SitesBLAST
Comparing WP_012967600.1 NCBI__GCF_000025465.1:WP_012967600.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
57% identity, 98% coverage: 4:456/460 of query aligns to 3:447/448 of 6nqhA
- active site: R12 (= R13), S97 (= S98), H98 (= H99), K107 (= K108), D237 (= D246), D239 (= D248), D241 (= D250), R242 (= R251), H324 (= H333)
- binding magnesium ion: D237 (= D246), D239 (= D248), D241 (= D250)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R13), S97 (= S98), H98 (= H99), K107 (= K108), D239 (= D248), R242 (= R251), R280 (= R289), S301 (≠ T310), G302 (= G311), E320 (= E329), S322 (= S331), H324 (= H333), R414 (= R423), S416 (= S425), N417 (= N426), T418 (= T427), R423 (= R432)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
57% identity, 98% coverage: 4:456/460 of query aligns to 3:447/448 of 6np8A
- active site: R12 (= R13), S97 (= S98), H98 (= H99), K107 (= K108), D237 (= D246), D239 (= D248), D241 (= D250), R242 (= R251), H324 (= H333)
- binding calcium ion: S97 (= S98), D237 (= D246), D239 (= D248), D241 (= D250)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y10), R280 (= R289), G302 (= G311), H303 (= H312), E320 (= E329), S322 (= S331), H324 (= H333), R414 (= R423), S416 (= S425), N417 (= N426), T418 (= T427), R423 (= R432)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
57% identity, 98% coverage: 4:456/460 of query aligns to 3:447/448 of 6nolA
- active site: R12 (= R13), S97 (= S98), H98 (= H99), K107 (= K108), D237 (= D246), D239 (= D248), D241 (= D250), R242 (= R251), H324 (= H333)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G311), E320 (= E329), S322 (= S331), H324 (= H333), R414 (= R423), S416 (= S425), N417 (= N426), T418 (= T427), R423 (= R432)
- binding magnesium ion: S97 (= S98), D237 (= D246), D239 (= D248), D241 (= D250)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
57% identity, 98% coverage: 4:456/460 of query aligns to 3:447/448 of 6nnpA
- active site: R12 (= R13), S97 (= S98), H98 (= H99), K107 (= K108), D237 (= D246), D239 (= D248), D241 (= D250), R242 (= R251), H324 (= H333)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (= R289), G302 (= G311), H303 (= H312), E320 (= E329), H324 (= H333), R414 (= R423), S416 (= S425), N417 (= N426), T418 (= T427), R423 (= R432)
- binding magnesium ion: S97 (= S98), D237 (= D246), D239 (= D248), D241 (= D250)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
57% identity, 98% coverage: 4:456/460 of query aligns to 3:447/448 of 6nn2A
- active site: R12 (= R13), S97 (= S98), H98 (= H99), K107 (= K108), D237 (= D246), D239 (= D248), D241 (= D250), R242 (= R251), H324 (= H333)
- binding calcium ion: S97 (= S98), D237 (= D246), D239 (= D248), D241 (= D250)
6n1eA Crystal structure of x. Citri phosphoglucomutase in complex with 1- methyl-glucose 6-phosphate (see paper)
57% identity, 98% coverage: 4:456/460 of query aligns to 3:447/448 of 6n1eA
6mnvA Crystal structure of x. Citri phosphoglucomutase in complex with ch2fg1p (see paper)
57% identity, 98% coverage: 4:456/460 of query aligns to 3:447/448 of 6mnvA
- binding 1-deoxy-1-fluoro-2-O-phosphono-alpha-D-gluco-hept-2-ulopyranose: R280 (= R289), G302 (= G311), E320 (= E329), S322 (= S331), H324 (= H333), R414 (= R423), S416 (= S425), N417 (= N426), T418 (= T427), R423 (= R432)
