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Comparing CCNA_00116 CCNA_00116 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)
51% identity, 100% coverage: 1:447/448 of query aligns to 1:444/445 of P31120
- M1 (= M1) modified: Initiator methionine, Removed
- S100 (= S102) 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 (= S104) 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)
48% identity, 99% coverage: 6:447/448 of query aligns to 3:442/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
48% identity, 99% coverage: 6:447/448 of query aligns to 3:442/445 of 7ojrA
3i3wA Structure of a phosphoglucosamine mutase from francisella tularensis
40% identity, 98% coverage: 6:446/448 of query aligns to 2:437/441 of 3i3wA
- active site: R9 (= R13), S99 (= S104), H100 (= H105), K109 (= K114), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H334)
- binding zinc ion: S99 (= S104), D237 (= D245), D239 (= D247), D241 (= D249)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
35% identity, 94% coverage: 7:427/448 of query aligns to 5:432/455 of 1wqaA
- active site: R11 (= R13), S101 (= S104), H102 (= H105), K111 (= K114), D243 (= D245), D245 (= D247), D247 (= D249), R248 (= R250), G330 (≠ H334), R340 (≠ G344)
- binding magnesium ion: S101 (= S104), D243 (= D245), D245 (= D247), D247 (= D249)
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
27% identity, 98% coverage: 7:446/448 of query aligns to 7:448/449 of 6mlwA
- active site: R13 (= R13), S98 (= S104), H99 (= H105), K108 (= K114), D238 (= D245), D240 (= D247), D242 (= D249), R243 (= R250), H325 (= H334)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G312), H304 (≠ D313), E321 (= E330), S323 (= S332), H325 (= H334), R415 (= R414), S417 (= S416), N418 (≠ G417), T419 (= T418), R424 (= R423)
- binding magnesium ion: S98 (= S104), D238 (= D245), D240 (= D247), D242 (= D249)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
27% identity, 98% coverage: 7:446/448 of query aligns to 7:448/449 of 5bmpA
- active site: R13 (= R13), S98 (= S104), H99 (= H105), K108 (= K114), D238 (= D245), D240 (= D247), D242 (= D249), R243 (= R250), H325 (= H334)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ M290), G303 (= G312), E321 (= E330), S323 (= S332), H325 (= H334), R415 (= R414), S417 (= S416), N418 (≠ G417), T419 (= T418), R424 (= R423)
- binding magnesium ion: S98 (= S104), D238 (= D245), D240 (= D247), D242 (= D249)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
27% identity, 98% coverage: 7:446/448 of query aligns to 6:447/448 of 6nqhA
- active site: R12 (= R13), S97 (= S104), H98 (= H105), K107 (= K114), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H334)
- binding magnesium ion: D237 (= D245), D239 (= D247), D241 (= D249)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R13), S97 (= S104), H98 (= H105), K107 (= K114), D239 (= D247), R242 (= R250), R280 (≠ M290), S301 (≠ V311), G302 (= G312), E320 (= E330), S322 (= S332), H324 (= H334), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
27% identity, 98% coverage: 7:446/448 of query aligns to 6:447/448 of 6np8A
- active site: R12 (= R13), S97 (= S104), H98 (= H105), K107 (= K114), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H334)
- binding calcium ion: S97 (= S104), D237 (= D245), D239 (= D247), D241 (= D249)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (≠ D10), R280 (≠ M290), G302 (= G312), H303 (≠ D313), E320 (= E330), S322 (= S332), H324 (= H334), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
27% identity, 98% coverage: 7:446/448 of query aligns to 6:447/448 of 6nolA
- active site: R12 (= R13), S97 (= S104), H98 (= H105), K107 (= K114), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H334)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G312), E320 (= E330), S322 (= S332), H324 (= H334), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S104), D237 (= D245), D239 (= D247), D241 (= D249)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
27% identity, 98% coverage: 7:446/448 of query aligns to 6:447/448 of 6nnpA
- active site: R12 (= R13), S97 (= S104), H98 (= H105), K107 (= K114), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H334)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ M290), G302 (= G312), H303 (≠ D313), E320 (= E330), H324 (= H334), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S104), D237 (= D245), D239 (= D247), D241 (= D249)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
27% identity, 98% coverage: 7:446/448 of query aligns to 6:447/448 of 6nn2A
- active site: R12 (= R13), S97 (= S104), H98 (= H105), K107 (= K114), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H334)
