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Comparing WP_012566880.1 NCBI__GCF_000016185.1:WP_012566880.1 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)
45% identity, 98% coverage: 10:460/460 of query aligns to 12:463/463 of P26276
- R15 (= R13) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y15) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- R20 (= R18) mutation to A: No phosphoglucomutase activity.
- S108 (= S106) 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 (= N108) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D240) binding Mg(2+)
- D244 (= D242) binding Mg(2+)
- D246 (= D244) binding Mg(2+)
- R247 (= R245) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Q260) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (= K283) binding alpha-D-glucose 1-phosphate
- H308 (= H306) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- E325 (= E323) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (= EMSGH 323:327) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- H329 (= H327) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P365) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R418) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (= RASNT 418:422) 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)
45% identity, 98% coverage: 10:460/460 of query aligns to 12:463/463 of Q02E40
- S108 (= S106) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
45% identity, 98% coverage: 10:460/460 of query aligns to 7:458/458 of 1pcjX
- active site: R15 (= R18), S103 (= S106), H104 (= H107), K113 (= K116), D237 (= D240), D239 (= D242), D241 (= D244), R242 (= R245), H324 (= H327), D335 (= D338)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (= Y15), S103 (= S106), T301 (= T304), G302 (= G305), E320 (= E323), S322 (= S325), H324 (= H327), R416 (= R418), S418 (= S420), N419 (= N421), T420 (= T422)
- binding zinc ion: S103 (= S106), D237 (= D240), D239 (= D242), D241 (= D244)
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
49% identity, 96% coverage: 10:450/460 of query aligns to 5:448/458 of 3uw2A
- active site: R13 (= R18), S109 (= S106), H110 (= H107), K119 (= K116), D243 (= D240), D245 (= D242), D247 (= D244), R248 (= R245), H330 (= H327)
- binding zinc ion: D243 (= D240), D245 (= D242), D247 (= D244)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
45% identity, 98% coverage: 10:460/460 of query aligns to 4:455/455 of 2h5aX
- active site: H101 (= H107), D234 (= D240), D236 (= D242), D238 (= D244), R239 (= R245), D332 (= D338)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y15), T298 (= T304), G299 (= G305), H300 (= H306), E317 (= E323), S319 (= S325), H321 (= H327), R413 (= R418), S415 (= S420), N416 (= N421), T417 (= T422)
- binding zinc ion: S100 (= S106), D234 (= D240), D236 (= D242), D238 (= D244)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
45% identity, 98% coverage: 10:460/460 of query aligns to 4:455/455 of 2h4lX
- active site: H101 (= H107), D234 (= D240), D236 (= D242), D238 (= D244), R239 (= R245), D332 (= D338)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y15), R12 (= R18), S100 (= S106), T298 (= T304), E317 (= E323), R413 (= R418), S415 (= S420), N416 (= N421), T417 (= T422)
- binding zinc ion: S100 (= S106), D234 (= D240), D236 (= D242), D238 (= D244)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
45% identity, 98% coverage: 10:460/460 of query aligns to 4:455/455 of 2fkfA
- active site: R12 (= R18), S100 (= S106), H101 (= H107), K110 (= K116), D234 (= D240), D236 (= D242), D238 (= D244), R239 (= R245), H321 (= H327), D332 (= D338)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (= R13), H101 (= H107), S319 (= S325), R413 (= R418), S415 (= S420), N416 (= N421), T417 (= T422)
