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Comparing Ac3H11_2215 FitnessBrowser__acidovorax_3H11:Ac3H11_2215 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)
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
58% identity, 97% coverage: 6:451/462 of query aligns to 7:450/458 of 1pcjX
- active site: R15 (= R14), S103 (= S101), H104 (= H102), K113 (= K111), D237 (= D236), D239 (= D238), D241 (= D240), R242 (= R241), H324 (= H323), D335 (= D334)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (= Y11), S103 (= S101), T301 (= T300), G302 (= G301), E320 (= E319), S322 (= S321), H324 (= H323), R416 (= R417), S418 (= S419), N419 (= N420), T420 (= T421)
- binding zinc ion: S103 (= S101), D237 (= D236), D239 (= D238), D241 (= D240)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
58% identity, 97% coverage: 6:451/462 of query aligns to 4:447/455 of 2h5aX
- active site: H101 (= H102), D234 (= D236), D236 (= D238), D238 (= D240), R239 (= R241), D332 (= D334)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y11), T298 (= T300), G299 (= G301), H300 (= H302), E317 (= E319), S319 (= S321), H321 (= H323), R413 (= R417), S415 (= S419), N416 (= N420), T417 (= T421)
- binding zinc ion: S100 (= S101), D234 (= D236), D236 (= D238), D238 (= D240)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
58% identity, 97% coverage: 6:451/462 of query aligns to 4:447/455 of 2h4lX
- active site: H101 (= H102), D234 (= D236), D236 (= D238), D238 (= D240), R239 (= R241), D332 (= D334)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y11), R12 (= R14), S100 (= S101), T298 (= T300), E317 (= E319), R413 (= R417), S415 (= S419), N416 (= N420), T417 (= T421)
- binding zinc ion: S100 (= S101), D234 (= D236), D236 (= D238), D238 (= D240)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
58% identity, 97% coverage: 6:451/462 of query aligns to 4:447/455 of 2fkfA
- active site: R12 (= R14), S100 (= S101), H101 (= H102), K110 (= K111), D234 (= D236), D236 (= D238), D238 (= D240), R239 (= R241), H321 (= H323), D332 (= D334)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (≠ K9), H101 (= H102), S319 (= S321), R413 (= R417), S415 (= S419), N416 (= N420), T417 (= T421)
- binding zinc ion: S100 (= S101), D234 (= D236), D236 (= D238), D238 (= D240)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
58% identity, 97% coverage: 6:451/462 of query aligns to 4:447/455 of 1pcmX
- active site: R12 (= R14), S100 (= S101), H101 (= H102), K110 (= K111), D234 (= D236), D236 (= D238), D238 (= D240), R239 (= R241), H321 (= H323), D332 (= D334)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y11), S100 (= S101), T298 (= T300), G299 (= G301), H300 (= H302), E317 (= E319), S319 (= S321), H321 (= H323), R413 (= R417), S415 (= S419)
- binding zinc ion: S100 (= S101), D234 (= D236), D236 (= D238), D238 (= D240)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
58% identity, 97% coverage: 6:451/462 of query aligns to 4:447/455 of 1p5gX
- active site: R12 (= R14), S100 (= S101), H101 (= H102), K110 (= K111), D234 (= D236), D236 (= D238), D238 (= D240), R239 (= R241), H321 (= H323), D332 (= D334)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y11), S100 (= S101), K277 (= K279), G299 (= G301), H300 (= H302), E317 (= E319), S319 (= S321), H321 (= H323), R413 (= R417), S415 (= S419), N416 (= N420), T417 (= T421)
- binding zinc ion: S100 (= S101), D234 (= D236), D236 (= D238), D238 (= D240)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
58% identity, 97% coverage: 6:451/462 of query aligns to 4:447/455 of 1p5dX
- active site: R12 (= R14), S100 (= S101), H101 (= H102), K110 (= K111), D234 (= D236), D236 (= D238), D238 (= D240), R239 (= R241), H321 (= H323), D332 (= D334)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (= Y11), S100 (= S101), R239 (= R241), T298 (= T300), G299 (= G301), H300 (= H302), E317 (= E319), S319 (= S321), H321 (= H323), R413 (= R417), S415 (= S419), T417 (= T421)
- binding zinc ion: S100 (= S101), D234 (= D236), D236 (= D238), D238 (= D240)
P26276 Phosphomannomutase/phosphoglucomutase; PMM / PGM; EC 5.4.2.2; EC 5.4.2.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 10 papers)
58% identity, 97% coverage: 6:451/462 of query aligns to 12:455/463 of P26276
- R15 (≠ K9) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y11) binding ; binding
- R20 (= R14) mutation to A: No phosphoglucomutase activity.