- binding calcium ion: S97 (= S104), D237 (= D245), D239 (= D247), D241 (= D249)
6n1eA Crystal structure of x. Citri phosphoglucomutase in complex with 1- methyl-glucose 6-phosphate (see paper)
27% identity, 98% coverage: 7:446/448 of query aligns to 6:447/448 of 6n1eA
6mnvA Crystal structure of x. Citri phosphoglucomutase in complex with ch2fg1p (see paper)
27% identity, 98% coverage: 7:446/448 of query aligns to 6:447/448 of 6mnvA
- binding 1-deoxy-1-fluoro-2-O-phosphono-alpha-D-gluco-hept-2-ulopyranose: R280 (≠ M290), G302 (= G312), E320 (= E330), S322 (= S332), H324 (= H334), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S104), D237 (= D245), D239 (= D247), D241 (= D249)
6mlhA Crystal structure of x. Citri phosphoglucomutase in complex with glucopyranosyl-1-methyl-phosphonic acid (see paper)
27% identity, 98% coverage: 7:446/448 of query aligns to 6:447/448 of 6mlhA
- active site: R12 (= R13), S97 (= S104), H98 (= H105), K107 (= K114), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H334)
- binding (1S)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: R280 (≠ M290), G302 (= G312), E320 (= E330), H324 (= H334), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S104), D237 (= D245), D239 (= D247), D241 (= D249)
6mlfA Crystal structure of x. Citri phosphoglucomutase in complex with 6- fluoro glucose 1-phosphate (see paper)
27% identity, 98% coverage: 7:446/448 of query aligns to 6:447/448 of 6mlfA
- active site: R12 (= R13), S97 (= S104), H98 (= H105), K107 (= K114), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H334)
- binding 6-deoxy-6-fluoro-1-O-phosphono-alpha-D-glucopyranose: R280 (≠ M290), G302 (= G312), E320 (= E330), H324 (= H334), R414 (= R414), S416 (= S416), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S104), D237 (= D245), D239 (= D247), D241 (= D249)
5kl0A Crystal structure of phosphoglucomutase from xanthomonas citri citri complexed with glucose-1,6-biphosphate (see paper)
27% identity, 98% coverage: 7:446/448 of query aligns to 6:447/448 of 5kl0A
- active site: R12 (= R13), S97 (= S104), H98 (= H105), K107 (= K114), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H334)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: S97 (= S104), G302 (= G312), H303 (≠ D313), E320 (= E330), H324 (= H334), R414 (= R414), S416 (= S416), N417 (≠ G417), R423 (= R423)
- binding magnesium ion: S97 (= S104), D237 (= D245), D239 (= D247), D241 (= D249)
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
25% identity, 95% coverage: 21:447/448 of query aligns to 22:449/458 of 1pcjX
- active site: S103 (= S104), H104 (= H105), K113 (= K114), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H334), D335 (≠ G344)
- binding 1-O-phosphono-alpha-D-mannopyranose: S103 (= S104), T301 (≠ V311), G302 (= G312), E320 (= E330), S322 (= S332), H324 (= H334), R416 (= R414), S418 (= S416), N419 (≠ G417), T420 (= T418)
- binding zinc ion: S103 (= S104), D237 (= D245), D239 (= D247), D241 (= D249)
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)
25% identity, 95% coverage: 21:447/448 of query aligns to 27:454/463 of P26276
- S108 (= S104) 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 (= N106) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D245) binding
- D244 (= D247) binding
- D246 (= D249) binding
- R247 (= R250) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Q265) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ M290) binding
- H308 (≠ D313) binding ; binding
- E325 (= E330) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ EQSGH 330:334) binding ; binding
- H329 (= H334) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (≠ E372) 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 (≠ RASGT 414:418) 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
- 20 R→A: No phosphoglucomutase activity.
Q02E40 Phosphomannomutase/phosphoglucomutase; PMM / PGM; EC 5.4.2.2; EC 5.4.2.8 from Pseudomonas aeruginosa (strain UCBPP-PA14) (see paper)
25% identity, 95% coverage: 21:447/448 of query aligns to 27:454/463 of Q02E40
- S108 (= S104) active site, Non-phosphorylated intermediate; modified: Phosphoserine
Query Sequence
>CCNA_00116 CCNA_00116 phosphoglucosamine mutase
MSKRAYFGTDGIRGQANKHPMTAEVALRVGLAAGKLFRSQDERRHLVVIGKDTRLSGYMI
EPALVAGLTSVGLDVRLFGPLPTPAVAMMTRSMRADLGIMISASHNSFADNGIKLFGPDG
YKLSDAQELGIEALMDQGLQEGLAAPRELGRVKRIDDAQARYVEIVKATFPRHLNLSGLR
IVIDCANGAAYKVAPTALYELGAEVITLGVSPDGTNINEECGSTHPEAMAKMVREYRADI
GIALDGDADRLVICDEKGVVVDGDQIMAIIAAASHKAGTLKGGGVVATVMSNLGLERQLN
TMGLSLERTAVGDRYVMQRMREGGFNVGGEQSGHLILSDFSTTGDGLIAALQVLAVMVET
DKPMSALGRQFEPVPQLLENVRFVGGKPLEAAAVKEAIADGEAQLNGAGRIVVRASGTEP
LIRIMAEGDDPALVKKVVKSIASAVKAA
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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