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Comparing WP_011383016.1 NCBI__GCF_000009985.1:WP_011383016.1 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: 8:456/460 of query aligns to 12:459/463 of P26276
- R15 (= R11) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y13) binding ; binding
- R20 (= R16) mutation to A: No phosphoglucomutase activity.
- S108 (= S104) 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 (= N106) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D238) binding
- D244 (= D240) binding
- D246 (= D242) binding
- R247 (= R243) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Q258) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (= K281) binding
- H308 (= H304) binding ; binding
- E325 (= E321) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (= EMSGH 321:325) binding ; binding
- H329 (= H325) 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 ; 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)
45% identity, 98% coverage: 8:456/460 of query aligns to 12:459/463 of Q02E40
- S108 (= S104) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
45% identity, 98% coverage: 8:456/460 of query aligns to 7:454/458 of 1pcjX
- active site: R15 (= R16), S103 (= S104), H104 (= H105), K113 (= K114), D237 (= D238), D239 (= D240), D241 (= D242), R242 (= R243), H324 (= H325), D335 (= D336)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (= Y13), S103 (= S104), T301 (= T302), G302 (= G303), E320 (= E321), S322 (= S323), H324 (= H325), R416 (= R418), S418 (= S420), N419 (= N421), T420 (= T422)
- binding zinc ion: S103 (= S104), D237 (= D238), D239 (= D240), D241 (= D242)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
45% identity, 98% coverage: 8:456/460 of query aligns to 4:451/455 of 2h5aX
- active site: H101 (= H105), D234 (= D238), D236 (= D240), D238 (= D242), R239 (= R243), D332 (= D336)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y13), T298 (= T302), G299 (= G303), H300 (= H304), E317 (= E321), S319 (= S323), H321 (= H325), R413 (= R418), S415 (= S420), N416 (= N421), T417 (= T422)
- binding zinc ion: S100 (= S104), D234 (= D238), D236 (= D240), D238 (= D242)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
45% identity, 98% coverage: 8:456/460 of query aligns to 4:451/455 of 2h4lX
- active site: H101 (= H105), D234 (= D238), D236 (= D240), D238 (= D242), R239 (= R243), D332 (= D336)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y13), R12 (= R16), S100 (= S104), T298 (= T302), E317 (= E321), R413 (= R418), S415 (= S420), N416 (= N421), T417 (= T422)
- binding zinc ion: S100 (= S104), D234 (= D238), D236 (= D240), D238 (= D242)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
45% identity, 98% coverage: 8:456/460 of query aligns to 4:451/455 of 2fkfA
- active site: R12 (= R16), S100 (= S104), H101 (= H105), K110 (= K114), D234 (= D238), D236 (= D240), D238 (= D242), R239 (= R243), H321 (= H325), D332 (= D336)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (= R11), H101 (= H105), S319 (= S323), R413 (= R418), S415 (= S420), N416 (= N421), T417 (= T422)
- binding zinc ion: S100 (= S104), D234 (= D238), D236 (= D240), D238 (= D242)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
45% identity, 98% coverage: 8:456/460 of query aligns to 4:451/455 of 1pcmX
- active site: R12 (= R16), S100 (= S104), H101 (= H105), K110 (= K114), D234 (= D238), D236 (= D240), D238 (= D242), R239 (= R243), H321 (= H325), D332 (= D336)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y13), S100 (= S104), T298 (= T302), G299 (= G303), H300 (= H304), E317 (= E321), S319 (= S323), H321 (= H325), R413 (= R418), S415 (= S420)
