SitesBLAST
Comparing Ac3H11_138 Gluconolactonase 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)
8dk0A Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound (s)gamma- valerolactone (see paper)
31% identity, 85% coverage: 42:302/307 of query aligns to 11:289/293 of 8dk0A
8djzA Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound product (see paper)
31% identity, 85% coverage: 42:302/307 of query aligns to 11:289/293 of 8djzA
8djfA Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound tetrahedral intermediate (see paper)
31% identity, 85% coverage: 42:302/307 of query aligns to 11:289/293 of 8djfA
7risA Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound phosphate (see paper)
31% identity, 85% coverage: 42:302/307 of query aligns to 9:289/293 of 7risA
2dsoC Crystal structure of d138n mutant of drp35, a 35kda drug responsive protein from staphylococcus aureus (see paper)
29% identity, 74% coverage: 30:255/307 of query aligns to 34:263/323 of 2dsoC
- binding calcium ion: E45 (= E45), S107 (≠ A110), T108 (= T111), G109 (= G112), D127 (vs. gap), T130 (vs. gap), A131 (vs. gap), Y132 (vs. gap), N135 (= N130), N182 (= N177), D233 (= D225), S234 (≠ G226)
7rizA Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound 2-hydroxyquinoline (see paper)
29% identity, 85% coverage: 42:302/307 of query aligns to 9:302/306 of 7rizA
Q99QV3 Lactonase drp35; EC 3.1.1.- from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see paper)
29% identity, 74% coverage: 30:255/307 of query aligns to 36:265/324 of Q99QV3
- E47 (= E45) mutation to A: Loss of activity.; mutation to Q: Loss of activity due to inability to bind calcium ion.; mutation to S: Loss of activity.
- F63 (≠ P61) mutation to A: 2.5-fold increase in lactonase activity.
- K92 (= K88) mutation to A: Increase in lactonase activity.
- D137 (≠ N130) mutation to A: Loss of activity.; mutation to N: Loss of activity but still able to bind calcium ion.; mutation to S: Loss of activity.
- D138 (= D131) mutation to A: Decrease in lactonase activity.
- D151 (= D144) mutation to A: Decrease in lactonase activity.
- N184 (= N177) mutation to A: Loss of activity.; mutation to D: Decrease in lactonase activity.; mutation to S: Loss of activity.
- G185 (= G178) mutation to A: Decrease in lactonase activity.
- D235 (= D225) mutation to A: Loss of activity.; mutation to N: Loss of activity due to inability to bind calcium ion.; mutation to S: Loss of activity.
- S236 (≠ G226) mutation to A: Decrease in lactonase activity.
- C237 (≠ L227) mutation to A: Increase in lactonase activity.
Sites not aligning to the query:
- 280 R→A: Increase in lactonase activity.
- 301 E→A: Increase in lactonase activity.
2gvvA Structure of diisopropyl fluorophosphatase (dfpase) in complex with dicyclopentylphosphoroamidate (dcppa) (see paper)
30% identity, 85% coverage: 45:306/307 of query aligns to 19:307/309 of 2gvvA
- active site: E19 (= E45), E35 (vs. gap), N118 (= N130), N173 (= N177), D227 (= D225), H285 (≠ S284)
- binding calcium ion: E19 (= E45), N118 (= N130), N173 (= N177), D227 (= D225), D230 (≠ A228), L271 (= L269), H272 (≠ A270)
- binding dicyclopentyl phosphoramidate: E19 (= E45), P34 (vs. gap), N118 (= N130), N173 (= N177), D227 (= D225), W242 (≠ P240)
3o4pA Dfpase at 0.85 angstrom resolution (h atoms included) (see paper)
30% identity, 85% coverage: 45:306/307 of query aligns to 21:309/314 of 3o4pA
- active site: E21 (= E45), E37 (vs. gap), N120 (= N130), N175 (= N177), D229 (= D225), H287 (≠ S284)
- binding calcium ion: E21 (= E45), N120 (= N130), N175 (= N177), D229 (= D225), D232 (≠ A228), L273 (= L269), H274 (≠ A270)
- binding 1,2-dimethoxyethane: W244 (≠ P240), K269 (≠ S265), E296 (≠ R293), W297 (≠ L294)
- binding 2-methoxyethanol: K151 (≠ P153), A170 (≠ N172), F171 (≠ V173), E194 (≠ A192), K214 (≠ A210)
Sites not aligning to the query:
Q7SIG4 Diisopropyl-fluorophosphatase; DFPase; EC 3.1.8.2 from Loligo vulgaris (Common European squid) (see 4 papers)
30% identity, 85% coverage: 45:306/307 of query aligns to 21:309/314 of Q7SIG4
- E21 (= E45) mutation to Q: 100% decrease in activity. Loss of calcium 1 binding.
