SitesBLAST
Comparing Ac3H11_615 FitnessBrowser__acidovorax_3H11:Ac3H11_615 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 15 hits to proteins with known functional sites (download)
Q9A9Z1 D-xylonolactone lactonase; Xylono-1,5-lactonase; EC 3.1.1.110 from Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) (see paper)
39% identity, 92% coverage: 21:312/316 of query aligns to 1:284/289 of Q9A9Z1
- E17 (= E37) binding
- N145 (= N170) binding
- D195 (= D222) binding
7pldB Caulobacter crescentus xylonolactonase with (r)-4-hydroxy-2- pyrrolidone (see paper)
39% identity, 92% coverage: 22:312/316 of query aligns to 2:284/289 of 7pldB
- binding (R)-4-hydroxy-2-pyrrolidone: L15 (= L35), E17 (= E37), I31 (= I53), A64 (= A86), G66 (= G88), F67 (= F89), P80 (= P102), R98 (= R122), N100 (= N124), E119 (≠ C143), D138 (= D163), N145 (= N170), K180 (= K208), D195 (= D222), W210 (= W237), W210 (= W237)
- binding fe (ii) ion: E17 (= E37), N145 (= N170), D195 (= D222)
7plbB Caulobacter crescentus xylonolactonase with d-xylose (see paper)
39% identity, 92% coverage: 22:312/316 of query aligns to 2:284/289 of 7plbB
- binding fe (ii) ion: E17 (= E37), N145 (= N170), D195 (= D222)
- binding beta-D-xylopyranose: L15 (= L35), E17 (= E37), E89 (≠ Q113), V90 (≠ P114), D92 (≠ P116), R98 (= R122), N100 (= N124), R109 (= R133), D130 (= D154), N145 (= N170), D174 (≠ T202), D195 (= D222)
- binding alpha-D-xylopyranose: A64 (= A86), G66 (= G88), F67 (= F89), P80 (= P102)
4gncA Human smp30/gnl-1,5-ag complex (see paper)
33% identity, 88% coverage: 25:302/316 of query aligns to 5:283/298 of 4gncA
- binding 1,5-anhydro-D-glucitol: E17 (= E37), R100 (= R122), N102 (= N124), D203 (= D222), T245 (= T264), N253 (≠ D272), Y254 (≠ L273)
- binding calcium ion: E17 (= E37), D103 (= D125), N153 (= N170), D203 (= D222)
Sites not aligning to the query:
Q15493 Regucalcin; RC; Gluconolactonase; GNL; Senescence marker protein 30; SMP-30; EC 3.1.1.17 from Homo sapiens (Human) (see 2 papers)
33% identity, 88% coverage: 25:302/316 of query aligns to 6:284/299 of Q15493
- E18 (= E37) binding ; mutation to A: Reduces enzyme activity by about 90%.
- N103 (= N124) mutation to A: Reduces enzyme activity by about 95%.
- N154 (= N170) binding ; mutation to A: Reduces enzyme activity by about 95%.
- D204 (= D222) binding ; mutation to A: Reduces enzyme activity by over 98%.
3g4hA Crystal structure of human senescence marker protein-30 (zinc bound) (see paper)
33% identity, 88% coverage: 25:302/316 of query aligns to 4:282/297 of 3g4hA
4gnaA Mouse smp30/gnl-xylitol complex (see paper)
32% identity, 88% coverage: 25:302/316 of query aligns to 4:282/297 of 4gnaA
4gn9A Mouse smp30/gnl-glucose complex (see paper)
32% identity, 88% coverage: 25:302/316 of query aligns to 4:282/297 of 4gn9A
- binding beta-D-glucopyranose: E16 (= E37), G66 (= G88), W80 (≠ A103), E81 (≠ T104), D92 (≠ E115), E93 (≠ P116), R99 (= R122), N101 (= N124), E119 (vs. gap), Y133 (= Y151), K143 (≠ R161), N152 (= N170), S168 (≠ T188), D202 (= D222), Y217 (≠ W237)
- binding calcium ion: E16 (= E37), N152 (= N170), D202 (= D222)
4gn8A Mouse smp30/gnl-1,5-ag complex (see paper)
32% identity, 88% coverage: 25:302/316 of query aligns to 4:282/297 of 4gn8A
- binding 1,5-anhydro-D-glucitol: Q63 (≠ H85), R99 (= R122), N101 (= N124), A108 (≠ Q131), G109 (= G132), E119 (vs. gap), P122 (vs. gap), N152 (= N170), Y164 (≠ F184), A175 (≠ R195), D179 (= D199), Q181 (≠ A201), R189 (≠ T209), V191 (≠ W211), D202 (= D222), Y217 (≠ W237), P227 (= P247)
- binding calcium ion: E16 (= E37), N152 (= N170), D202 (= D222)
Sites not aligning to the query:
4gn7A Mouse smp30/gnl (see paper)
32% identity, 88% coverage: 25:302/316 of query aligns to 4:282/297 of 4gn7A
5gx1A Luciferin-regenerating enzyme collected with serial synchrotron rotational crystallography with accumulated dose of 1.1 mgy (1st measurement) (see paper)
31% identity, 88% coverage: 24:302/316 of query aligns to 3:292/307 of 5gx1A
5d9bA Luciferin-regenerating enzyme solved by siras using xfel (refined against native data) (see paper)
31% identity, 88% coverage: 24:302/316 of query aligns to 3:292/307 of 5d9bA
3o4pA Dfpase at 0.85 angstrom resolution (h atoms included) (see paper)
24% identity, 53% coverage: 115:280/316 of query aligns to 108:286/314 of 3o4pA
- active site: N120 (= N124), N175 (= N170), D229 (= D222)
- binding calcium ion: N120 (= N124), N175 (= N170), D229 (= D222), D232 (≠ T225), L273 (≠ C266), H274 (≠ A267)
- binding 1,2-dimethoxyethane: W244 (= W237), K269 (≠ Q262)
- binding 2-methoxyethanol: K151 (≠ P146), A170 (≠ G165), F171 (= F166), E194 (≠ A187), K214 (= K208)
Sites not aligning to the query:
Q7SIG4 Diisopropyl-fluorophosphatase; DFPase; EC 3.1.8.2 from Loligo vulgaris (Common European squid) (see 4 papers)
24% identity, 53% coverage: 115:280/316 of query aligns to 108:286/314 of Q7SIG4
- N120 (= N124) mutation to D: 96% decrease in activity. 100% decrease in activity; when associated with N-229.