- S108 (= S101) binding via phosphate group; modified: Phosphoserine; mutation S->A,V: About 5% activity, still subject to substrate inhibition and requires G1,6P as an activator; phosphorylation occurs at a different site.; mutation to C: KM for G1P unchanged, kcat decreases 24-fold; G1,6P stimulates reaction by 2-3 orders of magnitude. No stable protein phosphorylation detected, altered ligation of metal residue.
- N110 (= N103) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D236) binding
- D244 (= D238) binding
- D246 (= D240) binding
- R247 (= R241) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (= R256) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (= K279) binding
- H308 (= H302) binding ; binding
- E325 (= E319) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (= EMSGH 319:323) binding ; binding
- H329 (= H323) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P361) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R417) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (= RASNT 417:421) binding ; binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q02E40 Phosphomannomutase/phosphoglucomutase; PMM / PGM; EC 5.4.2.2; EC 5.4.2.8 from Pseudomonas aeruginosa (strain UCBPP-PA14) (see paper)
58% identity, 97% coverage: 6:451/462 of query aligns to 12:455/463 of Q02E40
- S108 (= S101) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
58% identity, 97% coverage: 6:451/462 of query aligns to 8:451/459 of 1k2yX
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
58% identity, 97% coverage: 6:451/462 of query aligns to 8:451/459 of 4il8A
- active site: R16 (= R14), S104 (= S101), H105 (= H102), K114 (= K111), D238 (= D236), D240 (= D238), D242 (= D240), R243 (= R241), A325 (≠ H323), D336 (= D334)
- binding magnesium ion: S104 (= S101), D238 (= D236), D240 (= D238), D242 (= D240)
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
57% identity, 98% coverage: 4:457/462 of query aligns to 3:456/458 of 3uw2A
- active site: R13 (= R14), S109 (= S101), H110 (= H102), K119 (= K111), D243 (= D236), D245 (= D238), D247 (= D240), R248 (= R241), H330 (= H323)
- binding zinc ion: D243 (= D236), D245 (= D238), D247 (= D240)
3rsmA Crystal structure of s108c mutant of pmm/pgm (see paper)
56% identity, 93% coverage: 21:451/462 of query aligns to 6:428/436 of 3rsmA
- active site: C87 (≠ S101), K91 (= K111), D215 (= D236), D217 (= D238), D219 (= D240), R220 (= R241), H302 (= H323), D313 (= D334)
- binding phosphate ion: C87 (≠ S101), D215 (= D236), D217 (= D238), D219 (= D240), R220 (= R241)
- binding zinc ion: D215 (= D236), D217 (= D238), D219 (= D240)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
35% identity, 96% coverage: 8:450/462 of query aligns to 6:447/448 of 6nqhA
- active site: R12 (= R14), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D236), D239 (= D238), D241 (= D240), R242 (= R241), H324 (= H323)
- binding magnesium ion: D237 (= D236), D239 (= D238), D241 (= D240)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R14), S97 (= S101), H98 (= H102), K107 (= K111), D239 (= D238), R242 (= R241), R280 (≠ K279), S301 (≠ T300), G302 (= G301), E320 (= E319), S322 (= S321), H324 (= H323), R414 (= R417), S416 (= S419), N417 (= N420), T418 (= T421), R423 (≠ V426)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
