SitesBLAST
Comparing BWI76_RS25130 BWI76_RS25130 phosphoglucosamine mutase 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)
P31120 Phosphoglucosamine mutase; EC 5.4.2.10 from Escherichia coli (strain K12) (see 3 papers)
92% identity, 100% coverage: 1:445/445 of query aligns to 1:445/445 of P31120
- M1 (= M1) modified: Initiator methionine, Removed
- 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.
7omlA Bacillus subtilis phosphoglucomutase glmm (metal bound) (see paper)
46% identity, 99% coverage: 5:444/445 of query aligns to 2:442/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
46% identity, 99% coverage: 5:444/445 of query aligns to 2:442/445 of 7ojrA
3i3wA Structure of a phosphoglucosamine mutase from francisella tularensis
43% identity, 99% coverage: 5:443/445 of query aligns to 1:437/441 of 3i3wA
- active site: R9 (= R13), S99 (= S102), H100 (= H103), K109 (= K112), D237 (= D241), D239 (= D243), D241 (= D245), R242 (= R246), H324 (= H329)
- binding zinc ion: S99 (= S102), D237 (= D241), D239 (= D243), D241 (= D245)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
34% identity, 97% coverage: 5:434/445 of query aligns to 3:442/455 of 1wqaA
- active site: R11 (= R13), S101 (= S102), H102 (= H103), K111 (= K112), D243 (= D241), D245 (= D243), D247 (= D245), R248 (= R246), G330 (≠ H329), R340 (≠ G339)
- binding magnesium ion: S101 (= S102), D243 (= D241), D245 (= D243), D247 (= D245)
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, 98% coverage: 12:445/445 of query aligns to 19:455/463 of P26276
- R20 (= R13) 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 (= D241) binding
- D244 (= D243) binding
- D246 (= D245) binding
- R247 (= R246) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Q261) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ L284) binding
- H308 (≠ D308) binding ; binding
- E325 (= E325) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ ENSGH 325:329) binding ; binding
- H329 (= H329) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P370) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R411) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RKSGT 411:415) binding ; binding
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 ; binding
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, 98% coverage: 12:445/445 of query aligns to 19:455/463 of Q02E40
- S108 (= S102) active site, Non-phosphorylated intermediate; modified: Phosphoserine
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
28% identity, 98% coverage: 12:445/445 of query aligns to 11:447/455 of 2h5aX
- active site: H101 (= H103), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), D332 (≠ G339)
- binding 1-O-phosphono-alpha-D-xylopyranose: T298 (≠ V306), G299 (= G307), H300 (≠ D308), E317 (= E325), S319 (= S327), H321 (= H329), R413 (= R411), S415 (= S413), N416 (≠ G414), T417 (= T415)
- binding zinc ion: S100 (= S102), D234 (= D241), D236 (= D243), D238 (= D245)
Sites not aligning to the query:
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
28% identity, 98% coverage: 12:445/445 of query aligns to 11:447/455 of 2h4lX
- active site: H101 (= H103), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), D332 (≠ G339)
- binding 1-O-phosphono-alpha-D-ribofuranose: R12 (= R13), S100 (= S102), K277 (≠ L284), T298 (≠ V306), G299 (= G307), E317 (= E325), S319 (= S327), R413 (= R411), S415 (= S413), N416 (≠ G414), T417 (= T415)
- binding zinc ion: S100 (= S102), D234 (= D241), D236 (= D243), D238 (= D245)
Sites not aligning to the query:
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
28% identity, 98% coverage: 12:445/445 of query aligns to 11:447/455 of 2fkfA
- active site: R12 (= R13), S100 (= S102), H101 (= H103), K110 (= K112), D234 (= D241), D236 (= D243), D238 (= D245), R239 (= R246), H321 (= H329), D332 (≠ G339)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R12 (= R13), H101 (= H103), N102 (= N104), S319 (= S327), R413 (= R411), S415 (= S413), N416 (≠ G414), T417 (= T415)
- binding zinc ion: S100 (= S102), D234 (= D241), D236 (= D243), D238 (= D245)
Sites not aligning to the query:
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
28% identity, 98% coverage: 12:445/445 of query aligns to 11:447/455 of 1pcmX