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Comparing WP_057508397.1 NCBI__GCF_001431535.1:WP_057508397.1 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)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
83% identity, 100% coverage: 1:447/448 of query aligns to 1:447/448 of 6nqhA
- active site: R12 (= R12), S97 (= S97), H98 (= H98), K107 (= K107), D237 (= D237), D239 (= D239), D241 (= D241), R242 (= R242), H324 (= H324)
- binding magnesium ion: D237 (= D237), D239 (= D239), D241 (= D241)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R12), S97 (= S97), H98 (= H98), K107 (= K107), D239 (= D239), R242 (= R242), R280 (= R280), S301 (= S301), G302 (= G302), E320 (= E320), S322 (= S322), H324 (= H324), R414 (= R414), S416 (= S416), N417 (= N417), T418 (= T418), R423 (= R423)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
83% identity, 100% coverage: 1:447/448 of query aligns to 1:447/448 of 6np8A
- active site: R12 (= R12), S97 (= S97), H98 (= H98), K107 (= K107), D237 (= D237), D239 (= D239), D241 (= D241), R242 (= R242), H324 (= H324)
- binding calcium ion: S97 (= S97), D237 (= D237), D239 (= D239), D241 (= D241)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y9), R280 (= R280), G302 (= G302), H303 (= H303), E320 (= E320), S322 (= S322), H324 (= H324), R414 (= R414), S416 (= S416), N417 (= N417), T418 (= T418), R423 (= R423)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
83% identity, 100% coverage: 1:447/448 of query aligns to 1:447/448 of 6nolA
- active site: R12 (= R12), S97 (= S97), H98 (= H98), K107 (= K107), D237 (= D237), D239 (= D239), D241 (= D241), R242 (= R242), H324 (= H324)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G302), E320 (= E320), S322 (= S322), H324 (= H324), R414 (= R414), S416 (= S416), N417 (= N417), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S97), D237 (= D237), D239 (= D239), D241 (= D241)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
83% identity, 100% coverage: 1:447/448 of query aligns to 1:447/448 of 6nnpA
- active site: R12 (= R12), S97 (= S97), H98 (= H98), K107 (= K107), D237 (= D237), D239 (= D239), D241 (= D241), R242 (= R242), H324 (= H324)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (= R280), G302 (= G302), H303 (= H303), E320 (= E320), H324 (= H324), R414 (= R414), S416 (= S416), N417 (= N417), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S97), D237 (= D237), D239 (= D239), D241 (= D241)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
83% identity, 100% coverage: 1:447/448 of query aligns to 1:447/448 of 6nn2A
- active site: R12 (= R12), S97 (= S97), H98 (= H98), K107 (= K107), D237 (= D237), D239 (= D239), D241 (= D241), R242 (= R242), H324 (= H324)
- binding calcium ion: S97 (= S97), D237 (= D237), D239 (= D239), D241 (= D241)
6n1eA Crystal structure of x. Citri phosphoglucomutase in complex with 1- methyl-glucose 6-phosphate (see paper)
83% identity, 100% coverage: 1:447/448 of query aligns to 1:447/448 of 6n1eA
6mnvA Crystal structure of x. Citri phosphoglucomutase in complex with ch2fg1p (see paper)
83% identity, 100% coverage: 1:447/448 of query aligns to 1:447/448 of 6mnvA
- binding 1-deoxy-1-fluoro-2-O-phosphono-alpha-D-gluco-hept-2-ulopyranose: R280 (= R280), G302 (= G302), E320 (= E320), S322 (= S322), H324 (= H324), R414 (= R414), S416 (= S416), N417 (= N417), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S97), D237 (= D237), D239 (= D239), D241 (= D241)
6mlhA Crystal structure of x. Citri phosphoglucomutase in complex with glucopyranosyl-1-methyl-phosphonic acid (see paper)
83% identity, 100% coverage: 1:447/448 of query aligns to 1:447/448 of 6mlhA
- active site: R12 (= R12), S97 (= S97), H98 (= H98), K107 (= K107), D237 (= D237), D239 (= D239), D241 (= D241), R242 (= R242), H324 (= H324)