- binding magnesium ion: S97 (= S98), D237 (= D246), D239 (= D248), D241 (= D250)
6mlhA Crystal structure of x. Citri phosphoglucomutase in complex with glucopyranosyl-1-methyl-phosphonic acid (see paper)
57% identity, 98% coverage: 4:456/460 of query aligns to 3:447/448 of 6mlhA
- active site: R12 (= R13), S97 (= S98), H98 (= H99), K107 (= K108), D237 (= D246), D239 (= D248), D241 (= D250), R242 (= R251), H324 (= H333)
- binding (1S)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: R280 (= R289), G302 (= G311), E320 (= E329), H324 (= H333), R414 (= R423), S416 (= S425), N417 (= N426), T418 (= T427), R423 (= R432)
- binding magnesium ion: S97 (= S98), D237 (= D246), D239 (= D248), D241 (= D250)
6mlfA Crystal structure of x. Citri phosphoglucomutase in complex with 6- fluoro glucose 1-phosphate (see paper)
57% identity, 98% coverage: 4:456/460 of query aligns to 3:447/448 of 6mlfA
- active site: R12 (= R13), S97 (= S98), H98 (= H99), K107 (= K108), D237 (= D246), D239 (= D248), D241 (= D250), R242 (= R251), H324 (= H333)
- binding 6-deoxy-6-fluoro-1-O-phosphono-alpha-D-glucopyranose: R280 (= R289), G302 (= G311), E320 (= E329), H324 (= H333), R414 (= R423), S416 (= S425), T418 (= T427), R423 (= R432)
- binding magnesium ion: S97 (= S98), D237 (= D246), D239 (= D248), D241 (= D250)
5kl0A Crystal structure of phosphoglucomutase from xanthomonas citri citri complexed with glucose-1,6-biphosphate (see paper)
57% identity, 98% coverage: 4:456/460 of query aligns to 3:447/448 of 5kl0A
- active site: R12 (= R13), S97 (= S98), H98 (= H99), K107 (= K108), D237 (= D246), D239 (= D248), D241 (= D250), R242 (= R251), H324 (= H333)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: S97 (= S98), G302 (= G311), H303 (= H312), E320 (= E329), H324 (= H333), R414 (= R423), S416 (= S425), N417 (= N426), R423 (= R432)
- binding magnesium ion: S97 (= S98), D237 (= D246), D239 (= D248), D241 (= D250)
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
57% identity, 98% coverage: 4:456/460 of query aligns to 4:448/449 of 6mlwA
- active site: R13 (= R13), S98 (= S98), H99 (= H99), K108 (= K108), D238 (= D246), D240 (= D248), D242 (= D250), R243 (= R251), H325 (= H333)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G311), H304 (= H312), E321 (= E329), S323 (= S331), H325 (= H333), R415 (= R423), S417 (= S425), N418 (= N426), T419 (= T427), R424 (= R432)
- binding magnesium ion: S98 (= S98), D238 (= D246), D240 (= D248), D242 (= D250)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
57% identity, 98% coverage: 4:456/460 of query aligns to 4:448/449 of 5bmpA
- active site: R13 (= R13), S98 (= S98), H99 (= H99), K108 (= K108), D238 (= D246), D240 (= D248), D242 (= D250), R243 (= R251), H325 (= H333)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (= R289), G303 (= G311), E321 (= E329), S323 (= S331), H325 (= H333), R415 (= R423), S417 (= S425), N418 (= N426), T419 (= T427), R424 (= R432)
- binding magnesium ion: S98 (= S98), D238 (= D246), D240 (= D248), D242 (= D250)
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, 97% coverage: 5:448/460 of query aligns to 12:446/463 of P26276
- R15 (≠ K8) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (= Y10) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- R20 (= R13) mutation to A: No phosphoglucomutase activity.
