SitesBLAST
Comparing WP_012470571.1 NCBI__GCF_000020385.1:WP_012470571.1 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)
7omlA Bacillus subtilis phosphoglucomutase glmm (metal bound) (see paper)
50% identity, 99% coverage: 3:450/452 of query aligns to 2:445/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
50% identity, 99% coverage: 3:450/452 of query aligns to 2:445/445 of 7ojrA
P31120 Phosphoglucosamine mutase; EC 5.4.2.10 from Escherichia coli (strain K12) (see 3 papers)
51% identity, 98% coverage: 2:446/452 of query aligns to 4:443/445 of P31120
- S100 (= S100) mutation to A: 2% of wild-type activity.; mutation to T: 20-fold increase in the non-specific phosphoglucomutase activity towards glucose-phosphate substrates (non aminated).
- S102 (= S102) active site, Phosphoserine intermediate; modified: Phosphoserine; by autocatalysis; mutation to A: Loss of activity in the absence or presence of glucosamine-1,6-diP.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3i3wA Structure of a phosphoglucosamine mutase from francisella tularensis
40% identity, 99% coverage: 3:449/452 of query aligns to 1:440/441 of 3i3wA
- active site: R9 (= R11), S99 (= S102), H100 (= H103), K109 (= K112), D237 (= D244), D239 (= D246), D241 (= D248), R242 (= R249), H324 (= H333)
- binding zinc ion: S99 (= S102), D237 (= D244), D239 (= D246), D241 (= D248)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
34% identity, 97% coverage: 1:439/452 of query aligns to 1:444/455 of 1wqaA
- active site: R11 (= R11), S101 (= S102), H102 (= H103), K111 (= K112), D243 (= D244), D245 (= D246), D247 (= D248), R248 (= R249), G330 (≠ H333), R340 (≠ G343)
- binding magnesium ion: S101 (= S102), D243 (= D244), D245 (= D246), D247 (= D248)
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
27% identity, 99% coverage: 3:449/452 of query aligns to 7:447/458 of 1pcjX
- active site: R15 (= R11), S103 (= S102), H104 (= H103), K113 (= K112), D237 (= D244), D239 (= D246), D241 (= D248), R242 (= R249), H324 (= H333), D335 (≠ G343)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (≠ D8), S103 (= S102), T301 (≠ V310), G302 (= G311), E320 (= E329), S322 (= S331), H324 (= H333), R416 (= R414), S418 (= S416), N419 (≠ G417), T420 (= T418)
- binding zinc ion: S103 (= S102), D237 (= D244), D239 (= D246), D241 (= D248)
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)
27% identity, 99% coverage: 3:449/452 of query aligns to 12:452/463 of P26276
- R15 (≠ G6) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (≠ D8) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- R20 (= R11) mutation to A: No phosphoglucomutase activity.
- S108 (= S102) 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 (= N104) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D244) binding Mg(2+)
- D244 (= D246) binding Mg(2+)
- D246 (= D248) binding Mg(2+)
- R247 (= R249) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Q264) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ M289) binding alpha-D-glucose 1-phosphate
- H308 (≠ D312) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- E325 (= E329) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ EQSGH 329:333) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- H329 (= H333) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (vs. gap) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R414) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RYSGT 414:418) 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)
27% identity, 99% coverage: 3:449/452 of query aligns to 12:452/463 of Q02E40
- S108 (= S102) active site, Non-phosphorylated intermediate; modified: Phosphoserine
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
27% identity, 99% coverage: 3:449/452 of query aligns to 4:444/455 of 2h5aX
- active site: H101 (= H103), D234 (= D244), D236 (= D246), D238 (= D248), R239 (= R249), D332 (≠ G343)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (≠ D8), T298 (≠ V310), G299 (= G311), H300 (≠ D312), E317 (= E329), S319 (= S331), H321 (= H333), R413 (= R414), S415 (= S416), N416 (≠ G417), T417 (= T418)
- binding zinc ion: S100 (= S102), D234 (= D244), D236 (= D246), D238 (= D248)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
27% identity, 99% coverage: 3:449/452 of query aligns to 4:444/455 of 2h4lX