- binding (1S)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: R280 (= R280), G302 (= G302), E320 (= E320), H324 (= H324), R414 (= R414), S416 (= S416), N417 (= N417), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S97), D237 (= D237), D239 (= D239), D241 (= D241)
6mlfA Crystal structure of x. Citri phosphoglucomutase in complex with 6- fluoro glucose 1-phosphate (see paper)
83% identity, 100% coverage: 1:447/448 of query aligns to 1:447/448 of 6mlfA
- active site: R12 (= R12), S97 (= S97), H98 (= H98), K107 (= K107), D237 (= D237), D239 (= D239), D241 (= D241), R242 (= R242), H324 (= H324)
- binding 6-deoxy-6-fluoro-1-O-phosphono-alpha-D-glucopyranose: R280 (= R280), G302 (= G302), E320 (= E320), H324 (= H324), R414 (= R414), S416 (= S416), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S97), D237 (= D237), D239 (= D239), D241 (= D241)
5kl0A Crystal structure of phosphoglucomutase from xanthomonas citri citri complexed with glucose-1,6-biphosphate (see paper)
83% identity, 100% coverage: 1:447/448 of query aligns to 1:447/448 of 5kl0A
- active site: R12 (= R12), S97 (= S97), H98 (= H98), K107 (= K107), D237 (= D237), D239 (= D239), D241 (= D241), R242 (= R242), H324 (= H324)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: S97 (= S97), G302 (= G302), H303 (= H303), E320 (= E320), H324 (= H324), R414 (= R414), S416 (= S416), N417 (= N417), R423 (= R423)
- binding magnesium ion: S97 (= S97), D237 (= D237), D239 (= D239), D241 (= D241)
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
83% identity, 100% coverage: 1:447/448 of query aligns to 2:448/449 of 6mlwA
- active site: R13 (= R12), S98 (= S97), H99 (= H98), K108 (= K107), D238 (= D237), D240 (= D239), D242 (= D241), R243 (= R242), H325 (= H324)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G302), H304 (= H303), E321 (= E320), S323 (= S322), H325 (= H324), R415 (= R414), S417 (= S416), N418 (= N417), T419 (= T418), R424 (= R423)
- binding magnesium ion: S98 (= S97), D238 (= D237), D240 (= D239), D242 (= D241)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
83% identity, 100% coverage: 1:447/448 of query aligns to 2:448/449 of 5bmpA
- active site: R13 (= R12), S98 (= S97), H99 (= H98), K108 (= K107), D238 (= D237), D240 (= D239), D242 (= D241), R243 (= R242), H325 (= H324)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (= R280), G303 (= G302), E321 (= E320), S323 (= S322), H325 (= H324), R415 (= R414), S417 (= S416), N418 (= N417), T419 (= T418), R424 (= R423)
- binding magnesium ion: S98 (= S97), D238 (= D237), D240 (= D239), D242 (= D241)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
34% identity, 98% coverage: 1:439/448 of query aligns to 1:438/455 of 2h5aX
- active site: H101 (= H98), D234 (= D237), D236 (= D239), D238 (= D241), R239 (= R242), D332 (= D334)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y9), T298 (≠ S301), G299 (= G302), H300 (= H303), E317 (= E320), S319 (= S322), H321 (= H324), R413 (= R414), S415 (= S416), N416 (= N417), T417 (= T418)
- binding zinc ion: S100 (= S97), D234 (= D237), D236 (= D239), D238 (= D241)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
34% identity, 98% coverage: 1:439/448 of query aligns to 1:438/455 of 2h4lX
- active site: H101 (= H98), D234 (= D237), D236 (= D239), D238 (= D241), R239 (= R242), D332 (= D334)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y9), R12 (= R12), S100 (= S97), T298 (≠ S301), E317 (= E320), R413 (= R414), S415 (= S416), N416 (= N417), T417 (= T418)
- binding zinc ion: S100 (= S97), D234 (= D237), D236 (= D239), D238 (= D241)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
34% identity, 98% coverage: 1:439/448 of query aligns to 1:438/455 of 2fkfA
- active site: R12 (= R12), S100 (= S97), H101 (= H98), K110 (= K107), D234 (= D237), D236 (= D239), D238 (= D241), R239 (= R242), H321 (= H324), D332 (= D334)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (≠ K7), H101 (= H98), S319 (= S322), R413 (= R414), S415 (= S416), N416 (= N417), T417 (= T418)
