SitesBLAST
Comparing CCNA_01282 FitnessBrowser__Caulo:CCNA_01282 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 17 hits to proteins with known functional sites (download)
3dr2A Structural and functional analyses of xc5397 from xanthomonas campestris: a gluconolactonase important in glucose secondary metabolic pathways (see paper)
34% identity, 81% coverage: 50:330/347 of query aligns to 31:288/299 of 3dr2A
3e5zA X-ray structure of the putative gluconolactonase in protein family pf08450. Northeast structural genomics consortium target drr130.
31% identity, 89% coverage: 36:345/347 of query aligns to 2:288/290 of 3e5zA
7risA Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound phosphate (see paper)
25% identity, 80% coverage: 53:330/347 of query aligns to 1:269/293 of 7risA
8dk0A Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound (s)gamma- valerolactone (see paper)
25% identity, 80% coverage: 53:330/347 of query aligns to 3:269/293 of 8dk0A
8djzA Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound product (see paper)
25% identity, 80% coverage: 53:330/347 of query aligns to 3:269/293 of 8djzA
8djfA Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound tetrahedral intermediate (see paper)
25% identity, 80% coverage: 53:330/347 of query aligns to 3:269/293 of 8djfA
7rizA Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound 2-hydroxyquinoline (see paper)
24% identity, 80% coverage: 53:330/347 of query aligns to 1:282/306 of 7rizA
7pldB Caulobacter crescentus xylonolactonase with (r)-4-hydroxy-2- pyrrolidone (see paper)
27% identity, 78% coverage: 61:331/347 of query aligns to 14:252/289 of 7pldB
- binding (R)-4-hydroxy-2-pyrrolidone: L15 (≠ W62), E17 (= E64), I31 (≠ V80), A64 (≠ T123), G66 (= G125), F67 (≠ E126), P80 (≠ L142), R98 (≠ S161), N100 (= N163), E119 (≠ K195), D138 (= D215), N145 (= N222), K180 (≠ S259), D195 (= D278), W210 (vs. gap), W210 (vs. gap)
- binding fe (ii) ion: E17 (= E64), N145 (= N222), D195 (= D278)
7plbB Caulobacter crescentus xylonolactonase with d-xylose (see paper)
27% identity, 78% coverage: 61:331/347 of query aligns to 14:252/289 of 7plbB
- binding fe (ii) ion: E17 (= E64), N145 (= N222), D195 (= D278)
- binding beta-D-xylopyranose: L15 (≠ W62), E17 (= E64), E89 (≠ A151), V90 (≠ T152), D92 (≠ N155), R98 (≠ S161), N100 (= N163), R109 (≠ S176), D130 (≠ R206), N145 (= N222), D174 (= D253), D195 (= D278)
- binding alpha-D-xylopyranose: A64 (≠ T123), G66 (= G125), F67 (≠ E126), P80 (≠ L142)
Q9A9Z1 D-xylonolactone lactonase; Xylono-1,5-lactonase; EC 3.1.1.110 from Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) (see paper)
27% identity, 78% coverage: 61:331/347 of query aligns to 14:252/289 of Q9A9Z1
- E17 (= E64) binding
- N145 (= N222) binding
- D195 (= D278) binding
4gnaA Mouse smp30/gnl-xylitol complex (see paper)
24% identity, 77% coverage: 64:330/347 of query aligns to 16:259/297 of 4gnaA
4gn9A Mouse smp30/gnl-glucose complex (see paper)
24% identity, 77% coverage: 64:330/347 of query aligns to 16:259/297 of 4gn9A
- binding beta-D-glucopyranose: E16 (= E64), G66 (≠ T116), W80 (≠ L142), E81 (≠ S143), D92 (≠ F154), E93 (≠ N155), R99 (≠ S161), N101 (= N163), E119 (≠ D190), Y133 (= Y203), K143 (≠ L213), N152 (= N222), S168 (= S238), D202 (= D278), Y217 (vs. gap)
- binding calcium ion: E16 (= E64), N152 (= N222), D202 (= D278)
4gn8A Mouse smp30/gnl-1,5-ag complex (see paper)
24% identity, 77% coverage: 64:330/347 of query aligns to 16:259/297 of 4gn8A
- binding 1,5-anhydro-D-glucitol: Q63 (≠ E113), R99 (≠ S161), N101 (= N163), A108 (≠ G175), G109 (≠ S176), E119 (≠ D190), P122 (= P193), N152 (= N222), Y164 (= Y234), A175 (≠ I245), D179 (= D249), Q181 (≠ G251), R189 (≠ S259), V191 (= V261), D202 (= D278), Y217 (vs. gap), P227 (= P301)
- binding calcium ion: E16 (= E64), N152 (= N222), D202 (= D278)
Sites not aligning to the query:
4gn7A Mouse smp30/gnl (see paper)
24% identity, 77% coverage: 64:330/347 of query aligns to 16:259/297 of 4gn7A
3o4pA Dfpase at 0.85 angstrom resolution (h atoms included) (see paper)
