SitesBLAST
Comparing WP_012035846.1 NCBI__GCF_000063445.1:WP_012035846.1 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+
38% identity, 98% coverage: 3:433/438 of query aligns to 4:454/455 of 1wqaA
- active site: R11 (= R10), S101 (= S91), H102 (= H92), K111 (= K101), D243 (= D228), D245 (= D230), D247 (= D232), R248 (= R233), G330 (≠ T309), R340 (≠ P319)
- binding magnesium ion: S101 (= S91), D243 (= D228), D245 (= D230), D247 (= D232)
7omlA Bacillus subtilis phosphoglucomutase glmm (metal bound) (see paper)
33% identity, 93% coverage: 4:412/438 of query aligns to 4:423/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
33% identity, 93% coverage: 4:412/438 of query aligns to 4:423/445 of 7ojrA
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
32% identity, 99% coverage: 2:435/438 of query aligns to 8:453/459 of 4il8A
- active site: R16 (= R10), S104 (= S91), H105 (= H92), K114 (= K101), D238 (= D228), D240 (= D230), D242 (= D232), R243 (= R233), A325 (≠ T309), D336 (≠ P319)
- binding magnesium ion: S104 (= S91), D238 (= D228), D240 (= D230), D242 (= D232)
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)
32% identity, 99% coverage: 2:435/438 of query aligns to 12:457/463 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 (= S91) 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 (= N93) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D228) binding Mg(2+)
- D244 (= D230) binding Mg(2+)
- D246 (= D232) binding Mg(2+)
- R247 (= R233) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ E248) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ R274) binding alpha-D-glucose 1-phosphate
- H308 (≠ D288) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- E325 (= E305) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ ETSGT 305:309) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- H329 (≠ T309) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P349) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R398) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RPSGT 398:402) 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)
32% identity, 99% coverage: 2:435/438 of query aligns to 12:457/463 of Q02E40
- S108 (= S91) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
32% identity, 99% coverage: 2:435/438 of query aligns to 7:452/458 of 1pcjX
- active site: R15 (= R10), S103 (= S91), H104 (= H92), K113 (= K101), D237 (= D228), D239 (= D230), D241 (= D232), R242 (= R233), H324 (≠ T309), D335 (≠ P319)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (≠ S7), S103 (= S91), T301 (≠ I286), G302 (= G287), E320 (= E305), S322 (= S307), H324 (≠ T309), R416 (= R398), S418 (= S400), N419 (≠ G401), T420 (= T402)
- binding zinc ion: S103 (= S91), D237 (= D228), D239 (= D230), D241 (= D232)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
32% identity, 99% coverage: 2:435/438 of query aligns to 4:449/455 of 2h5aX
- active site: H101 (= H92), D234 (= D228), D236 (= D230), D238 (= D232), R239 (= R233), D332 (≠ P319)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (≠ S7), T298 (≠ I286), G299 (= G287), H300 (≠ D288), E317 (= E305), S319 (= S307), H321 (≠ T309), R413 (= R398), S415 (= S400), N416 (≠ G401), T417 (= T402)
- binding zinc ion: S100 (= S91), D234 (= D228), D236 (= D230), D238 (= D232)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
32% identity, 99% coverage: 2:435/438 of query aligns to 4:449/455 of 2h4lX
- active site: H101 (= H92), D234 (= D228), D236 (= D230), D238 (= D232), R239 (= R233), D332 (≠ P319)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (≠ S7), R12 (= R10), S100 (= S91), T298 (≠ I286), E317 (= E305), R413 (= R398), S415 (= S400), N416 (≠ G401), T417 (= T402)
- binding zinc ion: S100 (= S91), D234 (= D228), D236 (= D230), D238 (= D232)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
32% identity, 99% coverage: 2:435/438 of query aligns to 4:449/455 of 2fkfA
- active site: R12 (= R10), S100 (= S91), H101 (= H92), K110 (= K101), D234 (= D228), D236 (= D230), D238 (= D232), R239 (= R233), H321 (≠ T309), D332 (≠ P319)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (≠ G5), H101 (= H92), S319 (= S307), R413 (= R398), S415 (= S400), N416 (≠ G401), T417 (= T402)
- binding zinc ion: S100 (= S91), D234 (= D228), D236 (= D230), D238 (= D232)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
32% identity, 99% coverage: 2:435/438 of query aligns to 4:449/455 of 1pcmX