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Comparing SM_b21081 FitnessBrowser__Smeli:SM_b21081 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)
33% identity, 90% coverage: 28:492/515 of query aligns to 6:443/463 of P26276
- R15 (= R37) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y39) binding ; binding
- R20 (= R42) mutation to A: No phosphoglucomutase activity.
- S108 (= S138) 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 (= N140) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D275) binding
- D244 (= D277) binding
- D246 (= D279) binding
- R247 (= R280) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ K295) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (= K318) binding
- H308 (= H343) binding ; binding
- E325 (= E360) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ EKSGH 360:364) binding ; binding
- H329 (= H364) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P405) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R470) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RASSN 470:474) 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)
33% identity, 90% coverage: 28:492/515 of query aligns to 6:443/463 of Q02E40
- S108 (= S138) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
33% identity, 90% coverage: 28:492/515 of query aligns to 1:438/458 of 1pcjX
- active site: R15 (= R42), S103 (= S138), H104 (= H139), K113 (= K148), D237 (= D275), D239 (= D277), D241 (= D279), R242 (= R280), H324 (= H364), D335 (= D376)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (= Y39), S103 (= S138), T301 (= T341), G302 (= G342), E320 (= E360), S322 (= S362), H324 (= H364), R416 (= R470), S418 (= S472), N419 (≠ S473), T420 (≠ N474)
- binding zinc ion: S103 (= S138), D237 (= D275), D239 (= D277), D241 (= D279)
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
33% identity, 90% coverage: 28:492/515 of query aligns to 2:439/459 of 1k2yX
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
33% identity, 89% coverage: 33:492/515 of query aligns to 3:435/455 of 2h5aX
- active site: H101 (= H139), D234 (= D275), D236 (= D277), D238 (= D279), R239 (= R280), D332 (= D376)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y39), T298 (= T341), G299 (= G342), H300 (= H343), E317 (= E360), S319 (= S362), H321 (= H364), R413 (= R470), S415 (= S472), N416 (≠ S473), T417 (≠ N474)
- binding zinc ion: S100 (= S138), D234 (= D275), D236 (= D277), D238 (= D279)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
33% identity, 89% coverage: 33:492/515 of query aligns to 3:435/455 of 2h4lX
- active site: H101 (= H139), D234 (= D275), D236 (= D277), D238 (= D279), R239 (= R280), D332 (= D376)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y39), R12 (= R42), S100 (= S138), T298 (= T341), E317 (= E360), R413 (= R470), S415 (= S472), N416 (≠ S473), T417 (≠ N474)
- binding zinc ion: S100 (= S138), D234 (= D275), D236 (= D277), D238 (= D279)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
33% identity, 89% coverage: 33:492/515 of query aligns to 3:435/455 of 2fkfA
- active site: R12 (= R42), S100 (= S138), H101 (= H139), K110 (= K148), D234 (= D275), D236 (= D277), D238 (= D279), R239 (= R280), H321 (= H364), D332 (= D376)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (= R37), H101 (= H139), S319 (= S362), R413 (= R470), S415 (= S472), N416 (≠ S473), T417 (≠ N474)
- binding zinc ion: S100 (= S138), D234 (= D275), D236 (= D277), D238 (= D279)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
33% identity, 89% coverage: 33:492/515 of query aligns to 3:435/455 of 1pcmX
- active site: R12 (= R42), S100 (= S138), H101 (= H139), K110 (= K148), D234 (= D275), D236 (= D277), D238 (= D279), R239 (= R280), H321 (= H364), D332 (= D376)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y39), S100 (= S138), T298 (= T341), G299 (= G342), H300 (= H343), E317 (= E360), S319 (= S362), H321 (= H364), R413 (= R470), S415 (= S472)
- binding zinc ion: S100 (= S138), D234 (= D275), D236 (= D277), D238 (= D279)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
33% identity, 89% coverage: 33:492/515 of query aligns to 3:435/455 of 1p5gX
- active site: R12 (= R42), S100 (= S138), H101 (= H139), K110 (= K148), D234 (= D275), D236 (= D277), D238 (= D279), R239 (= R280), H321 (= H364), D332 (= D376)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y39), S100 (= S138), K277 (= K318), G299 (= G342), H300 (= H343), E317 (= E360), S319 (= S362), H321 (= H364), R413 (= R470), S415 (= S472), N416 (≠ S473), T417 (≠ N474)
- binding zinc ion: S100 (= S138), D234 (= D275), D236 (= D277), D238 (= D279)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
33% identity, 89% coverage: 33:492/515 of query aligns to 3:435/455 of 1p5dX
- active site: R12 (= R42), S100 (= S138), H101 (= H139), K110 (= K148), D234 (= D275), D236 (= D277), D238 (= D279), R239 (= R280), H321 (= H364), D332 (= D376)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (= Y39), S100 (= S138), R239 (= R280), T298 (= T341), G299 (= G342), H300 (= H343), E317 (= E360), S319 (= S362), H321 (= H364), R413 (= R470), S415 (= S472), T417 (≠ N474)
