SitesBLAST
Comparing WP_091375961.1 NCBI__GCF_900105165.1:WP_091375961.1 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)
Q15493 Regucalcin; RC; Gluconolactonase; GNL; Senescence marker protein 30; SMP-30; EC 3.1.1.17 from Homo sapiens (Human) (see 2 papers)
31% identity, 94% coverage: 6:282/295 of query aligns to 4:284/299 of Q15493
- E18 (= E20) binding a divalent metal cation; mutation to A: Reduces enzyme activity by about 90%.
- N103 (= N106) mutation to A: Reduces enzyme activity by about 95%.
- N154 (= N152) binding a divalent metal cation; mutation to A: Reduces enzyme activity by about 95%.
- D204 (= D202) binding a divalent metal cation; mutation to A: Reduces enzyme activity by over 98%.
4gncA Human smp30/gnl-1,5-ag complex (see paper)
31% identity, 94% coverage: 6:282/295 of query aligns to 3:283/298 of 4gncA
- binding 1,5-anhydro-D-glucitol: E17 (= E20), R100 (= R104), N102 (= N106), D203 (= D202), T245 (≠ S244), N253 (= N252), Y254 (≠ L253)
- binding calcium ion: E17 (= E20), D103 (= D107), N153 (= N152), D203 (= D202)
Sites not aligning to the query:
3g4hA Crystal structure of human senescence marker protein-30 (zinc bound) (see paper)
31% identity, 94% coverage: 6:282/295 of query aligns to 2:282/297 of 3g4hA
7pldB Caulobacter crescentus xylonolactonase with (r)-4-hydroxy-2- pyrrolidone (see paper)
35% identity, 96% coverage: 11:292/295 of query aligns to 8:284/289 of 7pldB
- binding (R)-4-hydroxy-2-pyrrolidone: L15 (= L18), E17 (= E20), I31 (= I36), A64 (≠ G69), G66 (vs. gap), F67 (≠ V71), P80 (≠ L84), R98 (= R104), N100 (= N106), E119 (≠ G125), D138 (≠ V145), N145 (= N152), K180 (= K188), D195 (= D202), W210 (= W217), W210 (= W217)
- binding fe (ii) ion: E17 (= E20), N145 (= N152), D195 (= D202)
7plbB Caulobacter crescentus xylonolactonase with d-xylose (see paper)
35% identity, 96% coverage: 11:292/295 of query aligns to 8:284/289 of 7plbB
- binding fe (ii) ion: E17 (= E20), N145 (= N152), D195 (= D202)
- binding beta-D-xylopyranose: L15 (= L18), E17 (= E20), E89 (≠ I93), V90 (≠ D94), D92 (= D96), R98 (= R104), N100 (= N106), R109 (= R115), D130 (≠ S136), N145 (= N152), D174 (≠ T182), D195 (= D202)
- binding alpha-D-xylopyranose: A64 (≠ G69), G66 (vs. gap), F67 (≠ V71), P80 (≠ L84)
Q9A9Z1 D-xylonolactone lactonase; Xylono-1,5-lactonase; EC 3.1.1.110 from Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus) (see paper)
35% identity, 96% coverage: 11:292/295 of query aligns to 8:284/289 of Q9A9Z1
- E17 (= E20) binding Fe(2+)
- N145 (= N152) binding Fe(2+)
- D195 (= D202) binding Fe(2+)
4gnaA Mouse smp30/gnl-xylitol complex (see paper)
31% identity, 94% coverage: 6:282/295 of query aligns to 2:282/297 of 4gnaA
4gn9A Mouse smp30/gnl-glucose complex (see paper)
31% identity, 94% coverage: 6:282/295 of query aligns to 2:282/297 of 4gn9A
- binding beta-D-glucopyranose: E16 (= E20), G66 (≠ D77), W80 (≠ Y91), E81 (≠ K92), D92 (vs. gap), E93 (vs. gap), R99 (= R104), N101 (= N106), E119 (≠ S124), Y133 (= Y133), K143 (≠ E143), N152 (= N152), S168 (≠ T168), D202 (= D202), Y217 (≠ W217)
- binding calcium ion: E16 (= E20), N152 (= N152), D202 (= D202)
4gn8A Mouse smp30/gnl-1,5-ag complex (see paper)
31% identity, 94% coverage: 6:282/295 of query aligns to 2:282/297 of 4gn8A
- binding 1,5-anhydro-D-glucitol: Q63 (≠ A74), R99 (= R104), N101 (= N106), A108 (≠ E113), G109 (= G114), E119 (≠ S124), P122 (≠ R127), N152 (= N152), Y164 (= Y164), A175 (≠ Q175), D179 (= D179), Q181 (= Q181), R189 (≠ K189), V191 (≠ I191), D202 (= D202), Y217 (≠ W217), P227 (= P227)
- binding calcium ion: E16 (= E20), N152 (= N152), D202 (= D202)
