SitesBLAST
Comparing WP_101447241.1 NCBI__GCF_002846395.1:WP_101447241.1 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+
37% identity, 95% coverage: 12:449/463 of query aligns to 6:444/455 of 1wqaA
- active site: R11 (vs. gap), S101 (= S104), H102 (= H105), K111 (= K114), D243 (= D249), D245 (= D251), D247 (= D253), R248 (= R254), G330 (= G335), R340 (= R345)
- binding magnesium ion: S101 (= S104), D243 (= D249), D245 (= D251), D247 (= D253)
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
28% identity, 97% coverage: 14:461/463 of query aligns to 15:454/459 of 4il8A
- active site: R16 (≠ G15), S104 (= S104), H105 (= H105), K114 (= K114), D238 (= D249), D240 (= D251), D242 (= D253), R243 (= R254), A325 (≠ G335), D336 (≠ R345)
- binding magnesium ion: S104 (= S104), D238 (= D249), D240 (= D251), D242 (= D253)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
28% identity, 97% coverage: 14:461/463 of query aligns to 11:450/455 of 2h5aX
- active site: H101 (= H105), D234 (= D249), D236 (= D251), D238 (= D253), R239 (= R254), D332 (≠ R345)
- binding 1-O-phosphono-alpha-D-xylopyranose: T298 (≠ V312), G299 (= G313), H300 (≠ E314), E317 (= E331), S319 (≠ N333), H321 (≠ G335), R413 (= R424), S415 (= S426), N416 (= N427), T417 (= T428)
- binding zinc ion: S100 (= S104), D234 (= D249), D236 (= D251), D238 (= D253)
Sites not aligning to the query:
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
28% identity, 97% coverage: 14:461/463 of query aligns to 11:450/455 of 2h4lX
- active site: H101 (= H105), D234 (= D249), D236 (= D251), D238 (= D253), R239 (= R254), D332 (≠ R345)
- binding 1-O-phosphono-alpha-D-ribofuranose: R12 (≠ G15), S100 (= S104), T298 (≠ V312), E317 (= E331), R413 (= R424), S415 (= S426), N416 (= N427), T417 (= T428)
- binding zinc ion: S100 (= S104), D234 (= D249), D236 (= D251), D238 (= D253)
Sites not aligning to the query:
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
28% identity, 97% coverage: 14:461/463 of query aligns to 11:450/455 of 2fkfA
- active site: R12 (≠ G15), S100 (= S104), H101 (= H105), K110 (= K114), D234 (= D249), D236 (= D251), D238 (= D253), R239 (= R254), H321 (≠ G335), D332 (≠ R345)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: H101 (= H105), S319 (≠ N333), R413 (= R424), S415 (= S426), N416 (= N427), T417 (= T428)
- binding zinc ion: S100 (= S104), D234 (= D249), D236 (= D251), D238 (= D253)
Sites not aligning to the query:
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
28% identity, 97% coverage: 14:461/463 of query aligns to 11:450/455 of 1pcmX
- active site: R12 (≠ G15), S100 (= S104), H101 (= H105), K110 (= K114), D234 (= D249), D236 (= D251), D238 (= D253), R239 (= R254), H321 (≠ G335), D332 (≠ R345)
- binding 6-O-phosphono-alpha-D-mannopyranose: S100 (= S104), T298 (≠ V312), G299 (= G313), H300 (≠ E314), E317 (= E331), S319 (≠ N333), H321 (≠ G335), R413 (= R424), S415 (= S426)
- binding zinc ion: S100 (= S104), D234 (= D249), D236 (= D251), D238 (= D253)
Sites not aligning to the query:
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
28% identity, 97% coverage: 14:461/463 of query aligns to 11:450/455 of 1p5gX
- active site: R12 (≠ G15), S100 (= S104), H101 (= H105), K110 (= K114), D234 (= D249), D236 (= D251), D238 (= D253), R239 (= R254), H321 (≠ G335), D332 (≠ R345)
- binding 6-O-phosphono-alpha-D-glucopyranose: S100 (= S104), K277 (≠ S291), G299 (= G313), H300 (≠ E314), E317 (= E331), S319 (≠ N333), H321 (≠ G335), R413 (= R424), S415 (= S426), N416 (= N427), T417 (= T428)
- binding zinc ion: S100 (= S104), D234 (= D249), D236 (= D251), D238 (= D253)
Sites not aligning to the query:
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
28% identity, 97% coverage: 14:461/463 of query aligns to 11:450/455 of 1p5dX
- active site: R12 (≠ G15), S100 (= S104), H101 (= H105), K110 (= K114), D234 (= D249), D236 (= D251), D238 (= D253), R239 (= R254), H321 (≠ G335), D332 (≠ R345)
- binding 1-O-phosphono-alpha-D-glucopyranose: S100 (= S104), R239 (= R254), T298 (≠ V312), G299 (= G313), H300 (≠ E314), E317 (= E331), S319 (≠ N333), H321 (≠ G335), R413 (= R424), S415 (= S426), T417 (= T428)
- binding zinc ion: S100 (= S104), D234 (= D249), D236 (= D251), D238 (= D253)
Sites not aligning to the query:
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)
28% identity, 97% coverage: 14:461/463 of query aligns to 19:458/463 of P26276
- R20 (≠ G15) mutation to A: No phosphoglucomutase activity.
- S108 (= S104) 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 (= N106) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D249) binding Mg(2+)
- D244 (= D251) binding Mg(2+)
- D246 (= D253) binding Mg(2+)
- R247 (= R254) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ E268) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ S291) binding alpha-D-glucose 1-phosphate
- H308 (≠ E314) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- E325 (= E331) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ EGNGG 331:335) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- H329 (≠ G335) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P373) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R424) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RKSNT 424:428) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 15 R→A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- 17 binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
Q02E40 Phosphomannomutase/phosphoglucomutase; PMM / PGM; EC 5.4.2.2; EC 5.4.2.8 from Pseudomonas aeruginosa (strain UCBPP-PA14) (see paper)
28% identity, 97% coverage: 14:461/463 of query aligns to 19:458/463 of Q02E40