SitesBLAST
Comparing 8501959 DvMF_2673 Phosphomannomutase (RefSeq) to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
46% identity, 95% coverage: 9:451/464 of query aligns to 9:449/458 of 1pcjX
- active site: R15 (= R15), S103 (= S103), H104 (= H104), K113 (= K113), D237 (= D241), D239 (= D243), D241 (= D245), R242 (= R246), H324 (= H328), D335 (= D339)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (= Y12), S103 (= S103), T301 (= T305), G302 (= G306), E320 (= E324), S322 (= S326), H324 (= H328), R416 (= R418), S418 (= S420), N419 (= N421), T420 (= T422)
- binding zinc ion: S103 (= S103), D237 (= D241), D239 (= D243), D241 (= D245)
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, 95% coverage: 9:451/464 of query aligns to 14:454/463 of P26276
- R15 (= R10) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y12) binding ; binding
- R20 (= R15) mutation to A: No phosphoglucomutase activity.
- S108 (= S103) 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 (= N105) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D241) binding
- D244 (= D243) binding
- D246 (= D245) binding
- R247 (= R246) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ E261) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (= K284) binding
- H308 (= H307) binding ; binding
- E325 (= E324) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (= EMSGH 324:328) binding ; binding
- H329 (= H328) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P366) 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)
46% identity, 95% coverage: 9:451/464 of query aligns to 14:454/463 of Q02E40
- S108 (= S103) active site, Non-phosphorylated intermediate; modified: Phosphoserine
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
46% identity, 95% coverage: 9:451/464 of query aligns to 6:446/455 of 2h5aX
- active site: H101 (= H104), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), D332 (= D339)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y12), T298 (= T305), G299 (= G306), H300 (= H307), E317 (= E324), S319 (= S326), H321 (= H328), R413 (= R418), S415 (= S420), N416 (= N421), T417 (= T422)
- binding zinc ion: S100 (= S103), D234 (= D241), D236 (= D243), D238 (= D245)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
46% identity, 95% coverage: 9:451/464 of query aligns to 6:446/455 of 2h4lX
- active site: H101 (= H104), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), D332 (= D339)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y12), R12 (= R15), S100 (= S103), T298 (= T305), E317 (= E324), R413 (= R418), S415 (= S420), N416 (= N421), T417 (= T422)
- binding zinc ion: S100 (= S103), D234 (= D241), D236 (= D243), D238 (= D245)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
46% identity, 95% coverage: 9:451/464 of query aligns to 6:446/455 of 2fkfA
- active site: R12 (= R15), S100 (= S103), H101 (= H104), K110 (= K113), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), H321 (= H328), D332 (= D339)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (= R10), H101 (= H104), S319 (= S326), R413 (= R418), S415 (= S420), N416 (= N421), T417 (= T422)
- binding zinc ion: S100 (= S103), D234 (= D241), D236 (= D243), D238 (= D245)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
46% identity, 95% coverage: 9:451/464 of query aligns to 6:446/455 of 1pcmX
- active site: R12 (= R15), S100 (= S103), H101 (= H104), K110 (= K113), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), H321 (= H328), D332 (= D339)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y12), S100 (= S103), T298 (= T305), G299 (= G306), H300 (= H307), E317 (= E324), S319 (= S326), H321 (= H328), R413 (= R418), S415 (= S420)
- binding zinc ion: S100 (= S103), D234 (= D241), D236 (= D243), D238 (= D245)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
46% identity, 95% coverage: 9:451/464 of query aligns to 6:446/455 of 1p5gX
- active site: R12 (= R15), S100 (= S103), H101 (= H104), K110 (= K113), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), H321 (= H328), D332 (= D339)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y12), S100 (= S103), K277 (= K284), G299 (= G306), H300 (= H307), E317 (= E324), S319 (= S326), H321 (= H328), R413 (= R418), S415 (= S420), N416 (= N421), T417 (= T422)
- binding zinc ion: S100 (= S103), D234 (= D241), D236 (= D243), D238 (= D245)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
46% identity, 95% coverage: 9:451/464 of query aligns to 6:446/455 of 1p5dX
- active site: R12 (= R15), S100 (= S103), H101 (= H104), K110 (= K113), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), H321 (= H328), D332 (= D339)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (= Y12), S100 (= S103), R239 (= R246), T298 (= T305), G299 (= G306), H300 (= H307), E317 (= E324), S319 (= S326), H321 (= H328), R413 (= R418), S415 (= S420), T417 (= T422)
- binding zinc ion: S100 (= S103), D234 (= D241), D236 (= D243), D238 (= D245)
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
46% identity, 95% coverage: 9:451/464 of query aligns to 10:450/459 of 1k2yX