- binding zinc ion: S100 (= S138), D234 (= D275), D236 (= D277), D238 (= D279)
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
33% identity, 90% coverage: 28:492/515 of query aligns to 2:439/459 of 4il8A
- active site: R16 (= R42), S104 (= S138), H105 (= H139), K114 (= K148), D238 (= D275), D240 (= D277), D242 (= D279), R243 (= R280), A325 (≠ H364), D336 (= D376)
- binding magnesium ion: S104 (= S138), D238 (= D275), D240 (= D277), D242 (= D279)
3rsmA Crystal structure of s108c mutant of pmm/pgm (see paper)
33% identity, 89% coverage: 36:492/515 of query aligns to 3:416/436 of 3rsmA
- active site: C87 (≠ W144), K91 (= K148), D215 (= D275), D217 (= D277), D219 (= D279), R220 (= R280), H302 (= H364), D313 (= D376)
- binding phosphate ion: C87 (≠ W144), D215 (= D275), D217 (= D277), D219 (= D279), R220 (= R280)
- binding zinc ion: D215 (= D275), D217 (= D277), D219 (= D279)
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
32% identity, 90% coverage: 30:492/515 of query aligns to 1:438/458 of 3uw2A
- active site: R13 (= R42), S109 (= S138), H110 (= H139), K119 (= K148), D243 (= D275), D245 (= D277), D247 (= D279), R248 (= R280), H330 (= H364)
- binding zinc ion: D243 (= D275), D245 (= D277), D247 (= D279)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
29% identity, 84% coverage: 61:494/515 of query aligns to 23:443/455 of 1wqaA
- active site: S101 (= S138), H102 (= H139), K111 (= K148), D243 (= D275), D245 (= D277), D247 (= D279), R248 (= R280), G330 (= G363), R340 (= R373)
- binding magnesium ion: S101 (= S138), D243 (= D275), D245 (= D277), D247 (= D279)
Sites not aligning to the query:
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
29% identity, 91% coverage: 36:503/515 of query aligns to 6:447/448 of 6nqhA
- active site: R12 (= R42), S97 (= S138), H98 (= H139), K107 (= K148), D237 (= D275), D239 (= D277), D241 (= D279), R242 (= R280), H324 (= H364)
- binding magnesium ion: D237 (= D275), D239 (= D277), D241 (= D279)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R42), S97 (= S138), H98 (= H139), K107 (= K148), D239 (= D277), R242 (= R280), R280 (≠ K318), S301 (≠ T341), G302 (= G342), E320 (= E360), S322 (= S362), H324 (= H364), R414 (= R470), S416 (= S472), N417 (≠ S473), T418 (≠ N474), R423 (≠ V479)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
29% identity, 91% coverage: 36:503/515 of query aligns to 6:447/448 of 6np8A
- active site: R12 (= R42), S97 (= S138), H98 (= H139), K107 (= K148), D237 (= D275), D239 (= D277), D241 (= D279), R242 (= R280), H324 (= H364)
- binding calcium ion: S97 (= S138), D237 (= D275), D239 (= D277), D241 (= D279)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y39), R280 (≠ K318), G302 (= G342), H303 (= H343), E320 (= E360), S322 (= S362), H324 (= H364), R414 (= R470), S416 (= S472), N417 (≠ S473), T418 (≠ N474), R423 (≠ V479)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
29% identity, 91% coverage: 36:503/515 of query aligns to 6:447/448 of 6nolA
- active site: R12 (= R42), S97 (= S138), H98 (= H139), K107 (= K148), D237 (= D275), D239 (= D277), D241 (= D279), R242 (= R280), H324 (= H364)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G342), E320 (= E360), S322 (= S362), H324 (= H364), R414 (= R470), S416 (= S472), N417 (≠ S473), T418 (≠ N474), R423 (≠ V479)
- binding magnesium ion: S97 (= S138), D237 (= D275), D239 (= D277), D241 (= D279)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
29% identity, 91% coverage: 36:503/515 of query aligns to 6:447/448 of 6nnpA
- active site: R12 (= R42), S97 (= S138), H98 (= H139), K107 (= K148), D237 (= D275), D239 (= D277), D241 (= D279), R242 (= R280), H324 (= H364)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ K318), G302 (= G342), H303 (= H343), E320 (= E360), H324 (= H364), R414 (= R470), S416 (= S472), N417 (≠ S473), T418 (≠ N474), R423 (≠ V479)
- binding magnesium ion: S97 (= S138), D237 (= D275), D239 (= D277), D241 (= D279)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
29% identity, 91% coverage: 36:503/515 of query aligns to 6:447/448 of 6nn2A
- active site: R12 (= R42), S97 (= S138), H98 (= H139), K107 (= K148), D237 (= D275), D239 (= D277), D241 (= D279), R242 (= R280), H324 (= H364)
- binding calcium ion: S97 (= S138), D237 (= D275), D239 (= D277), D241 (= D279)
6n1eA Crystal structure of x. Citri phosphoglucomutase in complex with 1- methyl-glucose 6-phosphate (see paper)
29% identity, 91% coverage: 36:503/515 of query aligns to 6:447/448 of 6n1eA
Query Sequence
>SM_b21081 FitnessBrowser__Smeli:SM_b21081
MNFARFEPASANGPAQESGPEKFTYETSPLIRATGFREYDARWWFGRSDCGKAPELNLMG
AQALGMGLGTFIQRSGAGPEIVTGHDFRSYSLGIKLALVCGLMAAGARVRDIGLALSPMA
YFAQFALDVPSVAMVTASHNENGWTGVKMGMARPLTFGPQEMAELRRIVLEADFDLTGGG
AYEFVPDFRRRYIDDLTRGRRIGRKLKVVAACGNGTAGAFAPDVLQRIGCEVIPLDCDLD
HSFPRYNPNPEDLKMLHAIRDKVLESGADVGLGFDGDGDRCGVVDNEGSEIFADKIGVML
ARDISASNPGSVFVVDVKSTGLFASDPVLKANGARTDYWKTGHSYIKRRVAELGAIAGFE
KSGHFFFNAPLGRGYDDGLITAISICEMLDRSPNRSIAEIYRALPMTWSSPTMSPHCADE
VKYAVAERVVERFRAMQRDGVPVAGQMIADLVTVNGVRVVTEDGTWGLVRASSNKPELVV
VVESPVSEARQRAMFEAVDCVLRENPEVGAYNQTI
Or try a new SitesBLAST search
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