- binding zinc ion: S100 (= S106), D234 (= D240), D236 (= D242), D238 (= D244)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
45% identity, 98% coverage: 10:460/460 of query aligns to 4:455/455 of 1pcmX
- active site: R12 (= R18), S100 (= S106), H101 (= H107), K110 (= K116), D234 (= D240), D236 (= D242), D238 (= D244), R239 (= R245), H321 (= H327), D332 (= D338)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y15), S100 (= S106), T298 (= T304), G299 (= G305), H300 (= H306), E317 (= E323), S319 (= S325), H321 (= H327), R413 (= R418), S415 (= S420)
- binding zinc ion: S100 (= S106), D234 (= D240), D236 (= D242), D238 (= D244)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
45% identity, 98% coverage: 10:460/460 of query aligns to 4:455/455 of 1p5gX
- active site: R12 (= R18), S100 (= S106), H101 (= H107), K110 (= K116), D234 (= D240), D236 (= D242), D238 (= D244), R239 (= R245), H321 (= H327), D332 (= D338)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y15), S100 (= S106), K277 (= K283), G299 (= G305), H300 (= H306), E317 (= E323), S319 (= S325), H321 (= H327), R413 (= R418), S415 (= S420), N416 (= N421), T417 (= T422)
- binding zinc ion: S100 (= S106), D234 (= D240), D236 (= D242), D238 (= D244)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
45% identity, 98% coverage: 10:460/460 of query aligns to 4:455/455 of 1p5dX
- active site: R12 (= R18), S100 (= S106), H101 (= H107), K110 (= K116), D234 (= D240), D236 (= D242), D238 (= D244), R239 (= R245), H321 (= H327), D332 (= D338)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (= Y15), S100 (= S106), R239 (= R245), T298 (= T304), G299 (= G305), H300 (= H306), E317 (= E323), S319 (= S325), H321 (= H327), R413 (= R418), S415 (= S420), T417 (= T422)
- binding zinc ion: S100 (= S106), D234 (= D240), D236 (= D242), D238 (= D244)
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
45% identity, 98% coverage: 10:460/460 of query aligns to 8:459/459 of 1k2yX
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
45% identity, 98% coverage: 10:460/460 of query aligns to 8:459/459 of 4il8A
- active site: R16 (= R18), S104 (= S106), H105 (= H107), K114 (= K116), D238 (= D240), D240 (= D242), D242 (= D244), R243 (= R245), A325 (≠ H327), D336 (= D338)
- binding magnesium ion: S104 (= S106), D238 (= D240), D240 (= D242), D242 (= D244)
3rsmA Crystal structure of s108c mutant of pmm/pgm (see paper)
43% identity, 96% coverage: 21:460/460 of query aligns to 2:436/436 of 3rsmA
- active site: C87 (≠ S106), K91 (= K116), D215 (= D240), D217 (= D242), D219 (= D244), R220 (= R245), H302 (= H327), D313 (= D338)
- binding phosphate ion: C87 (≠ S106), D215 (= D240), D217 (= D242), D219 (= D244), R220 (= R245)
- binding zinc ion: D215 (= D240), D217 (= D242), D219 (= D244)
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
34% identity, 91% coverage: 12:431/460 of query aligns to 7:428/449 of 6mlwA
- active site: R13 (= R18), S98 (= S106), H99 (= H107), K108 (= K116), D238 (= D240), D240 (= D242), D242 (= D244), R243 (= R245), H325 (= H327)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G305), H304 (= H306), E321 (= E323), S323 (= S325), H325 (= H327), R415 (= R418), S417 (= S420), N418 (= N421), T419 (= T422), R424 (≠ V427)
- binding magnesium ion: S98 (= S106), D238 (= D240), D240 (= D242), D242 (= D244)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
34% identity, 91% coverage: 12:431/460 of query aligns to 7:428/449 of 5bmpA
