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Comparing PP_5288 FitnessBrowser__Putida:PP_5288 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)
78% identity, 98% coverage: 9:463/463 of query aligns to 9:463/463 of P26276
- R15 (= R15) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y17) binding ; binding
- R20 (= R20) mutation to A: No phosphoglucomutase activity.
- S108 (= S108) 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 (= N110) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D242) binding
- D244 (= D244) binding
- D246 (= D246) binding
- R247 (= R247) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (= R262) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (= K285) binding
- H308 (= H308) binding ; binding
- E325 (= E325) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (= EMSGH 325:329) binding ; binding
- H329 (= H329) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P368) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R421) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (= RASNT 421:425) 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)
78% identity, 98% coverage: 9:463/463 of query aligns to 9:463/463 of Q02E40
- S108 (= S108) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
78% identity, 98% coverage: 9:463/463 of query aligns to 4:458/458 of 1pcjX
- active site: R15 (= R20), S103 (= S108), H104 (= H109), K113 (= K118), D237 (= D242), D239 (= D244), D241 (= D246), R242 (= R247), H324 (= H329), D335 (= D340)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (= Y17), S103 (= S108), T301 (= T306), G302 (= G307), E320 (= E325), S322 (= S327), H324 (= H329), R416 (= R421), S418 (= S423), N419 (= N424), T420 (= T425)
- binding zinc ion: S103 (= S108), D237 (= D242), D239 (= D244), D241 (= D246)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
78% identity, 98% coverage: 9:463/463 of query aligns to 1:455/455 of 2h5aX
- active site: H101 (= H109), D234 (= D242), D236 (= D244), D238 (= D246), R239 (= R247), D332 (= D340)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y17), T298 (= T306), G299 (= G307), H300 (= H308), E317 (= E325), S319 (= S327), H321 (= H329), R413 (= R421), S415 (= S423), N416 (= N424), T417 (= T425)
- binding zinc ion: S100 (= S108), D234 (= D242), D236 (= D244), D238 (= D246)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
78% identity, 98% coverage: 9:463/463 of query aligns to 1:455/455 of 2h4lX
- active site: H101 (= H109), D234 (= D242), D236 (= D244), D238 (= D246), R239 (= R247), D332 (= D340)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y17), R12 (= R20), S100 (= S108), T298 (= T306), E317 (= E325), R413 (= R421), S415 (= S423), N416 (= N424), T417 (= T425)
- binding zinc ion: S100 (= S108), D234 (= D242), D236 (= D244), D238 (= D246)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
78% identity, 98% coverage: 9:463/463 of query aligns to 1:455/455 of 2fkfA
- active site: R12 (= R20), S100 (= S108), H101 (= H109), K110 (= K118), D234 (= D242), D236 (= D244), D238 (= D246), R239 (= R247), H321 (= H329), D332 (= D340)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (= R15), H101 (= H109), S319 (= S327), R413 (= R421), S415 (= S423), N416 (= N424), T417 (= T425)
- binding zinc ion: S100 (= S108), D234 (= D242), D236 (= D244), D238 (= D246)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
78% identity, 98% coverage: 9:463/463 of query aligns to 1:455/455 of 1pcmX
