SitesBLAST
Comparing WP_061533873.1 NCBI__GCF_001584165.1:WP_061533873.1 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)
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
67% identity, 99% coverage: 4:464/468 of query aligns to 2:458/458 of 3uw2A
- active site: R13 (= R15), S109 (= S103), H110 (= H104), K119 (= K113), 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)
55% identity, 99% coverage: 4:464/468 of query aligns to 9:463/463 of P26276
- R15 (≠ K10) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y12) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- 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 (= 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 (≠ RSSNT 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)
55% identity, 99% coverage: 4:464/468 of query aligns to 9:463/463 of Q02E40
- S108 (= S103) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
55% identity, 99% coverage: 4:464/468 of query aligns to 4:458/458 of 1pcjX
- active site: R15 (= R15), S103 (= S103), H104 (= H104), K113 (= K113), D237 (= D243), D239 (= D245), D241 (= D247), R242 (= R248), H324 (= H330), D335 (= D341)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (= Y12), S103 (= S103), T301 (= T307), G302 (= G308), E320 (= E326), S322 (= S328), H324 (= H330), R416 (= R422), S418 (= S424), N419 (= N425), T420 (= T426)
- binding zinc ion: S103 (= S103), D237 (= D243), D239 (= D245), D241 (= D247)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
55% identity, 99% coverage: 4:464/468 of query aligns to 1:455/455 of 2h5aX
- active site: H101 (= H104), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), D332 (= D341)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y12), T298 (= T307), G299 (= G308), H300 (= H309), E317 (= E326), S319 (= S328), H321 (= H330), R413 (= R422), S415 (= S424), N416 (= N425), T417 (= T426)
- binding zinc ion: S100 (= S103), D234 (= D243), D236 (= D245), D238 (= D247)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
55% identity, 99% coverage: 4:464/468 of query aligns to 1:455/455 of 2h4lX
- active site: H101 (= H104), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), D332 (= D341)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y12), R12 (= R15), S100 (= S103), T298 (= T307), E317 (= E326), R413 (= R422), S415 (= S424), N416 (= N425), T417 (= T426)
- binding zinc ion: S100 (= S103), D234 (= D243), D236 (= D245), D238 (= D247)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
55% identity, 99% coverage: 4:464/468 of query aligns to 1:455/455 of 2fkfA
- active site: R12 (= R15), S100 (= S103), H101 (= H104), K110 (= K113), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), H321 (= H330), D332 (= D341)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (≠ K10), H101 (= H104), S319 (= S328), R413 (= R422), S415 (= S424), N416 (= N425), T417 (= T426)
- binding zinc ion: S100 (= S103), D234 (= D243), D236 (= D245), D238 (= D247)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
55% identity, 99% coverage: 4:464/468 of query aligns to 1:455/455 of 1pcmX
- active site: R12 (= R15), S100 (= S103), H101 (= H104), K110 (= K113), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), H321 (= H330), D332 (= D341)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y12), S100 (= S103), T298 (= T307), G299 (= G308), H300 (= H309), E317 (= E326), S319 (= S328), H321 (= H330), R413 (= R422), S415 (= S424)
- binding zinc ion: S100 (= S103), D234 (= D243), D236 (= D245), D238 (= D247)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
55% identity, 99% coverage: 4:464/468 of query aligns to 1:455/455 of 1p5gX
- active site: R12 (= R15), S100 (= S103), H101 (= H104), K110 (= K113), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), H321 (= H330), D332 (= D341)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y12), S100 (= S103), K277 (= K286), G299 (= G308), H300 (= H309), E317 (= E326), S319 (= S328), H321 (= H330), R413 (= R422), S415 (= S424), N416 (= N425), T417 (= T426)
- binding zinc ion: S100 (= S103), D234 (= D243), D236 (= D245), D238 (= D247)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
55% identity, 99% coverage: 4:464/468 of query aligns to 1:455/455 of 1p5dX