SitesBLAST
Comparing WP_007691377.1 NCBI__GCF_000336675.1:WP_007691377.1 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)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
44% identity, 99% coverage: 2:452/454 of query aligns to 3:455/455 of 1wqaA
- active site: R11 (= R10), S101 (= S94), H102 (= H95), K111 (= K104), D243 (= D237), D245 (= D239), D247 (= D241), R248 (= R242), G330 (= G327), R340 (= R337)
- binding magnesium ion: S101 (= S94), D243 (= D237), D245 (= D239), D247 (= D241)
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
30% identity, 98% coverage: 3:448/454 of query aligns to 9:449/459 of 4il8A
- active site: R16 (= R10), S104 (= S94), H105 (= H95), K114 (= K104), D238 (= D237), D240 (= D239), D242 (= D241), R243 (= R242), A325 (≠ G327), D336 (vs. gap)
- binding magnesium ion: S104 (= S94), D238 (= D237), D240 (= D239), D242 (= D241)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
30% identity, 98% coverage: 3:448/454 of query aligns to 5:445/455 of 2h5aX
- active site: H101 (= H95), D234 (= D237), D236 (= D239), D238 (= D241), R239 (= R242), D332 (vs. gap)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (≠ S7), T298 (≠ V299), G299 (= G300), H300 (≠ S301), E317 (= E323), S319 (≠ N325), H321 (≠ G327), R413 (= R416), S415 (= S418), N416 (≠ G419), T417 (= T420)
- binding zinc ion: S100 (= S94), D234 (= D237), D236 (= D239), D238 (= D241)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
30% identity, 98% coverage: 3:448/454 of query aligns to 5:445/455 of 2h4lX
- active site: H101 (= H95), D234 (= D237), D236 (= D239), D238 (= D241), R239 (= R242), D332 (vs. gap)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (≠ S7), R12 (= R10), S100 (= S94), T298 (≠ V299), E317 (= E323), R413 (= R416), S415 (= S418), N416 (≠ G419), T417 (= T420)
- binding zinc ion: S100 (= S94), D234 (= D237), D236 (= D239), D238 (= D241)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
30% identity, 98% coverage: 3:448/454 of query aligns to 5:445/455 of 2fkfA
- active site: R12 (= R10), S100 (= S94), H101 (= H95), K110 (= K104), D234 (= D237), D236 (= D239), D238 (= D241), R239 (= R242), H321 (≠ G327), D332 (vs. gap)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (≠ G5), H101 (= H95), S319 (≠ N325), R413 (= R416), S415 (= S418), N416 (≠ G419), T417 (= T420)
- binding zinc ion: S100 (= S94), D234 (= D237), D236 (= D239), D238 (= D241)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
30% identity, 98% coverage: 3:448/454 of query aligns to 5:445/455 of 1pcmX
- active site: R12 (= R10), S100 (= S94), H101 (= H95), K110 (= K104), D234 (= D237), D236 (= D239), D238 (= D241), R239 (= R242), H321 (≠ G327), D332 (vs. gap)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (≠ S7), S100 (= S94), T298 (≠ V299), G299 (= G300), H300 (≠ S301), E317 (= E323), S319 (≠ N325), H321 (≠ G327), R413 (= R416), S415 (= S418)
- binding zinc ion: S100 (= S94), D234 (= D237), D236 (= D239), D238 (= D241)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
30% identity, 98% coverage: 3:448/454 of query aligns to 5:445/455 of 1p5gX
- active site: R12 (= R10), S100 (= S94), H101 (= H95), K110 (= K104), D234 (= D237), D236 (= D239), D238 (= D241), R239 (= R242), H321 (≠ G327), D332 (vs. gap)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (≠ S7), S100 (= S94), K277 (≠ T278), G299 (= G300), H300 (≠ S301), E317 (= E323), S319 (≠ N325), H321 (≠ G327), R413 (= R416), S415 (= S418), N416 (≠ G419), T417 (= T420)
- binding zinc ion: S100 (= S94), D234 (= D237), D236 (= D239), D238 (= D241)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
30% identity, 98% coverage: 3:448/454 of query aligns to 5:445/455 of 1p5dX
- active site: R12 (= R10), S100 (= S94), H101 (= H95), K110 (= K104), D234 (= D237), D236 (= D239), D238 (= D241), R239 (= R242), H321 (≠ G327), D332 (vs. gap)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (≠ S7), S100 (= S94), R239 (= R242), T298 (≠ V299), G299 (= G300), H300 (≠ S301), E317 (= E323), S319 (≠ N325), H321 (≠ G327), R413 (= R416), S415 (= S418), T417 (= T420)
- binding zinc ion: S100 (= S94), D234 (= D237), D236 (= D239), D238 (= D241)
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)
30% identity, 98% coverage: 3:448/454 of query aligns to 13:453/463 of P26276
- R15 (≠ G5) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (≠ S7) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- R20 (= R10) mutation to A: No phosphoglucomutase activity.
- S108 (= S94) 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 (= N96) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D237) binding Mg(2+)
- D244 (= D239) binding Mg(2+)
- D246 (= D241) binding Mg(2+)
- R247 (= R242) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ A257) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ T278) binding alpha-D-glucose 1-phosphate
- H308 (≠ S301) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- E325 (= E323) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ EGNGG 323:327) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- H329 (≠ G327) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (≠ I359) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R416) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RESGT 416:420) 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)
30% identity, 98% coverage: 3:448/454 of query aligns to 13:453/463 of Q02E40