- binding zinc ion: S100 (= S104), D234 (= D238), D236 (= D240), D238 (= D242)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
45% identity, 98% coverage: 8:456/460 of query aligns to 4:451/455 of 1p5gX
- active site: R12 (= R16), S100 (= S104), H101 (= H105), K110 (= K114), D234 (= D238), D236 (= D240), D238 (= D242), R239 (= R243), H321 (= H325), D332 (= D336)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y13), S100 (= S104), K277 (= K281), G299 (= G303), H300 (= H304), E317 (= E321), S319 (= S323), H321 (= H325), R413 (= R418), S415 (= S420), N416 (= N421), T417 (= T422)
- binding zinc ion: S100 (= S104), D234 (= D238), D236 (= D240), D238 (= D242)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
45% identity, 98% coverage: 8:456/460 of query aligns to 4:451/455 of 1p5dX
- active site: R12 (= R16), S100 (= S104), H101 (= H105), K110 (= K114), D234 (= D238), D236 (= D240), D238 (= D242), R239 (= R243), H321 (= H325), D332 (= D336)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (= Y13), S100 (= S104), R239 (= R243), T298 (= T302), G299 (= G303), H300 (= H304), E317 (= E321), S319 (= S323), H321 (= H325), R413 (= R418), S415 (= S420), T417 (= T422)
- binding zinc ion: S100 (= S104), D234 (= D238), D236 (= D240), D238 (= D242)
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
45% identity, 98% coverage: 8:456/460 of query aligns to 8:455/459 of 1k2yX
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
45% identity, 98% coverage: 8:456/460 of query aligns to 8:455/459 of 4il8A
- active site: R16 (= R16), S104 (= S104), H105 (= H105), K114 (= K114), D238 (= D238), D240 (= D240), D242 (= D242), R243 (= R243), A325 (≠ H325), D336 (= D336)
- binding magnesium ion: S104 (= S104), D238 (= D238), D240 (= D240), D242 (= D242)
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
46% identity, 97% coverage: 8:452/460 of query aligns to 5:450/458 of 3uw2A
- active site: R13 (= R16), S109 (= S104), H110 (= H105), K119 (= K114), D243 (= D238), D245 (= D240), D247 (= D242), R248 (= R243), H330 (= H325)
- binding zinc ion: D243 (= D238), D245 (= D240), D247 (= D242)
3rsmA Crystal structure of s108c mutant of pmm/pgm (see paper)
43% identity, 95% coverage: 19:456/460 of query aligns to 2:432/436 of 3rsmA
- active site: C87 (≠ S104), K91 (= K114), D215 (= D238), D217 (= D240), D219 (= D242), R220 (= R243), H302 (= H325), D313 (= D336)
- binding phosphate ion: C87 (≠ S104), D215 (= D238), D217 (= D240), D219 (= D242), R220 (= R243)
- binding zinc ion: D215 (= D238), D217 (= D240), D219 (= D242)
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
32% identity, 94% coverage: 10:442/460 of query aligns to 7:439/449 of 6mlwA
- active site: R13 (= R16), S98 (= S104), H99 (= H105), K108 (= K114), D238 (= D238), D240 (= D240), D242 (= D242), R243 (= R243), H325 (= H325)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G303), H304 (= H304), E321 (= E321), S323 (= S323), H325 (= H325), R415 (= R418), S417 (= S420), N418 (= N421), T419 (= T422), R424 (≠ V427)
- binding magnesium ion: S98 (= S104), D238 (= D238), D240 (= D240), D242 (= D242)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
32% identity, 94% coverage: 10:442/460 of query aligns to 7:439/449 of 5bmpA
- active site: R13 (= R16), S98 (= S104), H99 (= H105), K108 (= K114), D238 (= D238), D240 (= D240), D242 (= D242), R243 (= R243), H325 (= H325)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ K281), G303 (= G303), E321 (= E321), S323 (= S323), H325 (= H325), R415 (= R418), S417 (= S420), N418 (= N421), T419 (= T422), R424 (≠ V427)
