SitesBLAST
Comparing PP_4716 FitnessBrowser__Putida:PP_4716 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)
62% identity, 99% coverage: 2:444/446 of query aligns to 3:445/445 of P31120
- S100 (= S99) 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 (= S101) 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
7omlA Bacillus subtilis phosphoglucomutase glmm (metal bound) (see paper)
44% identity, 98% coverage: 4:441/446 of query aligns to 2:440/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
44% identity, 98% coverage: 4:441/446 of query aligns to 2:440/445 of 7ojrA
3i3wA Structure of a phosphoglucosamine mutase from francisella tularensis
42% identity, 99% coverage: 4:446/446 of query aligns to 1:441/441 of 3i3wA
- active site: R9 (= R12), S99 (= S101), H100 (= H102), K109 (= K111), D237 (= D240), D239 (= D242), D241 (= D244), R242 (= R245), H324 (= H328)
- binding zinc ion: S99 (= S101), D237 (= D240), D239 (= D242), D241 (= D244)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
33% identity, 96% coverage: 4:433/446 of query aligns to 3:442/455 of 1wqaA
- active site: R11 (= R12), S101 (= S101), H102 (= H102), K111 (= K111), D243 (= D240), D245 (= D242), D247 (= D244), R248 (= R245), G330 (≠ H328), R340 (≠ G338)
- binding magnesium ion: S101 (= S101), D243 (= D240), D245 (= D242), D247 (= D244)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
28% identity, 94% coverage: 11:430/446 of query aligns to 11:433/455 of 2h5aX
- active site: H101 (= H102), D234 (= D240), D236 (= D242), D238 (= D244), R239 (= R245), D332 (≠ G338)
- binding 1-O-phosphono-alpha-D-xylopyranose: T298 (≠ V305), G299 (= G306), H300 (≠ D307), E317 (= E324), S319 (= S326), H321 (= H328), R413 (= R410), S415 (= S412), N416 (≠ G413), T417 (= T414)
- binding zinc ion: S100 (= S101), D234 (= D240), D236 (= D242), D238 (= D244)
Sites not aligning to the query:
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
28% identity, 94% coverage: 11:430/446 of query aligns to 11:433/455 of 2h4lX
- active site: H101 (= H102), D234 (= D240), D236 (= D242), D238 (= D244), R239 (= R245), D332 (≠ G338)
- binding 1-O-phosphono-alpha-D-ribofuranose: R12 (= R12), S100 (= S101), T298 (≠ V305), E317 (= E324), R413 (= R410), S415 (= S412), N416 (≠ G413), T417 (= T414)
- binding zinc ion: S100 (= S101), D234 (= D240), D236 (= D242), D238 (= D244)
Sites not aligning to the query:
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
28% identity, 94% coverage: 11:430/446 of query aligns to 11:433/455 of 2fkfA
- active site: R12 (= R12), S100 (= S101), H101 (= H102), K110 (= K111), D234 (= D240), D236 (= D242), D238 (= D244), R239 (= R245), H321 (= H328), D332 (≠ G338)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: H101 (= H102), S319 (= S326), R413 (= R410), S415 (= S412), N416 (≠ G413), T417 (= T414)
- binding zinc ion: S100 (= S101), D234 (= D240), D236 (= D242), D238 (= D244)
Sites not aligning to the query:
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
28% identity, 94% coverage: 11:430/446 of query aligns to 11:433/455 of 1pcmX
- active site: R12 (= R12), S100 (= S101), H101 (= H102), K110 (= K111), D234 (= D240), D236 (= D242), D238 (= D244), R239 (= R245), H321 (= H328), D332 (≠ G338)
- binding 6-O-phosphono-alpha-D-mannopyranose: S100 (= S101), T298 (≠ V305), G299 (= G306), H300 (≠ D307), E317 (= E324), S319 (= S326), H321 (= H328), R413 (= R410), S415 (= S412)
- binding zinc ion: S100 (= S101), D234 (= D240), D236 (= D242), D238 (= D244)
Sites not aligning to the query:
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
28% identity, 94% coverage: 11:430/446 of query aligns to 14:436/458 of 1pcjX
- active site: R15 (= R12), S103 (= S101), H104 (= H102), K113 (= K111), D237 (= D240), D239 (= D242), D241 (= D244), R242 (= R245), H324 (= H328), D335 (≠ G338)
- binding 1-O-phosphono-alpha-D-mannopyranose: S103 (= S101), T301 (≠ V305), G302 (= G306), E320 (= E324), S322 (= S326), H324 (= H328), R416 (= R410), S418 (= S412), N419 (≠ G413), T420 (= T414)
- binding zinc ion: S103 (= S101), D237 (= D240), D239 (= D242), D241 (= D244)
Sites not aligning to the query:
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
28% identity, 94% coverage: 11:430/446 of query aligns to 11:433/455 of 1p5gX
- active site: R12 (= R12), S100 (= S101), H101 (= H102), K110 (= K111), D234 (= D240), D236 (= D242), D238 (= D244), R239 (= R245), H321 (= H328), D332 (≠ G338)
- binding 6-O-phosphono-alpha-D-glucopyranose: S100 (= S101), K277 (≠ M284), G299 (= G306), H300 (≠ D307), E317 (= E324), S319 (= S326), H321 (= H328), R413 (= R410), S415 (= S412), N416 (≠ G413), T417 (= T414)
- binding zinc ion: S100 (= S101), D234 (= D240), D236 (= D242), D238 (= D244)
Sites not aligning to the query:
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
28% identity, 94% coverage: 11:430/446 of query aligns to 11:433/455 of 1p5dX
- active site: R12 (= R12), S100 (= S101), H101 (= H102), K110 (= K111), D234 (= D240), D236 (= D242), D238 (= D244), R239 (= R245), H321 (= H328), D332 (≠ G338)
- binding 1-O-phosphono-alpha-D-glucopyranose: S100 (= S101), R239 (= R245), T298 (≠ V305), G299 (= G306), H300 (≠ D307), E317 (= E324), S319 (= S326), H321 (= H328), R413 (= R410), S415 (= S412), T417 (= T414)
- binding zinc ion: S100 (= S101), D234 (= D240), D236 (= D242), D238 (= D244)
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, 94% coverage: 11:430/446 of query aligns to 19:441/463 of P26276
- R20 (= R12) mutation to A: No phosphoglucomutase activity.