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
46% identity, 95% coverage: 9:451/464 of query aligns to 10:450/459 of 4il8A
- active site: R16 (= R15), S104 (= S103), H105 (= H104), K114 (= K113), D238 (= D241), D240 (= D243), D242 (= D245), R243 (= R246), A325 (≠ H328), D336 (= D339)
- binding magnesium ion: S104 (= S103), D238 (= D241), D240 (= D243), D242 (= D245)
3rsmA Crystal structure of s108c mutant of pmm/pgm (see paper)
44% identity, 92% coverage: 24:451/464 of query aligns to 8:427/436 of 3rsmA
- active site: C87 (≠ S103), K91 (= K113), D215 (= D241), D217 (= D243), D219 (= D245), R220 (= R246), H302 (= H328), D313 (= D339)
- binding phosphate ion: C87 (≠ S103), D215 (= D241), D217 (= D243), D219 (= D245), R220 (= R246)
- binding zinc ion: D215 (= D241), D217 (= D243), D219 (= D245)
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
44% identity, 95% coverage: 4:442/464 of query aligns to 2:440/458 of 3uw2A
- active site: R13 (= R15), S109 (= S103), H110 (= H104), K119 (= K113), D243 (= D241), D245 (= D243), D247 (= D245), R248 (= R246), H330 (= H328)
- binding zinc ion: D243 (= D241), D245 (= D243), D247 (= D245)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
34% identity, 94% coverage: 7:444/464 of query aligns to 3:445/455 of 1wqaA
- active site: R11 (= R15), S101 (= S103), H102 (= H104), K111 (= K113), D243 (= D241), D245 (= D243), D247 (= D245), R248 (= R246), G330 (≠ H328), R340 (≠ F338)
- binding magnesium ion: S101 (= S103), D243 (= D241), D245 (= D243), D247 (= D245)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
35% identity, 94% coverage: 9:443/464 of query aligns to 6:439/448 of 6nqhA
- active site: R12 (= R15), S97 (= S103), H98 (= H104), K107 (= K113), D237 (= D241), D239 (= D243), D241 (= D245), R242 (= R246), H324 (= H328)
- binding magnesium ion: D237 (= D241), D239 (= D243), D241 (= D245)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R15), S97 (= S103), H98 (= H104), K107 (= K113), D239 (= D243), R242 (= R246), R280 (≠ K284), S301 (≠ T305), G302 (= G306), E320 (= E324), S322 (= S326), H324 (= H328), R414 (= R418), S416 (= S420), N417 (= N421), T418 (= T422), R423 (≠ V427)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
35% identity, 94% coverage: 9:443/464 of query aligns to 6:439/448 of 6np8A
- active site: R12 (= R15), S97 (= S103), H98 (= H104), K107 (= K113), D237 (= D241), D239 (= D243), D241 (= D245), R242 (= R246), H324 (= H328)
- binding calcium ion: S97 (= S103), D237 (= D241), D239 (= D243), D241 (= D245)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y12), R280 (≠ K284), G302 (= G306), H303 (= H307), E320 (= E324), S322 (= S326), H324 (= H328), R414 (= R418), S416 (= S420), N417 (= N421), T418 (= T422), R423 (≠ V427)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
35% identity, 94% coverage: 9:443/464 of query aligns to 6:439/448 of 6nolA
- active site: R12 (= R15), S97 (= S103), H98 (= H104), K107 (= K113), D237 (= D241), D239 (= D243), D241 (= D245), R242 (= R246), H324 (= H328)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G306), E320 (= E324), S322 (= S326), H324 (= H328), R414 (= R418), S416 (= S420), N417 (= N421), T418 (= T422), R423 (≠ V427)
- binding magnesium ion: S97 (= S103), D237 (= D241), D239 (= D243), D241 (= D245)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
35% identity, 94% coverage: 9:443/464 of query aligns to 6:439/448 of 6nnpA
- active site: R12 (= R15), S97 (= S103), H98 (= H104), K107 (= K113), D237 (= D241), D239 (= D243), D241 (= D245), R242 (= R246), H324 (= H328)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ K284), G302 (= G306), H303 (= H307), E320 (= E324), H324 (= H328), R414 (= R418), S416 (= S420), N417 (= N421), T418 (= T422), R423 (≠ V427)
- binding magnesium ion: S97 (= S103), D237 (= D241), D239 (= D243), D241 (= D245)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
35% identity, 94% coverage: 9:443/464 of query aligns to 6:439/448 of 6nn2A
- active site: R12 (= R15), S97 (= S103), H98 (= H104), K107 (= K113), D237 (= D241), D239 (= D243), D241 (= D245), R242 (= R246), H324 (= H328)
- binding calcium ion: S97 (= S103), D237 (= D241), D239 (= D243), D241 (= D245)
6n1eA Crystal structure of x. Citri phosphoglucomutase in complex with 1- methyl-glucose 6-phosphate (see paper)
35% identity, 94% coverage: 9:443/464 of query aligns to 6:439/448 of 6n1eA
Query Sequence
>8501959 DvMF_2673 Phosphomannomutase (RefSeq)
MKPISDRPFRAYDIRGIVDADFDAEWVERLGRACGTYLLERGIGAAVVGHDCRHSSPAYH
DALTAGLIACGIDVVSVGMVPTPLLYFAVRHLERQGGIMITASHNPPEYNGFKVWAGQTT
IHTTEIRRIYEIFAAGRFASGKGVGCTMDIVPAYMEAVTQRVQLAPRARGPLKVVVDGGN
GAGGDICADLLRRLGADVIEQYCDPDGAFPNHHPDPVVEANMRDLIARVASEGADLGIGL
DGDADRLGAVDAQGRLLFGDELLSLFARDLLARVPGGEVMADVKCSHRLFRDIEAHGGKP
TMWITGHSVMKARMLEVNAPLAGEMSGHMFFNEGWYGFDDAIYAAALLLRILSASDVPLT
ALPGWPPSHATPELHMPCPDELKFAVVSRAQEHFRALYDVNEIDGARITWPDGWALVRAS
NTQPVLVLRFEAETPERLAEIRTLVETPLAAWIAEARAARDATA
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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