ P150), P189 (= P153), L190 (vs. gap), Y193 (= Y156), R226 (≠ Q189)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K41), T106 (≠ S68), S107 (= S69), N109 (= N71), T110 (= T72), Q182 (= Q146), G216 (= G179), T217 (= T180), G218 (= G181), T220 (≠ S183), G265 (= G228), S309 (= S269), P335 (≠ A295), D336 (= D296)
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)
33% identity, 97% coverage: 6:330/336 of query aligns to 80:410/551 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 (≠ I31) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P36) 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 (= K41) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ S47) 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 (= M48) to V: in CBSD; loss of activity
- E131 (≠ L53) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G61) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (≠ V65) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (= E66) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G70) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N71) binding pyridoxal 5'-phosphate
- L154 (= L76) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (= A77) 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 (≠ F87) 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 (≠ A95) 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 (≠ D98) 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 (≠ M102) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (≠ V113) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ G135) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ P150) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N152) 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 (≠ E154) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ T157) 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 (≠ GTGGS 179:183) binding pyridoxal 5'-phosphate
- T257 (= T180) 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 (≠ Q189) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (= K192) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ N195) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ V198) 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 (= I201) 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 (≠ E204) to N: in CBSD; loss of activity
- A288 (≠ G212) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ Y219) 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 (= G222) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G224) 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 (≠ I240) 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 (≠ I258) 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 (≠ T289) 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 (≠ E299) 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 (≠ T304) 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
4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
34% identity, 93% coverage: 6:317/336 of query aligns to 38:353/486 of 4pcuA
- active site: K77 (= K41), S105 (= S69), D237 (≠ E204), S305 (= S269)
- binding protoporphyrin ix containing fe: A182 (≠ P150), P185 (= P153), L186 (vs. gap), Y189 (= Y156), R222 (≠ Q189), T269 (≠ K233)
- binding pyridoxal-5'-phosphate: K77 (= K41), N107 (= N71), G212 (= G179), T213 (= T180), G214 (= G181), T216 (≠ S183), G261 (= G222), S305 (= S269), P331 (≠ A295), D332 (= D296)
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
1jbqA Structure of human cystathionine beta-synthase: a unique pyridoxal 5'- phosphate dependent hemeprotein (see paper)
34% identity, 93% coverage: 6:317/336 of query aligns to 38:348/348 of 1jbqA
- active site: K77 (= K41), S105 (= S69), D232 (≠ E204), S236 (= S208), L238 (≠ F211), S300 (= S269), P326 (≠ A295)
- binding protoporphyrin ix containing fe: A177 (≠ P150), P180 (= P153), L181 (vs. gap), Y184 (= Y156), R217 (≠ Q189)
- binding pyridoxal-5'-phosphate: K77 (= K41), N107 (= N71), V206 (= V178), G207 (= G179), T208 (= T180), G209 (= G181), G210 (= G182), T211 (≠ S183), G256 (= G222), S300 (= S269), P326 (≠ A295), 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)
34% identity, 96% coverage: 5:325/336 of query aligns to 9:344/344 of 6c4pA
- binding calcium ion: N179 (vs. gap), D182 (= D169), N183 (≠ G170)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (= K41), N80 (= N71), A191 (≠ V178), G192 (= G179), T193 (= T180), G194 (= G181), T196 (≠ S183), G241 (= G222), S285 (= S269), P314 (≠ A295), D315 (= D296)
6c2zA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-aminoacrylate intermediate (see paper)
34% identity, 96% coverage: 5:325/336 of query aligns to 10:345/345 of 6c2zA
- binding calcium ion: N180 (vs. gap), D183 (= D169), N184 (≠ G170)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K50 (= K41), T78 (≠ S68), S79 (= S69), N81 (= N71), T82 (= T72), Q154 (= Q146), A192 (≠ V178), G193 (= G179), T194 (= T180), G195 (= G181), T197 (≠ S183), G242 (= G222), S286 (= S269), P315 (≠ A295), D316 (= D296)
6c2qA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-l-serine intermediate (see paper)
34% identity, 96% coverage: 5:325/336 of query aligns to 10:345/345 of 6c2qA
- binding calcium ion: N180 (vs. gap), D183 (= D169), N184 (≠ G170)
- binding L-Serine, N-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]: K50 (= K41), T78 (≠ S68), S79 (= S69), N81 (= N71), T82 (= T72), Q154 (= Q146), A192 (≠ V178), G193 (= G179), T194 (= T180), G195 (= G181), T197 (≠ S183), G242 (= G222), Y245 (≠ T225), S286 (= S269), P315 (≠ A295), D316 (= D296)
6c2hA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the catalytic core (see paper)
34% identity, 96% coverage: 5:325/336 of query aligns to 10:345/345 of 6c2hA
- binding calcium ion: N180 (vs. gap), D183 (= D169), N184 (≠ G170)
- binding pyridoxal-5'-phosphate: K50 (= K41), N81 (= N71), A192 (≠ V178), G193 (= G179), T194 (= T180), G195 (= G181), T197 (≠ S183), G242 (= G222), S286 (= S269), P315 (≠ A295), D316 (= D296)
5b1iA Crystal structure of k42a mutant of cystathionine beta-synthase from lactobacillus plantarum in a complex with l-methionine (see paper)
36% identity, 90% coverage: 1:303/336 of query aligns to 1:297/303 of 5b1iA
- active site: A42 (≠ K41), S263 (= S269)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: T69 (≠ S68), A70 (≠ S69), N72 (= N71), T73 (= T72), G176 (= G179), S177 (≠ T180), G178 (= G181), T180 (≠ S183), G219 (= G222), S263 (= S269), P289 (≠ A295), D290 (= D296)
5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
34% identity, 96% coverage: 10:331/336 of query aligns to 39:362/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (= P150), P184 (= P153), Y188 (= Y156), R221 (≠ Q189)
- binding pyridoxal-5'-phosphate: K74 (= K41), N104 (= N71), G209 (≠ C177), G211 (= G179), T212 (= T180), G213 (= G181), G214 (= G182), T215 (≠ S183), G256 (vs. gap), S300 (= S269), P326 (≠ A295), D327 (= D296)
Sites not aligning to the query:
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
34% identity, 96% coverage: 10:331/336 of query aligns to 43:369/504 of Q2V0C9
- K78 (= K41) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N71) binding pyridoxal 5'-phosphate
- GTGGT 215:219 (≠ GTGGS 179:183) 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)
35% identity, 92% coverage: 5:314/336 of query aligns to 11:327/477 of 6xwlC
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
35% identity, 92% coverage: 5:314/336 of query aligns to 11:327/468 of 6xylA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K41), T82 (= T72), Q154 (= Q146), G188 (= G179), T189 (= T180), G190 (= G181), T192 (≠ S183), G238 (= G222), I239 (≠ T223), Y241 (≠ T225), S282 (= S269), P308 (≠ A295), D309 (= D296)
5d85A Staphyloferrin b precursor biosynthetic enzyme sbna bound to aminoacrylate intermediate (see paper)
30% identity, 93% coverage: 3:315/336 of query aligns to 1:310/313 of 5d85A
- active site: K39 (= K41), S264 (= S269)
- binding citrate anion: S67 (= S69), K92 (≠ H94), G119 (≠ D116), Y120 (≠ F117), L121 (≠ R118), R124 (≠ E121), R216 (≠ Q220), A223 (= A227), S224 (≠ G228)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K39 (= K41), T66 (≠ S68), S67 (= S69), N69 (= N71), L70 (≠ T72), Q143 (= Q146), V176 (= V178), S177 (≠ G179), T178 (= T180), T179 (≠ G181), S181 (= S183), G220 (= G224), S264 (= S269), P290 (≠ A295), D291 (= D296)
A6QDA0 N-(2-amino-2-carboxyethyl)-L-glutamate synthase; ACEGA synthase; Staphyloferrin B biosynthesis protein SbnA; EC 2.5.1.140 from Staphylococcus aureus (strain Newman) (see paper)
30% identity, 93% coverage: 3:315/336 of query aligns to 9:318/326 of A6QDA0
- K47 (= K41) modified: N6-(pyridoxal phosphate)lysine
- N77 (= N71) binding pyridoxal 5'-phosphate
- R132 (≠ E121) mutation to A: No detectable enzyme activity. Does not form pyridoxal 5'-phosphate-alpha-aminoacrylate reaction intermediate.
- Y152 (≠ S147) mutation to F: Very low enzyme activity. Does not form pyridoxal 5'-phosphate-alpha-aminoacrylate reaction intermediate; when associated with G-185.
- STTGS 185:189 (≠ GTGGS 179:183) binding pyridoxal 5'-phosphate
- S272 (= S269) binding pyridoxal 5'-phosphate
5d84A Staphyloferrin b precursor biosynthetic enzyme sbna bound to plp (see paper)
30% identity, 93% coverage: 3:315/336 of query aligns to 3:312/318 of 5d84A
- active site: K41 (= K41), S266 (= S269)
- binding pyridoxal-5'-phosphate: K41 (= K41), N71 (= N71), V178 (= V178), S179 (≠ G179), T180 (= T180), T181 (≠ G181), S183 (= S183), G222 (= G224), S266 (= S269), P292 (≠ A295), D293 (= D296)
5d86A Staphyloferrin b precursor biosynthetic enzyme sbna y152f variant (see paper)
30% identity, 93% coverage: 3:315/336 of query aligns to 2:311/318 of 5d86A
- active site: K40 (= K41), S265 (= S269)
- binding magnesium ion: S225 (≠ G228), R226 (≠ E230)
- binding pyridoxal-5'-phosphate: K40 (= K41), N70 (= N71), V177 (= V178), S178 (≠ G179), T179 (= T180), T180 (≠ G181), S182 (= S183), G221 (= G224), S265 (= S269), P291 (≠ A295), D292 (= D296)
6vjuB Crystal structure of cystathionine beta synthase from legionella pneumophila with llp, plp, and homocysteine
34% identity, 94% coverage: 1:317/336 of query aligns to 2:317/317 of 6vjuB
6ahiB Crystal structure of o-acetylserine dependent cystathionine beta- synthase from helicobacter pylori. (see paper)
33% identity, 90% coverage: 1:302/336 of query aligns to 2:300/306 of 6ahiB
Query Sequence
>WP_010875114.1 NCBI__GCF_000018545.1:WP_010875114.1
MLHTTVTQLIGQTPVMSIDVPGRNATLVLKIEKNNPGGSMKDRMARSMVIAALQDGRLPP
GGTIVESSSGNTGTGLALAALEFGLRFIAVVDHHAAPDKIRMMRALGAEIRYVEGDFRED
EVAVVERQRLAAQLGAQLPGALFMNQSDNPANPEGYTGLVDELVAQLPDGIDAFVGCVGT
GGSMTGISQRLKRNNPAVRTIAVEPAGSIVFGKPGHPYYQSGTGTPAGDEVGKVLDYGCI
DEGVQVTDTQAFETARYIARRKGLLVGGSTGGAIYKALEFIGAGKLTGTVVTTVADGGEK
YLGTIFDEEWMAKRRLLDPAIAAQLDGWLFGKARAA
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