SitesBLAST
Comparing Dsui_3344 FitnessBrowser__PS:Dsui_3344 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)
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
66% identity, 97% coverage: 13:464/464 of query aligns to 5:458/458 of 3uw2A
- active site: R13 (= R21), S109 (= S109), H110 (= H110), K119 (= K119), D243 (= D243), D245 (= D245), D247 (= D247), R248 (= R248), H330 (= H330)
- binding zinc ion: D243 (= D243), D245 (= D245), D247 (= D247)
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)
57% identity, 100% coverage: 3:464/464 of query aligns to 2:463/463 of P26276
- R15 (≠ K16) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y18) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- R20 (= R21) mutation to A: No phosphoglucomutase activity.
- S108 (= S109) 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 (= N111) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D243) binding Mg(2+)
- D244 (= D245) binding Mg(2+)
- D246 (= D247) binding Mg(2+)
- R247 (= R248) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (= R263) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (= K286) binding alpha-D-glucose 1-phosphate
- H308 (= H309) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- E325 (= E326) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (= EMSGH 326:330) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- H329 (= H330) 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 (= R422) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RPSNT 422:426) 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)
57% identity, 100% coverage: 3:464/464 of query aligns to 2:463/463 of Q02E40
- S108 (= S109) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
57% identity, 98% coverage: 8:464/464 of query aligns to 2:458/458 of 1pcjX
- active site: R15 (= R21), S103 (= S109), H104 (= H110), K113 (= K119), D237 (= D243), D239 (= D245), D241 (= D247), R242 (= R248), H324 (= H330), D335 (= D341)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (= Y18), S103 (= S109), T301 (= T307), G302 (= G308), E320 (= E326), S322 (= S328), H324 (= H330), R416 (= R422), S418 (= S424), N419 (= N425), T420 (= T426)
- binding zinc ion: S103 (= S109), D237 (= D243), D239 (= D245), D241 (= D247)
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
57% identity, 98% coverage: 8:464/464 of query aligns to 3:459/459 of 1k2yX
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
57% identity, 98% coverage: 10:464/464 of query aligns to 1:455/455 of 2h5aX
- active site: H101 (= H110), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), D332 (= D341)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y18), T298 (= T307), G299 (= G308), H300 (= H309), E317 (= E326), S319 (= S328), H321 (= H330), R413 (= R422), S415 (= S424), N416 (= N425), T417 (= T426)
- binding zinc ion: S100 (= S109), D234 (= D243), D236 (= D245), D238 (= D247)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
57% identity, 98% coverage: 10:464/464 of query aligns to 1:455/455 of 2h4lX
- active site: H101 (= H110), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), D332 (= D341)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y18), R12 (= R21), S100 (= S109), T298 (= T307), E317 (= E326), R413 (= R422), S415 (= S424), N416 (= N425), T417 (= T426)
- binding zinc ion: S100 (= S109), D234 (= D243), D236 (= D245), D238 (= D247)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
57% identity, 98% coverage: 10:464/464 of query aligns to 1:455/455 of 2fkfA
- active site: R12 (= R21), S100 (= S109), H101 (= H110), K110 (= K119), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), H321 (= H330), D332 (= D341)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (≠ K16), H101 (= H110), S319 (= S328), R413 (= R422), S415 (= S424), N416 (= N425), T417 (= T426)
- binding zinc ion: S100 (= S109), D234 (= D243), D236 (= D245), D238 (= D247)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
57% identity, 98% coverage: 10:464/464 of query aligns to 1:455/455 of 1pcmX
- active site: R12 (= R21), S100 (= S109), H101 (= H110), K110 (= K119), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), H321 (= H330), D332 (= D341)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y18), S100 (= S109), T298 (= T307), G299 (= G308), H300 (= H309), E317 (= E326), S319 (= S328), H321 (= H330), R413 (= R422), S415 (= S424)
- binding zinc ion: S100 (= S109), D234 (= D243), D236 (= D245), D238 (= D247)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
57% identity, 98% coverage: 10:464/464 of query aligns to 1:455/455 of 1p5gX
- active site: R12 (= R21), S100 (= S109), H101 (= H110), K110 (= K119), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), H321 (= H330), D332 (= D341)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y18), S100 (= S109), K277 (= K286), G299 (= G308), H300 (= H309), E317 (= E326), S319 (= S328), H321 (= H330), R413 (= R422), S415 (= S424), N416 (= N425), T417 (= T426)
- binding zinc ion: S100 (= S109), D234 (= D243), D236 (= D245), D238 (= D247)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
57% identity, 98% coverage: 10:464/464 of query aligns to 1:455/455 of 1p5dX
- active site: R12 (= R21), S100 (= S109), H101 (= H110), K110 (= K119), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), H321 (= H330), D332 (= D341)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (= Y18), S100 (= S109), R239 (= R248), T298 (= T307), G299 (= G308), H300 (= H309), E317 (= E326), S319 (= S328), H321 (= H330), R413 (= R422), S415 (= S424), T417 (= T426)