Sites not aligning to the query:
4gn7A Mouse smp30/gnl (see paper)
31% identity, 94% coverage: 6:282/295 of query aligns to 2:282/297 of 4gn7A
5gx1A Luciferin-regenerating enzyme collected with serial synchrotron rotational crystallography with accumulated dose of 1.1 mgy (1st measurement) (see paper)
32% identity, 91% coverage: 14:282/295 of query aligns to 11:292/307 of 5gx1A
5d9bA Luciferin-regenerating enzyme solved by siras using xfel (refined against native data) (see paper)
32% identity, 91% coverage: 14:282/295 of query aligns to 11:292/307 of 5d9bA
3dr2A Structural and functional analyses of xc5397 from xanthomonas campestris: a gluconolactonase important in glucose secondary metabolic pathways (see paper)
25% identity, 79% coverage: 15:248/295 of query aligns to 40:278/299 of 3dr2A
3o4pA Dfpase at 0.85 angstrom resolution (h atoms included) (see paper)
27% identity, 64% coverage: 70:259/295 of query aligns to 84:285/314 of 3o4pA
- active site: N120 (= N106), N175 (= N152), D229 (= D202)
- binding calcium ion: N120 (= N106), N175 (= N152), D229 (= D202), D232 (≠ T205), L273 (≠ C246), H274 (≠ A247)
- binding 1,2-dimethoxyethane: W244 (= W217), K269 (= K242)
- binding 2-methoxyethanol: K151 (≠ E128), A170 (≠ G147), F171 (≠ V148), E194 (≠ D167), K214 (= K188)
Sites not aligning to the query:
Q7SIG4 Diisopropyl-fluorophosphatase; DFPase; EC 3.8.2.2 from Loligo vulgaris (Common European squid) (see 4 papers)
27% identity, 64% coverage: 70:259/295 of query aligns to 84:285/314 of Q7SIG4
- N120 (= N106) mutation to D: 96% decrease in activity. 100% decrease in activity; when associated with N-229.
- D121 (= D107) mutation to F: 100% decrease in activity.
- Y144 (≠ H121) mutation to S: 8% increase in activity.
- R146 (≠ M123) mutation to S: 45% decrease in activity.
- M148 (≠ G125) mutation to A: 26% decrease in activity.
- F173 (≠ I150) 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 (= N152) mutation to D: 98% decrease in activity.
- H181 (vs. gap) mutation to N: 20% decrease in activity.
- T195 (= T168) mutation to A: 60% decrease in activity.; mutation to L: 11% decrease in activity.; mutation to V: 3% decrease in activity.
- H219 (≠ T193) mutation to N: 3% increase in activity.
- H224 (≠ E197) mutation to N: 14% increase in activity.
- D229 (= D202) mutation to N: 100% decrease in activity. Loss of calcium 1 binding. 100% decrease in activity; when associated with D-120.
- D232 (≠ T205) binding Ca(2+); mutation to S: 3% increase in activity. 19% decrease in activity; when associated with A-271.
- N237 (≠ G210) mutation to S: 4% decrease in activity.
- W244 (= W217) 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 (≠ C221) mutation to N: 4% increase in activity.
- S271 (= S244) mutation to A: 30% increase in activity. 19% decrease in activity; when associated with S-232.
- N272 (≠ S245) mutation to F: 100% decrease in activity.
- L273 (≠ C246) binding Ca(2+)
- H274 (≠ A247) binding Ca(2+); 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)
27% identity, 64% coverage: 70:259/295 of query aligns to 82:283/309 of 2gvvA
- active site: N118 (= N106), N173 (= N152), D227 (= D202)
- binding calcium ion: N118 (= N106), N173 (= N152), D227 (= D202), D230 (≠ T205), L271 (≠ C246), H272 (≠ A247)
- binding dicyclopentyl phosphoramidate: N118 (= N106), N173 (= N152), D227 (= D202), W242 (= W217)
Sites not aligning to the query:
8dk0A Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound (s)gamma- valerolactone (see paper)
26% identity, 55% coverage: 103:265/295 of query aligns to 112:276/293 of 8dk0A