- D121 (= D125) mutation to F: 100% decrease in activity.
- Y144 (≠ F141) mutation to S: 8% increase in activity.
- R146 (vs. gap) mutation to S: 45% decrease in activity.
- M148 (≠ C143) mutation to A: 26% decrease in activity.
- F173 (≠ V168) mutation to A: 84% decrease in activity.; mutation to L: 28% decrease in activity.; mutation to S: 68% decrease in activity.; mutation to V: 46% decrease in activity.; mutation to W: 19% decrease in activity.; mutation to Y: 53% decrease in activity.
- N175 (= N170) mutation to D: 98% decrease in activity.
- H181 (≠ G176) mutation to N: 20% decrease in activity.
- T195 (= T188) mutation to A: 60% decrease in activity.; mutation to L: 11% decrease in activity.; mutation to V: 3% decrease in activity.
- H219 (= H213) mutation to N: 3% increase in activity.
- H224 (≠ E217) mutation to N: 14% increase in activity.
- D229 (= D222) mutation to N: 100% decrease in activity. Loss of calcium 1 binding. 100% decrease in activity; when associated with D-120.
- D232 (≠ T225) binding ; mutation to S: 3% increase in activity. 19% decrease in activity; when associated with A-271.
- N237 (≠ G230) mutation to S: 4% decrease in activity.
- W244 (= W237) mutation to F: 44% decrease in activity.; mutation to H: 27% decrease in activity.; mutation to L: 62% decrease in activity.; mutation to Y: No effect on activity.
- H248 (≠ C241) mutation to N: 4% increase in activity.
- S271 (≠ T264) mutation to A: 30% increase in activity. 19% decrease in activity; when associated with S-232.
- N272 (≠ T265) mutation to F: 100% decrease in activity.
- L273 (≠ C266) binding
- H274 (≠ A267) binding ; mutation to N: 85% decrease in activity.
Sites not aligning to the query:
- 21 E→Q: 100% decrease in activity. Loss of calcium 1 binding.
- 37 E→Q: 50% decrease in activity.
- 77 Q→F: 100% decrease in activity.; Q→W: No effect on activity.; Q→Y: 6% increase in activity.
- 287 active site, Proton acceptor; H→A: 90% decrease in activity.; H→F: 36% decrease in activity.; H→L: 21% decrease in activity.; H→N: 97% decrease in activity.; H→Q: 54% decrease in activity.; H→W: 44% decrease in activity.; H→Y: 57% decrease in activity.
- 304 Q→F: 50% decrease in activity.; Q→W: 3% decrease in activity.
- 314 F→A: 3% increase in activity.
2gvvA Structure of diisopropyl fluorophosphatase (dfpase) in complex with dicyclopentylphosphoroamidate (dcppa) (see paper)
24% identity, 53% coverage: 115:280/316 of query aligns to 106:284/309 of 2gvvA
- active site: N118 (= N124), N173 (= N170), D227 (= D222)
- binding calcium ion: N118 (= N124), N173 (= N170), D227 (= D222), D230 (≠ T225), L271 (≠ C266), H272 (≠ A267)
- binding dicyclopentyl phosphoramidate: N118 (= N124), N173 (= N170), D227 (= D222), W242 (= W237)
Sites not aligning to the query:
Query Sequence
>Ac3H11_615 FitnessBrowser__acidovorax_3H11:Ac3H11_615
MRPFLDTPFSPPEGAAFSAPVTGAVRCVIALGNALGEGVLWSVREQAVYWVDILGRELHR
WDPATGAHQRWTFDEEISAIAERAHAPGFIVTLRRGFALFDPATDMAPRYLHQPEPDRAG
NRFNDGKCDAQGRFWAGSMDFACEAPTGALYRYDSDGSCTRHDDGFAVTNGPTWSGTGQG
AAMFFNATIEGNTYRYDSDLATGTVSNKTLWKHWLPEDGLPDGMTTDAQGRLWIAHWGGW
CVTCHDPVTAAELGRVRLPVSQVTTCAFGGADLRTLFISSARVGLTPEQLAAEPLAGALF
AVDTDSLGLPAHPFGG
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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