23% identity, 80% coverage: 55:333/347 of query aligns to 12:288/314 of 3o4pA
- active site: E21 (= E64), E37 (≠ D79), N120 (= N163), N175 (= N222), D229 (= D278), H287 (≠ N332)
- binding calcium ion: E21 (= E64), N120 (= N163), N175 (= N222), D229 (= D278), D232 (≠ K281), L273 (≠ C318), H274 (≠ V319)
- binding 1,2-dimethoxyethane: W244 (vs. gap), K269 (≠ A315)
- binding 2-methoxyethanol: K151 (≠ A198), A170 (≠ S217), F171 (≠ L218), E194 (≠ D239), K214 (≠ S259)
Sites not aligning to the query:
2gvvA Structure of diisopropyl fluorophosphatase (dfpase) in complex with dicyclopentylphosphoroamidate (dcppa) (see paper)
23% identity, 80% coverage: 55:333/347 of query aligns to 10:286/309 of 2gvvA
- active site: E19 (= E64), E35 (≠ D79), N118 (= N163), N173 (= N222), D227 (= D278), H285 (≠ N332)
- binding calcium ion: E19 (= E64), N118 (= N163), N173 (= N222), D227 (= D278), D230 (≠ K281), L271 (≠ C318), H272 (≠ V319)
- binding dicyclopentyl phosphoramidate: E19 (= E64), P34 (≠ S78), N118 (= N163), N173 (= N222), D227 (= D278), W242 (vs. gap)
Q7SIG4 Diisopropyl-fluorophosphatase; DFPase; EC 3.1.8.2 from Loligo vulgaris (Common European squid) (see 4 papers)
23% identity, 80% coverage: 55:333/347 of query aligns to 12:288/314 of Q7SIG4
- E21 (= E64) mutation to Q: 100% decrease in activity. Loss of calcium 1 binding.
- E37 (≠ D79) mutation to Q: 50% decrease in activity.
- Q77 (≠ N117) mutation to F: 100% decrease in activity.; mutation to W: No effect on activity.; mutation to Y: 6% increase in activity.
- N120 (= N163) mutation to D: 96% decrease in activity. 100% decrease in activity; when associated with N-229.
- D121 (= D164) mutation to F: 100% decrease in activity.
- Y144 (≠ A191) mutation to S: 8% increase in activity.
- R146 (≠ P193) mutation to S: 45% decrease in activity.
- M148 (≠ K195) mutation to A: 26% decrease in activity.
- F173 (= F220) 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 (= N222) mutation to D: 98% decrease in activity.
- H181 (≠ P228) mutation to N: 20% decrease in activity.
- T195 (≠ P240) mutation to A: 60% decrease in activity.; mutation to L: 11% decrease in activity.; mutation to V: 3% decrease in activity.
- H219 (≠ D264) mutation to N: 3% increase in activity.
- H224 (≠ L269) mutation to N: 14% increase in activity.
- D229 (= D278) mutation to N: 100% decrease in activity. Loss of calcium 1 binding. 100% decrease in activity; when associated with D-120.
- D232 (≠ K281) binding ; mutation to S: 3% increase in activity. 19% decrease in activity; when associated with A-271.
- N237 (≠ G286) mutation to S: 4% decrease in activity.
- W244 (vs. gap) 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 (≠ C295) mutation to N: 4% increase in activity.
- S271 (≠ A316) mutation to A: 30% increase in activity. 19% decrease in activity; when associated with S-232.
- N272 (= N317) mutation to F: 100% decrease in activity.
- L273 (≠ C318) binding
- H274 (≠ V319) binding ; mutation to N: 85% decrease in activity.
- H287 (≠ N332) active site, Proton acceptor; mutation to A: 90% decrease in activity.; mutation to F: 36% decrease in activity.; mutation to L: 21% decrease in activity.; mutation to N: 97% decrease in activity.; mutation to Q: 54% decrease in activity.; mutation to W: 44% decrease in activity.; mutation to Y: 57% decrease in activity.
Sites not aligning to the query:
- 304 Q→F: 50% decrease in activity.; Q→W: 3% decrease in activity.
- 314 F→A: 3% increase in activity.
Query Sequence
>CCNA_01282 FitnessBrowser__Caulo:CCNA_01282
MTTRRAMLGAGVALIAGAQGFAAQARGAGSPKIGRIRRLSPELDAVVDANAPIEQLTDGI
TWAEGPAWVANGSYLLFSDVPGNVMHRWDAKGGKTDFLRPSGYDGPPTKIFREAGTNGAI
ISTAGELLVCDCGNRAVARIDLSTRKKTLLATTFNGKKFNSPNDLVEVRHGPLKGSLYFT
DPPYGLEGGDASPAKEQAFNGVYLLRPNGEVALVDGSLSFPNGVGLSPDGRRLYVAISDP
KRPVIMAYDLGADGLPTASRVFFDASDLLKAGGPGLPDGMKVDAQGRLFASGPGCIMILT
PDAKLLGVIETGFPAANCVFGEDGGTLFITSNHLVARVRTKTKGLGR
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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