35% identity, 96% coverage: 8:450/462 of query aligns to 6:447/448 of 6np8A
- active site: R12 (= R14), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D236), D239 (= D238), D241 (= D240), R242 (= R241), H324 (= H323)
- binding calcium ion: S97 (= S101), D237 (= D236), D239 (= D238), D241 (= D240)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y11), R280 (≠ K279), G302 (= G301), H303 (= H302), E320 (= E319), S322 (= S321), H324 (= H323), R414 (= R417), S416 (= S419), N417 (= N420), T418 (= T421), R423 (≠ V426)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
35% identity, 96% coverage: 8:450/462 of query aligns to 6:447/448 of 6nolA
- active site: R12 (= R14), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D236), D239 (= D238), D241 (= D240), R242 (= R241), H324 (= H323)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G301), E320 (= E319), S322 (= S321), H324 (= H323), R414 (= R417), S416 (= S419), N417 (= N420), T418 (= T421), R423 (≠ V426)
- binding magnesium ion: S97 (= S101), D237 (= D236), D239 (= D238), D241 (= D240)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
35% identity, 96% coverage: 8:450/462 of query aligns to 6:447/448 of 6nnpA
- active site: R12 (= R14), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D236), D239 (= D238), D241 (= D240), R242 (= R241), H324 (= H323)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ K279), G302 (= G301), H303 (= H302), E320 (= E319), H324 (= H323), R414 (= R417), S416 (= S419), N417 (= N420), T418 (= T421), R423 (≠ V426)
- binding magnesium ion: S97 (= S101), D237 (= D236), D239 (= D238), D241 (= D240)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
35% identity, 96% coverage: 8:450/462 of query aligns to 6:447/448 of 6nn2A
- active site: R12 (= R14), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D236), D239 (= D238), D241 (= D240), R242 (= R241), H324 (= H323)
- binding calcium ion: S97 (= S101), D237 (= D236), D239 (= D238), D241 (= D240)
6n1eA Crystal structure of x. Citri phosphoglucomutase in complex with 1- methyl-glucose 6-phosphate (see paper)
35% identity, 96% coverage: 8:450/462 of query aligns to 6:447/448 of 6n1eA
6mnvA Crystal structure of x. Citri phosphoglucomutase in complex with ch2fg1p (see paper)
35% identity, 96% coverage: 8:450/462 of query aligns to 6:447/448 of 6mnvA
- binding 1-deoxy-1-fluoro-2-O-phosphono-alpha-D-gluco-hept-2-ulopyranose: R280 (≠ K279), G302 (= G301), E320 (= E319), S322 (= S321), H324 (= H323), R414 (= R417), S416 (= S419), N417 (= N420), T418 (= T421), R423 (≠ V426)
- binding magnesium ion: S97 (= S101), D237 (= D236), D239 (= D238), D241 (= D240)
Query Sequence
>Ac3H11_2215 FitnessBrowser__acidovorax_3H11:Ac3H11_2215
VQPTPAIFKAYDIRGIVPSTLNEEVALGLGRAFGTAARAEGQTTVAVGRDGRLSGPAMSA
ALIQGLVEAGIEVIDVGLVTTPLLYFAASTLCNSGIQVTGSHNPKDYNGFKMVLNGRAIY
GEEIQGLRRTMEQESWQLAPGGSVRHVDVLPTYRERIVGDVKLARPMKIVVDCGNGIAGA
SAPAIFRALGCEVIELFSEVDGNFPNHHPDPSKPENLRDLIDALKASDAELGLAFDGDGD
RLGIVTKDGTNIFPDRQMMLFAQDVLSRVPGGEIIFDVKCTQRLAPAIAAAGGVPVMFKT
GHSLIKARMKETNSPLGGEMSGHIFFKERWYGFDDGTYAGCRLLEILSKSQDPSAVLNAL
PTSFSTPELNVACAEGEPHRLTAELQALAAGQFAAPATVSTIDGLRVDWPDGFGLIRASN
TTPVLVLRFEGHTPEALARIEAAMLALLHRVLPDAHVGAASH
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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