- S108 (= S101) 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 (= N103) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D240) binding Mg(2+)
- D244 (= D242) binding Mg(2+)
- D246 (= D244) binding Mg(2+)
- R247 (= R245) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ E260) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ M284) binding alpha-D-glucose 1-phosphate
- H308 (≠ D307) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- E325 (= E324) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ ENSGH 324:328) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- H329 (= H328) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (≠ Q363) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R410) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RKSGT 410:414) 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, 94% coverage: 11:430/446 of query aligns to 19:441/463 of Q02E40
- S108 (= S101) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
27% identity, 94% coverage: 11:430/446 of query aligns to 15:437/459 of 1k2yX
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
32% identity, 58% coverage: 11:269/446 of query aligns to 15:267/459 of 4il8A
- active site: R16 (= R12), S104 (= S101), H105 (= H102), K114 (= K111), D238 (= D240), D240 (= D242), D242 (= D244), R243 (= R245)
- binding magnesium ion: S104 (= S101), D238 (= D240), D240 (= D242), D242 (= D244)
Sites not aligning to the query:
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
28% identity, 95% coverage: 1:423/446 of query aligns to 2:428/449 of 6mlwA
- active site: R13 (= R12), S98 (= S101), H99 (= H102), K108 (= K111), D238 (= D240), D240 (= D242), D242 (= D244), R243 (= R245), H325 (= H328)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G306), H304 (≠ D307), E321 (= E324), S323 (= S326), H325 (= H328), R415 (= R410), S417 (= S412), N418 (≠ G413), T419 (= T414), R424 (= R419)
- binding magnesium ion: S98 (= S101), D238 (= D240), D240 (= D242), D242 (= D244)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
28% identity, 95% coverage: 1:423/446 of query aligns to 2:428/449 of 5bmpA
- active site: R13 (= R12), S98 (= S101), H99 (= H102), K108 (= K111), D238 (= D240), D240 (= D242), D242 (= D244), R243 (= R245), H325 (= H328)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ L283), G303 (= G306), E321 (= E324), S323 (= S326), H325 (= H328), R415 (= R410), S417 (= S412), N418 (≠ G413), T419 (= T414), R424 (= R419)
- binding magnesium ion: S98 (= S101), D238 (= D240), D240 (= D242), D242 (= D244)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
28% identity, 95% coverage: 1:423/446 of query aligns to 1:427/448 of 6nqhA
- active site: R12 (= R12), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D240), D239 (= D242), D241 (= D244), R242 (= R245), H324 (= H328)
- binding magnesium ion: D237 (= D240), D239 (= D242), D241 (= D244)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R12), S97 (= S101), H98 (= H102), K107 (= K111), D239 (= D242), R242 (= R245), R280 (≠ L283), S301 (≠ V305), G302 (= G306), E320 (= E324), S322 (= S326), H324 (= H328), R414 (= R410), S416 (= S412), N417 (≠ G413), T418 (= T414), R423 (= R419)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
28% identity, 95% coverage: 1:423/446 of query aligns to 1:427/448 of 6np8A
- active site: R12 (= R12), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D240), D239 (= D242), D241 (= D244), R242 (= R245), H324 (= H328)
- binding calcium ion: S97 (= S101), D237 (= D240), D239 (= D242), D241 (= D244)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (≠ D9), R280 (≠ L283), G302 (= G306), H303 (≠ D307), E320 (= E324), S322 (= S326), H324 (= H328), R414 (= R410), S416 (= S412), N417 (≠ G413), T418 (= T414), R423 (= R419)
Query Sequence
>PP_4716 FitnessBrowser__Putida:PP_4716
MSRKYFGTDGIRGRVGEYPITPDFMLKLGWAAGMAFRKQGHCRVLVGKDTRISGYMFESA
LEAGLSAAGADVMLLGPMPTPAIAYLTRTFHAEAGIVISASHNPHDDNGIKFFSGQGTKL
PDEVELMIEELLDQPMTVVESGKLGKVSRINDAAGRYIEFCKSSVPSSTSFEGLKLVVDC
AHGATYKVAPSVFRELGADVTVLHAQPDGLNINEGCGSTHIESLQAAVLVGHADLGIAFD
GDGDRVLMVDHTGAIVDGDELLFIIARDLQEHGKLQGGVVGTLMSNLGLELALKDLDIPF
VRAKVGDRYVMAELLEREWLVGGENSGHVVCCNHTTTGDAIIAALQVLMALKRRGETLAQ
ARQALRKCPQVLINVRFGASKVDPLEHPAVKEASAKVTEALAGRGRVLLRKSGTEPLVRV
MVEGEDESQVRAHAEALAKLVGEVCV
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory