SitesBLAST
Comparing WP_013707055.1 NCBI__GCF_000195295.1:WP_013707055.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 6 hits to proteins with known functional sites (download)
F9VMT6 Fructose-1,6-bisphosphate aldolase/phosphatase; FBP A/P; FBP aldolase/phosphatase; Fructose-1,6-bisphosphatase; FBPase; EC 3.1.3.11; EC 4.1.2.13 from Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) (see 2 papers)
60% identity, 98% coverage: 4:363/367 of query aligns to 2:362/384 of F9VMT6
- D11 (= D13) binding ; mutation to A: 930-fold decrease in FBPase catalytic efficiency.
- H18 (= H20) binding in other chain; binding ; binding ; mutation to A: 1.7-fold increase in FBPase catalytic activity and 5-fold decrease in FBP affinity, leading to a 2.7-fold decrease in FBPase catalytic efficiency.
- D52 (= D54) binding ; binding ; mutation to A: 175-fold decrease in FBPase catalytic efficiency.
- D53 (= D55) binding ; mutation to A: 1000-fold decrease in FBPase catalytic activity.
- Y90 (= Y92) binding in other chain
- Q94 (= Q96) binding ; mutation to A: 1.3-fold increase in FBPase catalytic efficiency.
- GN 103:104 (= GN 105:106) binding in other chain
- D131 (= D133) binding ; mutation to A: 2-fold increase in FBP affinity and 10-fold decrease in FBPase catalytic activity, leading to a 5.5-fold decrease in FBPase catalytic efficiency.
- K132 (= K134) binding in other chain; binding
- Y228 (= Y229) mutation to F: Retains the FBPase activity, but loses the FBP aldolase activity.
- K231 (= K232) active site, Schiff-base intermediate with DHAP; for FBP aldolase activity; binding
- D232 (= D233) binding ; binding ; mutation to A: 275-fold decrease in FBPase catalytic activity.
- D233 (= D234) binding ; binding ; mutation to A: 2000-fold decrease in FBPase catalytic activity.
- QH 241:242 (≠ QG 242:243) binding
- R265 (= R266) binding in other chain; binding
- D286 (= D287) binding in other chain; binding
- Y347 (= Y348) binding in other chain
1umgA Crystal structure of fructose-1,6-bisphosphatase (see paper)
59% identity, 98% coverage: 4:363/367 of query aligns to 1:358/359 of 1umgA
- binding 1,6-fructose diphosphate (linear form): H17 (= H20), D51 (= D54), Y89 (= Y92), Q93 (= Q96), S101 (= S104), G102 (= G105), N103 (= N106), K131 (= K134), D228 (= D233), D229 (= D234), M260 (= M265), R261 (= R266), D282 (= D287), Y343 (= Y348)
- binding magnesium ion: D10 (= D13), H17 (= H20), D51 (= D54), D51 (= D54), D52 (= D55), Q93 (= Q96), D130 (= D133), D228 (= D233), D229 (= D234), D229 (= D234)
B1YAL1 Fructose-1,6-bisphosphate aldolase/phosphatase; FBP A/P; FBP aldolase/phosphatase; EC 3.1.3.11; EC 4.1.2.13 from Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta) (Thermoproteus neutrophilus) (see paper)
57% identity, 97% coverage: 4:359/367 of query aligns to 2:369/399 of B1YAL1
- D11 (= D13) binding
- H18 (= H20) binding in other chain; binding ; binding
- D52 (= D54) binding ; binding
- D53 (= D55) binding
- Y91 (= Y92) binding in other chain
- Q95 (= Q96) binding
- GN 104:105 (= GN 105:106) binding in other chain
- D132 (= D133) binding
- K133 (= K134) binding in other chain; binding
- Y229 (= Y229) mutation to F: Shows unaltered FBP phosphatase activity, whereas FBP aldolase activity is completely abolished.