- E37 (vs. gap) mutation to Q: 50% decrease in activity.
- Q77 (≠ K88) mutation to F: 100% decrease in activity.; mutation to W: No effect on activity.; mutation to Y: 6% increase in activity.
- N120 (= N130) mutation to D: 96% decrease in activity. 100% decrease in activity; when associated with N-229.
- D121 (= D131) mutation to F: 100% decrease in activity.
- Y144 (≠ Q145) mutation to S: 8% increase in activity.
- R146 (≠ Q147) mutation to S: 45% decrease in activity.
- M148 (≠ L150) mutation to A: 26% decrease in activity.
- F173 (≠ S175) 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 (= N177) mutation to D: 98% decrease in activity.
- H181 (≠ P183) mutation to N: 20% decrease in activity.
- T195 (= T193) mutation to A: 60% decrease in activity.; mutation to L: 11% decrease in activity.; mutation to V: 3% decrease in activity.
- H219 (≠ F215) mutation to N: 3% increase in activity.
- H224 (≠ G220) mutation to N: 14% increase in activity.
- D229 (= D225) mutation to N: 100% decrease in activity. Loss of calcium 1 binding. 100% decrease in activity; when associated with D-120.
- D232 (≠ A228) binding ; mutation to S: 3% increase in activity. 19% decrease in activity; when associated with A-271.
- N237 (≠ G233) mutation to S: 4% decrease in activity.
- W244 (≠ P240) 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 (≠ Y244) mutation to N: 4% increase in activity.
- S271 (≠ T267) mutation to A: 30% increase in activity. 19% decrease in activity; when associated with S-232.
- N272 (= N268) mutation to F: 100% decrease in activity.
- L273 (= L269) binding
- H274 (≠ A270) binding ; mutation to N: 85% decrease in activity.
- H287 (≠ S284) 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.
- Q304 (≠ L301) mutation to F: 50% decrease in activity.; mutation to W: 3% decrease in activity.
Sites not aligning to the query:
- 314 F→A: 3% increase in activity.
7zp7A Crystal structure of evolved photoenzyme ent1.3 (truncated) with bound product (see paper)
27% identity, 85% coverage: 46:305/307 of query aligns to 20:306/306 of 7zp7A
- binding (1~{R},10~{R},12~{S})-15-oxa-8-azatetracyclo[8.5.0.0^{1,12}.0^{2,7}]pentadeca-2(7),3,5-trien-9-one: Y35 (vs. gap), Y119 (≠ D131), F171 (≠ S175), Q193 (≠ T193), S227 (≠ D225), W242 (≠ P240), H285 (≠ S284)
3e5zA X-ray structure of the putative gluconolactonase in protein family pf08450. Northeast structural genomics consortium target drr130.