- active site: R12 (= R20), S100 (= S108), H101 (= H109), K110 (= K118), D234 (= D242), D236 (= D244), D238 (= D246), R239 (= R247), H321 (= H329), D332 (= D340)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y17), S100 (= S108), T298 (= T306), G299 (= G307), H300 (= H308), E317 (= E325), S319 (= S327), H321 (= H329), R413 (= R421), S415 (= S423)
- binding zinc ion: S100 (= S108), D234 (= D242), D236 (= D244), D238 (= D246)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
78% identity, 98% coverage: 9:463/463 of query aligns to 1:455/455 of 1p5gX
- active site: R12 (= R20), S100 (= S108), H101 (= H109), K110 (= K118), D234 (= D242), D236 (= D244), D238 (= D246), R239 (= R247), H321 (= H329), D332 (= D340)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y17), S100 (= S108), K277 (= K285), G299 (= G307), H300 (= H308), E317 (= E325), S319 (= S327), H321 (= H329), R413 (= R421), S415 (= S423), N416 (= N424), T417 (= T425)
- binding zinc ion: S100 (= S108), D234 (= D242), D236 (= D244), D238 (= D246)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
78% identity, 98% coverage: 9:463/463 of query aligns to 1:455/455 of 1p5dX
- active site: R12 (= R20), S100 (= S108), H101 (= H109), K110 (= K118), D234 (= D242), D236 (= D244), D238 (= D246), R239 (= R247), H321 (= H329), D332 (= D340)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (= Y17), S100 (= S108), R239 (= R247), T298 (= T306), G299 (= G307), H300 (= H308), E317 (= E325), S319 (= S327), H321 (= H329), R413 (= R421), S415 (= S423), T417 (= T425)
- binding zinc ion: S100 (= S108), D234 (= D242), D236 (= D244), D238 (= D246)
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
78% identity, 98% coverage: 9:463/463 of query aligns to 5:459/459 of 1k2yX
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
78% identity, 98% coverage: 9:463/463 of query aligns to 5:459/459 of 4il8A
- active site: R16 (= R20), S104 (= S108), H105 (= H109), K114 (= K118), D238 (= D242), D240 (= D244), D242 (= D246), R243 (= R247), A325 (≠ H329), D336 (= D340)
- binding magnesium ion: S104 (= S108), D238 (= D242), D240 (= D244), D242 (= D246)
3rsmA Crystal structure of s108c mutant of pmm/pgm (see paper)
75% identity, 98% coverage: 12:463/463 of query aligns to 1:436/436 of 3rsmA
- active site: C87 (≠ S108), K91 (= K118), D215 (= D242), D217 (= D244), D219 (= D246), R220 (= R247), H302 (= H329), D313 (= D340)
- binding phosphate ion: C87 (≠ S108), D215 (= D242), D217 (= D244), D219 (= D246), R220 (= R247)
- binding zinc ion: D215 (= D242), D217 (= D244), D219 (= D246)
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
56% identity, 98% coverage: 12:463/463 of query aligns to 5:458/458 of 3uw2A
- active site: R13 (= R20), S109 (= S108), H110 (= H109), K119 (= K118), D243 (= D242), D245 (= D244), D247 (= D246), R248 (= R247), H330 (= H329)
- binding zinc ion: D243 (= D242), D245 (= D244), D247 (= D246)
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
36% identity, 95% coverage: 14:454/463 of query aligns to 7:448/449 of 6mlwA
- active site: R13 (= R20), S98 (= S108), H99 (= H109), K108 (= K118), D238 (= D242), D240 (= D244), D242 (= D246), R243 (= R247), H325 (= H329)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G307), H304 (= H308), E321 (= E325), S323 (= S327), H325 (= H329), R415 (= R421), S417 (= S423), N418 (= N424), T419 (= T425), R424 (≠ V430)
- binding magnesium ion: S98 (= S108), D238 (= D242), D240 (= D244), D242 (= D246)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
36% identity, 95% coverage: 14:454/463 of query aligns to 7:448/449 of 5bmpA