- binding zinc ion: S100 (= S97), D234 (= D237), D236 (= D239), D238 (= D241)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
34% identity, 98% coverage: 1:439/448 of query aligns to 1:438/455 of 1pcmX
- active site: R12 (= R12), S100 (= S97), H101 (= H98), K110 (= K107), D234 (= D237), D236 (= D239), D238 (= D241), R239 (= R242), H321 (= H324), D332 (= D334)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y9), S100 (= S97), T298 (≠ S301), G299 (= G302), H300 (= H303), E317 (= E320), S319 (= S322), H321 (= H324), R413 (= R414), S415 (= S416)
- binding zinc ion: S100 (= S97), D234 (= D237), D236 (= D239), D238 (= D241)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
34% identity, 98% coverage: 1:439/448 of query aligns to 1:438/455 of 1p5gX
- active site: R12 (= R12), S100 (= S97), H101 (= H98), K110 (= K107), D234 (= D237), D236 (= D239), D238 (= D241), R239 (= R242), H321 (= H324), D332 (= D334)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y9), S100 (= S97), K277 (≠ R280), G299 (= G302), H300 (= H303), E317 (= E320), S319 (= S322), H321 (= H324), R413 (= R414), S415 (= S416), N416 (= N417), T417 (= T418)
- binding zinc ion: S100 (= S97), D234 (= D237), D236 (= D239), D238 (= D241)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
34% identity, 98% coverage: 1:439/448 of query aligns to 1:438/455 of 1p5dX
- active site: R12 (= R12), S100 (= S97), H101 (= H98), K110 (= K107), D234 (= D237), D236 (= D239), D238 (= D241), R239 (= R242), H321 (= H324), D332 (= D334)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (= Y9), S100 (= S97), R239 (= R242), T298 (≠ S301), G299 (= G302), H300 (= H303), E317 (= E320), S319 (= S322), H321 (= H324), R413 (= R414), S415 (= S416), T417 (= T418)
- binding zinc ion: S100 (= S97), D234 (= D237), D236 (= D239), D238 (= D241)
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
34% identity, 98% coverage: 1:439/448 of query aligns to 4:441/458 of 1pcjX
- active site: R15 (= R12), S103 (= S97), H104 (= H98), K113 (= K107), D237 (= D237), D239 (= D239), D241 (= D241), R242 (= R242), H324 (= H324), D335 (= D334)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (= Y9), S103 (= S97), T301 (≠ S301), G302 (= G302), E320 (= E320), S322 (= S322), H324 (= H324), R416 (= R414), S418 (= S416), N419 (= N417), T420 (= T418)
- binding zinc ion: S103 (= S97), D237 (= D237), D239 (= D239), D241 (= D241)
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)
34% identity, 98% coverage: 1:439/448 of query aligns to 9:446/463 of P26276
- R15 (≠ K7) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y9) binding ; binding
- R20 (= R12) mutation to A: No phosphoglucomutase activity.
- S108 (= S97) 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 (= N99) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D237) binding
- D244 (= D239) binding
- D246 (= D241) binding
- R247 (= R242) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Y257) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ R280) binding
- H308 (= H303) binding ; binding
- E325 (= E320) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ EMSAH 320:324) binding ; binding
- H329 (= H324) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P366) 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 (≠ RSSNT 414:418) binding ; binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>WP_057508397.1 NCBI__GCF_001431535.1:WP_057508397.1
MPLPAFKAYDIRGRVPDELNEDLARRIGVALSDQLEPGTVVVGHDVRLTSAALQDALVVG
LRGAGREVIDIGLCGTEEVYFQTDHLGAAGGVMVTASHNPMDYNGMKLVRENARPISSDT
GLFAISDAVAADTAAALPPKAGQSEQHDKSAYIAHLLSYVDAAALKPLKVVVNAGNGGAG
AIVDLLAPHLPLQFIRVNHEPDGNFPNGIPNPLLPENRAATAEAVREHGADFGIAWDGDF
DRCFFFDHTGRFIEGYYLVGLLAQAALKRHPGGKVVHDPRLVWNTVEMVEQAGGIPVLCK
SGHAFIKEKMRAEDAVYGGEMSAHHYFREFAYADSGMIPWLLIAALVSESGRSLADWVED
RMAAYPCSGEINFKVADAKVSVARVMEHFASHAPALDHTDGISADFGDWRFNLRSSNTEP
LLRLNVETRGDAALLQSRTDEISSLLQR
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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