28% identity, 80% coverage: 42:286/307 of query aligns to 27:277/290 of 3e5zA
7pldB Caulobacter crescentus xylonolactonase with (r)-4-hydroxy-2- pyrrolidone (see paper)
26% identity, 79% coverage: 45:287/307 of query aligns to 17:256/289 of 7pldB
- binding (R)-4-hydroxy-2-pyrrolidone: E17 (= E45), I31 (= I60), A64 (≠ G93), G66 (≠ L95), F67 (≠ L96), P80 (≠ I109), R98 (≠ G128), N100 (= N130), E119 (≠ L150), D138 (≠ L170), N145 (= N177), K180 (≠ V212), D195 (= D225), W210 (≠ P240), W210 (≠ P240)
- binding fe (ii) ion: E17 (= E45), N145 (= N177), D195 (= D225)
Sites not aligning to the query:
7plbB Caulobacter crescentus xylonolactonase with d-xylose (see paper)
26% identity, 79% coverage: 45:287/307 of query aligns to 17:256/289 of 7plbB
- binding fe (ii) ion: E17 (= E45), N145 (= N177), D195 (= D225)
- binding beta-D-xylopyranose: E17 (= E45), E89 (= E119), V90 (≠ R120), D92 (≠ N122), R98 (≠ G128), N100 (= N130), R109 (≠ N139), D130 (≠ R161), N145 (= N177), D174 (= D206), D195 (= D225)
- binding alpha-D-xylopyranose: A64 (≠ G93), G66 (≠ L95), F67 (≠ L96), P80 (≠ I109)
Sites not aligning to the query:
Q9A9Z1 D-xylonolactone lactonase; Xylono-1,5-lactonase; EC 3.1.1.110 from Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) (see paper)
26% identity, 79% coverage: 45:287/307 of query aligns to 17:256/289 of Q9A9Z1
- E17 (= E45) binding
- N145 (= N177) binding
- D195 (= D225) binding
3dr2A Structural and functional analyses of xc5397 from xanthomonas campestris: a gluconolactonase important in glucose secondary metabolic pathways (see paper)
27% identity, 79% coverage: 42:282/307 of query aligns to 42:288/299 of 3dr2A
6rekA Crystal structure of pizza6-sh with cu2+ (see paper)
29% identity, 82% coverage: 45:296/307 of query aligns to 16:251/251 of 6rekA
6rejA Crystal structure of pizza6-sh with zn2+ (see paper)
29% identity, 82% coverage: 45:296/307 of query aligns to 15:250/250 of 6rejA
P9WI79 Serine/threonine-protein kinase PknD; EC 2.7.11.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
27% identity, 80% coverage: 45:290/307 of query aligns to 429:660/664 of P9WI79
Sites not aligning to the query:
- 79 H→A: Lack of activity.
- 81 Y→A: Decreases activity and alters substrate specificity.
- 135 modified: Phosphothreonine; by autocatalysis
- 138 D→N: 2600-fold decrease in activity.
- 169 modified: Phosphothreonine; by autocatalysis
- 171 modified: Phosphothreonine; by autocatalysis
- 173 modified: Phosphothreonine; by autocatalysis
- 209 modified: Phosphothreonine; by autocatalysis
7ov7A The hybrid cage formed between pizza6-s and cu(ii)-substituted trilacunary keggin
29% identity, 64% coverage: 45:241/307 of query aligns to 58:242/250 of 7ov7A
Sites not aligning to the query:
Query Sequence
>Ac3H11_138 Gluconolactonase
MFLLQSPELRELAFFSSMPDTFRRPERSAWADANRGGTVTDSFLEGPVFDGVGNLYVTDI
PWGRIFRIDPQGAWTLVAEYDGEPNGMKFMDAGTLLITDYKNGLMRLDIATGGVTPYLER
RNSERFKGVNDLIFDADGNLYFTDQGQSGLHDPSGRLYRLRPNGQLDLLLANVPSPNGVA
LSPDGRVLYLAATRGNCVWRVPLLPDGSVAKVGQFFTSHGPSGPDGLAVDTSGRLLVANP
GLGYVWVLNHRAEPVLVLRGPAGASTTNLAFGGQGGQTVFVTDSTHGHILCARLDAPGLP
LHCSTLD
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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