- binding magnesium ion: S98 (= S104), D238 (= D238), D240 (= D240), D242 (= D242)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
32% identity, 94% coverage: 10:442/460 of query aligns to 6:438/448 of 6nqhA
- active site: R12 (= R16), S97 (= S104), H98 (= H105), K107 (= K114), D237 (= D238), D239 (= D240), D241 (= D242), R242 (= R243), H324 (= H325)
- binding magnesium ion: D237 (= D238), D239 (= D240), D241 (= D242)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R16), S97 (= S104), H98 (= H105), K107 (= K114), D239 (= D240), R242 (= R243), R280 (≠ K281), S301 (≠ T302), G302 (= G303), E320 (= E321), S322 (= S323), H324 (= H325), R414 (= R418), S416 (= S420), N417 (= N421), T418 (= T422), R423 (≠ V427)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
32% identity, 94% coverage: 10:442/460 of query aligns to 6:438/448 of 6np8A
- active site: R12 (= R16), S97 (= S104), H98 (= H105), K107 (= K114), D237 (= D238), D239 (= D240), D241 (= D242), R242 (= R243), H324 (= H325)
- binding calcium ion: S97 (= S104), D237 (= D238), D239 (= D240), D241 (= D242)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y13), R280 (≠ K281), G302 (= G303), H303 (= H304), E320 (= E321), S322 (= S323), H324 (= H325), R414 (= R418), S416 (= S420), N417 (= N421), T418 (= T422), R423 (≠ V427)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
32% identity, 94% coverage: 10:442/460 of query aligns to 6:438/448 of 6nolA
- active site: R12 (= R16), S97 (= S104), H98 (= H105), K107 (= K114), D237 (= D238), D239 (= D240), D241 (= D242), R242 (= R243), H324 (= H325)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G303), E320 (= E321), S322 (= S323), H324 (= H325), R414 (= R418), S416 (= S420), N417 (= N421), T418 (= T422), R423 (≠ V427)
- binding magnesium ion: S97 (= S104), D237 (= D238), D239 (= D240), D241 (= D242)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
32% identity, 94% coverage: 10:442/460 of query aligns to 6:438/448 of 6nnpA
- active site: R12 (= R16), S97 (= S104), H98 (= H105), K107 (= K114), D237 (= D238), D239 (= D240), D241 (= D242), R242 (= R243), H324 (= H325)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ K281), G302 (= G303), H303 (= H304), E320 (= E321), H324 (= H325), R414 (= R418), S416 (= S420), N417 (= N421), T418 (= T422), R423 (≠ V427)
- binding magnesium ion: S97 (= S104), D237 (= D238), D239 (= D240), D241 (= D242)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
32% identity, 94% coverage: 10:442/460 of query aligns to 6:438/448 of 6nn2A
- active site: R12 (= R16), S97 (= S104), H98 (= H105), K107 (= K114), D237 (= D238), D239 (= D240), D241 (= D242), R242 (= R243), H324 (= H325)
- binding calcium ion: S97 (= S104), D237 (= D238), D239 (= D240), D241 (= D242)
Query Sequence
>WP_011383016.1 NCBI__GCF_000009985.1:WP_011383016.1
MTHIFHPTILREYDIRGIIGETLFAADAEAIGRAFGTRVRRNGGHVVCLGWDGRLSSPEM
AEALTKGLMAAGCTVRRVGRGPTPMLYFAAKVRDADGGIMVTGSHNPPNHNGFKMVLAGR
PFFGPDIQSLGTIAAAGDFASGEGKAVEDSVFEEYVSRLAQDYDGLRDLRVVWDCGNGAT
GEVLHALVKRLPGTHTVLFGEIDGHFPNHHPDPTEPHNLVALQDKVLTESAHLGIAFDGD
GDRIGVVDAEGRILYGDQILVILAEDLLKSLPGATIIADVKASKVFFDEVRRMGGNAVMG
RTGHSLIKTQMAETGAPLAGEMSGHIFFADRYYGFDDALYAAIRLLGIVARWDHTTIGQR
RDRLPHMVNTPELRFDCPEERKFAVVAEVKARLEAEGASFSAIDGVRVDTPDGWWLLRAS
NTQAVLVARCEAASSEGLKHLRQTLADQLAASGVSLGHTH
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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