- active site: R13 (= R18), S98 (= S106), H99 (= H107), K108 (= K116), D238 (= D240), D240 (= D242), D242 (= D244), R243 (= R245), H325 (= H327)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ K283), G303 (= G305), E321 (= E323), S323 (= S325), H325 (= H327), R415 (= R418), S417 (= S420), N418 (= N421), T419 (= T422), R424 (≠ V427)
- binding magnesium ion: S98 (= S106), D238 (= D240), D240 (= D242), D242 (= D244)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
34% identity, 91% coverage: 12:431/460 of query aligns to 6:427/448 of 6nqhA
- active site: R12 (= R18), S97 (= S106), H98 (= H107), K107 (= K116), D237 (= D240), D239 (= D242), D241 (= D244), R242 (= R245), H324 (= H327)
- binding magnesium ion: D237 (= D240), D239 (= D242), D241 (= D244)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R18), S97 (= S106), H98 (= H107), K107 (= K116), D239 (= D242), R242 (= R245), R280 (≠ K283), S301 (≠ T304), G302 (= G305), E320 (= E323), S322 (= S325), H324 (= H327), R414 (= R418), S416 (= S420), N417 (= N421), T418 (= T422), R423 (≠ V427)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
34% identity, 91% coverage: 12:431/460 of query aligns to 6:427/448 of 6np8A
- active site: R12 (= R18), S97 (= S106), H98 (= H107), K107 (= K116), D237 (= D240), D239 (= D242), D241 (= D244), R242 (= R245), H324 (= H327)
- binding calcium ion: S97 (= S106), D237 (= D240), D239 (= D242), D241 (= D244)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y15), R280 (≠ K283), G302 (= G305), H303 (= H306), E320 (= E323), S322 (= S325), H324 (= H327), R414 (= R418), S416 (= S420), N417 (= N421), T418 (= T422), R423 (≠ V427)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
34% identity, 91% coverage: 12:431/460 of query aligns to 6:427/448 of 6nolA
- active site: R12 (= R18), S97 (= S106), H98 (= H107), K107 (= K116), D237 (= D240), D239 (= D242), D241 (= D244), R242 (= R245), H324 (= H327)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G305), E320 (= E323), S322 (= S325), H324 (= H327), R414 (= R418), S416 (= S420), N417 (= N421), T418 (= T422), R423 (≠ V427)
- binding magnesium ion: S97 (= S106), D237 (= D240), D239 (= D242), D241 (= D244)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
34% identity, 91% coverage: 12:431/460 of query aligns to 6:427/448 of 6nnpA
- active site: R12 (= R18), S97 (= S106), H98 (= H107), K107 (= K116), D237 (= D240), D239 (= D242), D241 (= D244), R242 (= R245), H324 (= H327)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ K283), G302 (= G305), H303 (= H306), E320 (= E323), H324 (= H327), R414 (= R418), S416 (= S420), N417 (= N421), T418 (= T422), R423 (≠ V427)
- binding magnesium ion: S97 (= S106), D237 (= D240), D239 (= D242), D241 (= D244)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
34% identity, 91% coverage: 12:431/460 of query aligns to 6:427/448 of 6nn2A
- active site: R12 (= R18), S97 (= S106), H98 (= H107), K107 (= K116), D237 (= D240), D239 (= D242), D241 (= D244), R242 (= R245), H324 (= H327)
- binding calcium ion: S97 (= S106), D237 (= D240), D239 (= D242), D241 (= D244)
Query Sequence
>WP_012566880.1 NCBI__GCF_000016185.1:WP_012566880.1
MSLAYQFHPTVLREYDIRGIIGKTLGPDDARAIGRAFGSMVARSGGKRVAVGYDGRLSSP
GLEAALVEGLTSTGLHVVRIGLGPTPMLYFATRHLPADAGIMITGSHNPPDYNGFKMMLG
KAPVFGETILEIGRIAAAGDFVTGEGSAETVDIRDVYVDRLLQDYDGTTPLKVVWDAGNG
ATGDILRRLVKKLPGEHVTLFDDIDGTFPNHHPDPTVPENLEDITERLHAEKAAIGIAFD
GDGDRIGAIDEKGRIVWGDQLIAIYAADVLKTHPGATIIADVKASQTLFDEIARLGGHPL
MWKTGHSLLKAKMAETGSPLAGEMSGHIFFADKYYGFDDALYCAVRLIGLVSRTGPLSAL
RDRLPAVLNTPEVRFQVDEERKFASVREIQERVRASGAQVNDIDGVRVTTPDGWWLLRAS
NTQDVLVARAEAYSAEGLERLKASIREQLKLSGIAAPEGF
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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