- K232 (= K232) active site, Schiff-base intermediate with DHAP; for FBP aldolase activity
- D233 (= D233) binding ; binding
- D234 (= D234) binding ; binding
- QS 242:243 (≠ QG 242:243) binding
- R266 (= R266) binding in other chain; binding
- D297 (= D287) binding in other chain; binding ; mutation to N: 18-fold decrease in FBP phosphatase activity, whereas FBP aldolase activity is completely abolished.
- Y358 (= Y348) binding in other chain
3t2dA Fructose-1,6-bisphosphate aldolase/phosphatase from thermoproteus neutrophilus, fbp-bound form (see paper)
57% identity, 97% coverage: 4:359/367 of query aligns to 2:369/390 of 3t2dA
- binding magnesium ion: D11 (= D13), H18 (= H20), D52 (= D54), D52 (= D54), D53 (= D55), Q95 (= Q96), D132 (= D133), D233 (= D233), D234 (= D234), D234 (= D234)
- binding 1,6-di-O-phosphono-D-fructose: H18 (= H20), D52 (= D54), Y91 (= Y92), Q95 (= Q96), S103 (= S104), G104 (= G105), N105 (= N106), K133 (= K134), D233 (= D233), D234 (= D234), M265 (= M265), R266 (= R266), D297 (= D287), Y358 (= Y348)
3t2eA Fructose-1,6-bisphosphate aldolase/phosphatase from thermoproteus neutrophilus, f6p-bound form (see paper)
57% identity, 97% coverage: 4:359/367 of query aligns to 2:365/385 of 3t2eA
- binding fructose -6-phosphate: H18 (= H20), Y91 (= Y92), M261 (= M265), R262 (= R266), D293 (= D287), Y354 (= Y348)
- binding magnesium ion: D11 (= D13), H18 (= H20), D52 (= D54), D52 (= D54), D53 (= D55), Q95 (= Q96), D132 (= D133), D230 (= D234)
A0RV30 Fructose-1,6-bisphosphate aldolase/phosphatase; FBP A/P; FBP aldolase/phosphatase; EC 3.1.3.11; EC 4.1.2.13 from Cenarchaeum symbiosum (strain A) (see 2 papers)
43% identity, 99% coverage: 4:367/367 of query aligns to 2:362/376 of A0RV30
- Y224 (= Y229) mutation to F: Shows slightly decreased FBP phosphatase activity, whereas FBP aldolase activity is nearly completely abolished.
- K227 (= K232) active site, Schiff-base intermediate with DHAP; for FBP aldolase activity; mutation to R: Shows enhanced FBP phosphatase activity, whereas FBP aldolase activity is completely abolished.
- D228 (= D233) mutation to N: Shows completely abolition of both FBP aldolase and FBP phosphatase activities.
- E341 (= E347) mutation to Q: Shows unaltered FBP aldolase activity, whereas FBP phosphatase activity is completely abolished.
- Y342 (= Y348) mutation to F: Shows unaltered FBP aldolase activity, whereas FBP phosphatase activity is completely abolished.
Query Sequence
>WP_013707055.1 NCBI__GCF_000195295.1:WP_013707055.1
MADKITLSVIKADVGGYVGHCAMHGELILEASRHLDDARSQGVLVDYHVTACGDDLELIM
THSHGVDNRDVHHLAWEVFEACTEVAKKLKLYGAGQDLLSHAFSGNVRGMGPGVAEMEFV
ERESEPIVIFMADKTSAGAWNLPLYKIFADPFNTAGLVIAPTLHAGFRYEVHDVKGHQKI
LFSTPEELYDLLVFIGATGRYLVKAVYTKDGEIAAVSSTERLALIAGKYVGKDDPVCVVR
CQGKFPAVGEVVEPFSMPHIVEGWMRGSHYGPLMPVPLSQARPTRFDGPPRVICLGFQLA
NGHLVGPCDIFDDPSFNEARRLCNVIADHLRRHGPFEPHRLPMDEMEYTTLPQVMAKLQD
RWQPLEN
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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