SitesBLAST
Comparing WP_047006996.1 NCBI__GCF_001010925.1:WP_047006996.1 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)
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)
46% identity, 96% coverage: 8:459/472 of query aligns to 12:452/463 of P26276
- R15 (= R11) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y13) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- R20 (= R16) mutation to A: No phosphoglucomutase activity.
- S108 (= S110) 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 (= N112) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D249) binding Mg(2+)
- D244 (= D251) binding Mg(2+)
- D246 (= D253) binding Mg(2+)
- R247 (= R254) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Q269) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (= K292) binding alpha-D-glucose 1-phosphate
- H308 (= H315) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- E325 (= E332) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (= EMSGH 332:336) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- H329 (= H336) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P375) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R428) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (= RASNT 428:432) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
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)
46% identity, 96% coverage: 8:459/472 of query aligns to 12:452/463 of Q02E40
- S108 (= S110) active site, Non-phosphorylated intermediate; modified: Phosphoserine
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
46% identity, 96% coverage: 8:459/472 of query aligns to 4:444/455 of 2h5aX
- active site: H101 (= H111), D234 (= D249), D236 (= D251), D238 (= D253), R239 (= R254), D332 (= D347)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y13), T298 (= T313), G299 (= G314), H300 (= H315), E317 (= E332), S319 (= S334), H321 (= H336), R413 (= R428), S415 (= S430), N416 (= N431), T417 (= T432)
- binding zinc ion: S100 (= S110), D234 (= D249), D236 (= D251), D238 (= D253)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
46% identity, 96% coverage: 8:459/472 of query aligns to 4:444/455 of 2h4lX
- active site: H101 (= H111), D234 (= D249), D236 (= D251), D238 (= D253), R239 (= R254), D332 (= D347)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y13), R12 (= R16), S100 (= S110), T298 (= T313), E317 (= E332), R413 (= R428), S415 (= S430), N416 (= N431), T417 (= T432)
- binding zinc ion: S100 (= S110), D234 (= D249), D236 (= D251), D238 (= D253)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
46% identity, 96% coverage: 8:459/472 of query aligns to 4:444/455 of 2fkfA
- active site: R12 (= R16), S100 (= S110), H101 (= H111), K110 (= K120), D234 (= D249), D236 (= D251), D238 (= D253), R239 (= R254), H321 (= H336), D332 (= D347)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (= R11), H101 (= H111), S319 (= S334), R413 (= R428), S415 (= S430), N416 (= N431), T417 (= T432)
- binding zinc ion: S100 (= S110), D234 (= D249), D236 (= D251), D238 (= D253)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
46% identity, 96% coverage: 8:459/472 of query aligns to 4:444/455 of 1pcmX
- active site: R12 (= R16), S100 (= S110), H101 (= H111), K110 (= K120), D234 (= D249), D236 (= D251), D238 (= D253), R239 (= R254), H321 (= H336), D332 (= D347)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y13), S100 (= S110), T298 (= T313), G299 (= G314), H300 (= H315), E317 (= E332), S319 (= S334), H321 (= H336), R413 (= R428), S415 (= S430)
- binding zinc ion: S100 (= S110), D234 (= D249), D236 (= D251), D238 (= D253)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
46% identity, 96% coverage: 8:459/472 of query aligns to 4:444/455 of 1p5gX
- active site: R12 (= R16), S100 (= S110), H101 (= H111), K110 (= K120), D234 (= D249), D236 (= D251), D238 (= D253), R239 (= R254), H321 (= H336), D332 (= D347)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y13), S100 (= S110), K277 (= K292), G299 (= G314), H300 (= H315), E317 (= E332), S319 (= S334), H321 (= H336), R413 (= R428), S415 (= S430), N416 (= N431), T417 (= T432)
- binding zinc ion: S100 (= S110), D234 (= D249), D236 (= D251), D238 (= D253)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
46% identity, 96% coverage: 8:459/472 of query aligns to 4:444/455 of 1p5dX
- active site: R12 (= R16), S100 (= S110), H101 (= H111), K110 (= K120), D234 (= D249), D236 (= D251), D238 (= D253), R239 (= R254), H321 (= H336), D332 (= D347)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (= Y13), S100 (= S110), R239 (= R254), T298 (= T313), G299 (= G314), H300 (= H315), E317 (= E332), S319 (= S334), H321 (= H336), R413 (= R428), S415 (= S430), T417 (= T432)
- binding zinc ion: S100 (= S110), D234 (= D249), D236 (= D251), D238 (= D253)
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
46% identity, 96% coverage: 8:459/472 of query aligns to 7:447/458 of 1pcjX
- active site: R15 (= R16), S103 (= S110), H104 (= H111), K113 (= K120), D237 (= D249), D239 (= D251), D241 (= D253), R242 (= R254), H324 (= H336), D335 (= D347)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (= Y13), S103 (= S110), T301 (= T313), G302 (= G314), E320 (= E332), S322 (= S334), H324 (= H336), R416 (= R428), S418 (= S430), N419 (= N431), T420 (= T432)
- binding zinc ion: S103 (= S110), D237 (= D249), D239 (= D251), D241 (= D253)
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
46% identity, 96% coverage: 8:459/472 of query aligns to 8:448/459 of 1k2yX