- binding zinc ion: S100 (= S109), D234 (= D243), D236 (= D245), D238 (= D247)
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
57% identity, 98% coverage: 8:464/464 of query aligns to 3:459/459 of 4il8A
- active site: R16 (= R21), S104 (= S109), H105 (= H110), K114 (= K119), D238 (= D243), D240 (= D245), D242 (= D247), R243 (= R248), A325 (≠ H330), D336 (= D341)
- binding magnesium ion: S104 (= S109), D238 (= D243), D240 (= D245), D242 (= D247)
3rsmA Crystal structure of s108c mutant of pmm/pgm (see paper)
55% identity, 95% coverage: 26:464/464 of query aligns to 4:436/436 of 3rsmA
- active site: C87 (≠ S109), K91 (= K119), D215 (= D243), D217 (= D245), D219 (= D247), R220 (= R248), H302 (= H330), D313 (= D341)
- binding phosphate ion: C87 (≠ S109), D215 (= D243), D217 (= D245), D219 (= D247), R220 (= R248)
- binding zinc ion: D215 (= D243), D217 (= D245), D219 (= D247)
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
34% identity, 92% coverage: 15:442/464 of query aligns to 7:435/449 of 6mlwA
- active site: R13 (= R21), S98 (= S109), H99 (= H110), K108 (= K119), D238 (= D243), D240 (= D245), D242 (= D247), R243 (= R248), H325 (= H330)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G308), H304 (= H309), E321 (= E326), S323 (= S328), H325 (= H330), R415 (= R422), S417 (= S424), N418 (= N425), T419 (= T426), R424 (≠ V431)
- binding magnesium ion: S98 (= S109), D238 (= D243), D240 (= D245), D242 (= D247)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
34% identity, 92% coverage: 15:442/464 of query aligns to 7:435/449 of 5bmpA
- active site: R13 (= R21), S98 (= S109), H99 (= H110), K108 (= K119), D238 (= D243), D240 (= D245), D242 (= D247), R243 (= R248), H325 (= H330)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ K286), G303 (= G308), E321 (= E326), S323 (= S328), H325 (= H330), R415 (= R422), S417 (= S424), N418 (= N425), T419 (= T426), R424 (≠ V431)
- binding magnesium ion: S98 (= S109), D238 (= D243), D240 (= D245), D242 (= D247)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
34% identity, 92% coverage: 15:442/464 of query aligns to 6:434/448 of 6nqhA
- active site: R12 (= R21), S97 (= S109), H98 (= H110), K107 (= K119), D237 (= D243), D239 (= D245), D241 (= D247), R242 (= R248), H324 (= H330)
- binding magnesium ion: D237 (= D243), D239 (= D245), D241 (= D247)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R21), S97 (= S109), H98 (= H110), K107 (= K119), D239 (= D245), R242 (= R248), R280 (≠ K286), S301 (≠ T307), G302 (= G308), E320 (= E326), S322 (= S328), H324 (= H330), R414 (= R422), S416 (= S424), N417 (= N425), T418 (= T426), R423 (≠ V431)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
34% identity, 92% coverage: 15:442/464 of query aligns to 6:434/448 of 6np8A
- active site: R12 (= R21), S97 (= S109), H98 (= H110), K107 (= K119), D237 (= D243), D239 (= D245), D241 (= D247), R242 (= R248), H324 (= H330)
- binding calcium ion: S97 (= S109), D237 (= D243), D239 (= D245), D241 (= D247)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y18), R280 (≠ K286), G302 (= G308), H303 (= H309), E320 (= E326), S322 (= S328), H324 (= H330), R414 (= R422), S416 (= S424), N417 (= N425), T418 (= T426), R423 (≠ V431)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
34% identity, 92% coverage: 15:442/464 of query aligns to 6:434/448 of 6nolA
- active site: R12 (= R21), S97 (= S109), H98 (= H110), K107 (= K119), D237 (= D243), D239 (= D245), D241 (= D247), R242 (= R248), H324 (= H330)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G308), E320 (= E326), S322 (= S328), H324 (= H330), R414 (= R422), S416 (= S424), N417 (= N425), T418 (= T426), R423 (≠ V431)
- binding magnesium ion: S97 (= S109), D237 (= D243), D239 (= D245), D241 (= D247)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
34% identity, 92% coverage: 15:442/464 of query aligns to 6:434/448 of 6nnpA
- active site: R12 (= R21), S97 (= S109), H98 (= H110), K107 (= K119), D237 (= D243), D239 (= D245), D241 (= D247), R242 (= R248), H324 (= H330)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ K286), G302 (= G308), H303 (= H309), E320 (= E326), H324 (= H330), R414 (= R422), S416 (= S424), N417 (= N425), T418 (= T426), R423 (≠ V431)
- binding magnesium ion: S97 (= S109), D237 (= D243), D239 (= D245), D241 (= D247)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
34% identity, 92% coverage: 15:442/464 of query aligns to 6:434/448 of 6nn2A
- active site: R12 (= R21), S97 (= S109), H98 (= H110), K107 (= K119), D237 (= D243), D239 (= D245), D241 (= D247), R242 (= R248), H324 (= H330)
- binding calcium ion: S97 (= S109), D237 (= D243), D239 (= D245), D241 (= D247)
Query Sequence
>Dsui_3344 FitnessBrowser__PS:Dsui_3344
MNASVQIPALPPEIFKAYDIRGIVGKSLTADVVRAIGHGLGSLARERQQTAIAIGRDGRL
SGPELAGALADGIRAAGVDVIDIGCVPTPVTYFAAHHLGCHSCVSVTGSHNPPDYNGLKM
VIGGETLAGEAIQALKRRIEAGDLARGEGKLTQADVKAAYVERILADVKLARPMKIVMDC
GNGVAGAVAPELFKKLGCDIVPLFCEVDGTFPNHHPDPSKPENLADVIRALKETDAEIGI
AFDGDGDRLGVVTKDGEVIFPDRQLMLFAADVLSRVPGGEIVYDVKCTRLLAPWIREHGG
KPVMWQTGHALIKKKLKESGAPLAGEMSGHVFFKERWFGFDDGLYTGARLLEILARAADA
NPVLKGLPNATSTPELNIKMAEGEPFALLDKLKAGAKFEAAREIITIDGLRVEYADGFGL
ARPSNTTPVVVLRFEADNAEALARIQADFRRELAAAWPGLTLPF
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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