- active site: R13 (= R20), S98 (= S108), H99 (= H109), K108 (= K118), D238 (= D242), D240 (= D244), D242 (= D246), R243 (= R247), H325 (= H329)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ K285), G303 (= G307), E321 (= E325), S323 (= S327), H325 (= H329), R415 (= R421), S417 (= S423), N418 (= N424), T419 (= T425), R424 (≠ V430)
- binding magnesium ion: S98 (= S108), D238 (= D242), D240 (= D244), D242 (= D246)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
36% identity, 95% coverage: 14:454/463 of query aligns to 6:447/448 of 6nqhA
- active site: R12 (= R20), S97 (= S108), H98 (= H109), K107 (= K118), D237 (= D242), D239 (= D244), D241 (= D246), R242 (= R247), H324 (= H329)
- binding magnesium ion: D237 (= D242), D239 (= D244), D241 (= D246)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R20), S97 (= S108), H98 (= H109), K107 (= K118), D239 (= D244), R242 (= R247), R280 (≠ K285), S301 (≠ T306), G302 (= G307), E320 (= E325), S322 (= S327), H324 (= H329), R414 (= R421), S416 (= S423), N417 (= N424), T418 (= T425), R423 (≠ V430)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
36% identity, 95% coverage: 14:454/463 of query aligns to 6:447/448 of 6np8A
- active site: R12 (= R20), S97 (= S108), H98 (= H109), K107 (= K118), D237 (= D242), D239 (= D244), D241 (= D246), R242 (= R247), H324 (= H329)
- binding calcium ion: S97 (= S108), D237 (= D242), D239 (= D244), D241 (= D246)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y17), R280 (≠ K285), G302 (= G307), H303 (= H308), E320 (= E325), S322 (= S327), H324 (= H329), R414 (= R421), S416 (= S423), N417 (= N424), T418 (= T425), R423 (≠ V430)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
36% identity, 95% coverage: 14:454/463 of query aligns to 6:447/448 of 6nolA
- active site: R12 (= R20), S97 (= S108), H98 (= H109), K107 (= K118), D237 (= D242), D239 (= D244), D241 (= D246), R242 (= R247), H324 (= H329)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G307), E320 (= E325), S322 (= S327), H324 (= H329), R414 (= R421), S416 (= S423), N417 (= N424), T418 (= T425), R423 (≠ V430)
- binding magnesium ion: S97 (= S108), D237 (= D242), D239 (= D244), D241 (= D246)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
36% identity, 95% coverage: 14:454/463 of query aligns to 6:447/448 of 6nnpA
- active site: R12 (= R20), S97 (= S108), H98 (= H109), K107 (= K118), D237 (= D242), D239 (= D244), D241 (= D246), R242 (= R247), H324 (= H329)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ K285), G302 (= G307), H303 (= H308), E320 (= E325), H324 (= H329), R414 (= R421), S416 (= S423), N417 (= N424), T418 (= T425), R423 (≠ V430)
- binding magnesium ion: S97 (= S108), D237 (= D242), D239 (= D244), D241 (= D246)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
36% identity, 95% coverage: 14:454/463 of query aligns to 6:447/448 of 6nn2A
- active site: R12 (= R20), S97 (= S108), H98 (= H109), K107 (= K118), D237 (= D242), D239 (= D244), D241 (= D246), R242 (= R247), H324 (= H329)
- binding calcium ion: S97 (= S108), D237 (= D242), D239 (= D244), D241 (= D246)
Query Sequence
>PP_5288 FitnessBrowser__Putida:PP_5288
MAHLVPAALPDSIFRAYDIRGVVGKTLHAETAYWIGRAIGAQSLAQGEPQVSVGRDGRLS
GPMLVEQLIKGLVDAGCNVSDVGLVPTPALYYAANVLAGKSGVMLTGSHNPSDYNGFKIV
IAGDTLANEQIQALLTRLKTNDLTLAQGRVEKVEILDRYFKQIVGDVKLAKKLKVVVDCG
NGAAGVVAPQLIEALGCEVIPLFCEVDGNFPNHHPDPGKPENLEDLIAKVKETGADIGLA
FDGDGDRVGVVTNTGSIVYPDRLLMLFAQDVLSRNPGAEIIFDVKCTRRLTPLIEQHGGR
ALMWKTGHSLIKKKMKQTGSLLAGEMSGHIFIKERWYGFDDGIYSAARLLEILSKTEQSA
ENLFAAFPNDISTPEINIDVTDEGKFSIIDALQRDADWGEANLTTIDGVRVDYANGWGLV
RASNTTPVLVLRFEADSDAELQRIKDVFRTQLLRVEPELQLPF
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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