- S108 (= S98) 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 (= N100) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D246) binding Mg(2+)
- D244 (= D248) binding Mg(2+)
- D246 (= D250) binding Mg(2+)
- R247 (= R251) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Y266) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ R289) binding alpha-D-glucose 1-phosphate
- H308 (= H312) 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 (≠ EMSAH 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 (= P375) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R423) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RTSNT 423:427) 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)
34% identity, 97% coverage: 5:448/460 of query aligns to 12:446/463 of Q02E40
- S108 (= S98) active site, Non-phosphorylated intermediate; modified: Phosphoserine
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
34% identity, 97% coverage: 5:448/460 of query aligns to 4:438/455 of 2h5aX
- active site: H101 (= H99), D234 (= D246), D236 (= D248), D238 (= D250), R239 (= R251), D332 (= D343)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (= Y10), T298 (= T310), G299 (= G311), H300 (= H312), E317 (= E329), S319 (= S331), H321 (= H333), R413 (= R423), S415 (= S425), N416 (= N426), T417 (= T427)
- binding zinc ion: S100 (= S98), D234 (= D246), D236 (= D248), D238 (= D250)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
34% identity, 97% coverage: 5:448/460 of query aligns to 4:438/455 of 2h4lX
- active site: H101 (= H99), D234 (= D246), D236 (= D248), D238 (= D250), R239 (= R251), D332 (= D343)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (= Y10), R12 (= R13), S100 (= S98), T298 (= T310), E317 (= E329), R413 (= R423), S415 (= S425), N416 (= N426), T417 (= T427)
- binding zinc ion: S100 (= S98), D234 (= D246), D236 (= D248), D238 (= D250)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
34% identity, 97% coverage: 5:448/460 of query aligns to 4:438/455 of 2fkfA
- active site: R12 (= R13), S100 (= S98), H101 (= H99), K110 (= K108), D234 (= D246), D236 (= D248), D238 (= D250), R239 (= R251), H321 (= H333), D332 (= D343)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (≠ K8), H101 (= H99), S319 (= S331), R413 (= R423), S415 (= S425), N416 (= N426), T417 (= T427)
- binding zinc ion: S100 (= S98), D234 (= D246), D236 (= D248), D238 (= D250)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
34% identity, 97% coverage: 5:448/460 of query aligns to 4:438/455 of 1pcmX
- active site: R12 (= R13), S100 (= S98), H101 (= H99), K110 (= K108), D234 (= D246), D236 (= D248), D238 (= D250), R239 (= R251), H321 (= H333), D332 (= D343)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (= Y10), S100 (= S98), T298 (= T310), G299 (= G311), H300 (= H312), E317 (= E329), S319 (= S331), H321 (= H333), R413 (= R423), S415 (= S425)
- binding zinc ion: S100 (= S98), D234 (= D246), D236 (= D248), D238 (= D250)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
34% identity, 97% coverage: 5:448/460 of query aligns to 4:438/455 of 1p5gX
- active site: R12 (= R13), S100 (= S98), H101 (= H99), K110 (= K108), D234 (= D246), D236 (= D248), D238 (= D250), R239 (= R251), H321 (= H333), D332 (= D343)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (= Y10), S100 (= S98), K277 (≠ R289), G299 (= G311), H300 (= H312), E317 (= E329), S319 (= S331), H321 (= H333), R413 (= R423), S415 (= S425), N416 (= N426), T417 (= T427)
- binding zinc ion: S100 (= S98), D234 (= D246), D236 (= D248), D238 (= D250)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
34% identity, 97% coverage: 5:448/460 of query aligns to 4:438/455 of 1p5dX
- active site: R12 (= R13), S100 (= S98), H101 (= H99), K110 (= K108), D234 (= D246), D236 (= D248), D238 (= D250), R239 (= R251), H321 (= H333), D332 (= D343)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (= Y10), S100 (= S98), R239 (= R251), T298 (= T310), G299 (= G311), H300 (= H312), E317 (= E329), S319 (= S331), H321 (= H333), R413 (= R423), S415 (= S425), T417 (= T427)
- binding zinc ion: S100 (= S98), D234 (= D246), D236 (= D248), D238 (= D250)
Query Sequence
>WP_012967600.1 NCBI__GCF_000025465.1:WP_012967600.1
MTQLTCFKAYDIRGELGEELNEDIAYRIGRAYGEFLKPGKIVVGGDVRLTSESLKLALAR
GLMDAGTDVLDIGLSGTEEIYFATFHLGVDGGIEVTASHNPMNYNGMKLVRENAKPISGD
TGLRDIQRLAEENQFPPVDPARRGTLRQISVLKEYVDHLMGYVDLANFTRPLKLVVNSGN
GAAGHVIDEVEKRFAAAGAPVTFIKVHHQPDGHFPNGIPNPLLPECRQDTADAVRAHQAD
MGIAFDGDFDRCFLFDDEASFIEGYYIVGLLAEAFLQKQPGAKIIHDPRLTWNTVDIVTR
SGGQPVMSKTGHAFIKERMRQEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELLCLKN
SSLKSLVADRQAAFPASGEINRKLGNAAEAIARIRAQYEPAAAHIDTTDGISIEYPEWRF
NLRTSNTEPVVRLNVESRADTALMNEKTAELLNLLKEESL
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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