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Comparing AZOBR_RS07040 AZOBR_RS07040 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)
52% identity, 98% coverage: 2:445/455 of query aligns to 3:445/445 of P31120
- S100 (= S100) 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 (= S102) 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)
46% identity, 97% coverage: 6:445/455 of query aligns to 4:440/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
46% identity, 97% coverage: 6:445/455 of query aligns to 4:440/445 of 7ojrA
3i3wA Structure of a phosphoglucosamine mutase from francisella tularensis
40% identity, 94% coverage: 6:433/455 of query aligns to 3:424/441 of 3i3wA
- active site: R9 (= R12), S99 (= S102), H100 (= H103), K109 (= K112), D237 (= D243), D239 (= D245), D241 (= D247), R242 (= R248), H324 (= H332)
- binding zinc ion: S99 (= S102), D237 (= D243), D239 (= D245), D241 (= D247)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
35% identity, 93% coverage: 4:427/455 of query aligns to 3:432/455 of 1wqaA
- active site: R11 (= R12), S101 (= S102), H102 (= H103), K111 (= K112), D243 (= D243), D245 (= D245), D247 (= D247), R248 (= R248), G330 (≠ H332), R340 (≠ G342)
- binding magnesium ion: S101 (= S102), D243 (= D243), D245 (= D245), D247 (= D247)
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)
29% identity, 94% coverage: 5:431/455 of query aligns to 13:438/463 of P26276
- R15 (≠ G7) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (≠ D9) binding ; binding
- R20 (= R12) mutation to A: No phosphoglucomutase activity.
- S108 (= S102) 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 (= N104) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D243) binding
- D244 (= D245) binding
- D246 (= D247) binding
- R247 (= R248) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Q263) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ M288) binding
- H308 (≠ D311) binding ; binding
- E325 (= E328) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ EQSGH 328:332) binding ; binding
- H329 (= H332) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P374) 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 (≠ RKSGT 414:418) binding ; binding
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)
29% identity, 94% coverage: 5:431/455 of query aligns to 13:438/463 of Q02E40
- S108 (= S102) active site, Non-phosphorylated intermediate; modified: Phosphoserine
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
29% identity, 94% coverage: 5:431/455 of query aligns to 5:430/455 of 2h5aX
- active site: H101 (= H103), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), D332 (≠ G342)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (≠ D9), T298 (≠ V309), G299 (= G310), H300 (≠ D311), E317 (= E328), S319 (= S330), H321 (= H332), R413 (= R414), S415 (= S416), N416 (≠ G417), T417 (= T418)
- binding zinc ion: S100 (= S102), D234 (= D243), D236 (= D245), D238 (= D247)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
29% identity, 94% coverage: 5:431/455 of query aligns to 5:430/455 of 2h4lX
- active site: H101 (= H103), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), D332 (≠ G342)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (≠ D9), R12 (= R12), S100 (= S102), T298 (≠ V309), E317 (= E328), R413 (= R414), S415 (= S416), N416 (≠ G417), T417 (= T418)
- binding zinc ion: S100 (= S102), D234 (= D243), D236 (= D245), D238 (= D247)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
29% identity, 94% coverage: 5:431/455 of query aligns to 5:430/455 of 2fkfA
- active site: R12 (= R12), S100 (= S102), H101 (= H103), K110 (= K112), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), H321 (= H332), D332 (≠ G342)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (≠ G7), H101 (= H103), S319 (= S330), R413 (= R414), S415 (= S416), N416 (≠ G417), T417 (= T418)
- binding zinc ion: S100 (= S102), D234 (= D243), D236 (= D245), D238 (= D247)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
29% identity, 94% coverage: 5:431/455 of query aligns to 5:430/455 of 1pcmX
- active site: R12 (= R12), S100 (= S102), H101 (= H103), K110 (= K112), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), H321 (= H332), D332 (≠ G342)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (≠ D9), S100 (= S102), T298 (≠ V309), G299 (= G310), H300 (≠ D311), E317 (= E328), S319 (= S330), H321 (= H332), R413 (= R414), S415 (= S416)
- binding zinc ion: S100 (= S102), D234 (= D243), D236 (= D245), D238 (= D247)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
29% identity, 94% coverage: 5:431/455 of query aligns to 5:430/455 of 1p5gX
- active site: R12 (= R12), S100 (= S102), H101 (= H103), K110 (= K112), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), H321 (= H332), D332 (≠ G342)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (≠ D9), S100 (= S102), K277 (≠ M288), G299 (= G310), H300 (≠ D311), E317 (= E328), S319 (= S330), H321 (= H332), R413 (= R414), S415 (= S416), N416 (≠ G417), T417 (= T418)
- binding zinc ion: S100 (= S102), D234 (= D243), D236 (= D245), D238 (= D247)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
29% identity, 94% coverage: 5:431/455 of query aligns to 5:430/455 of 1p5dX
- active site: R12 (= R12), S100 (= S102), H101 (= H103), K110 (= K112), D234 (= D243), D236 (= D245), D238 (= D247), R239 (= R248), H321 (= H332), D332 (≠ G342)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (≠ D9), S100 (= S102), R239 (= R248), T298 (≠ V309), G299 (= G310), H300 (≠ D311), E317 (= E328), S319 (= S330), H321 (= H332), R413 (= R414), S415 (= S416), T417 (= T418)
- binding zinc ion: S100 (= S102), D234 (= D243), D236 (= D245), D238 (= D247)
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
29% identity, 94% coverage: 5:431/455 of query aligns to 8:433/458 of 1pcjX
- active site: R15 (= R12), S103 (= S102), H104 (= H103), K113 (= K112), D237 (= D243), D239 (= D245), D241 (= D247), R242 (= R248), H324 (= H332), D335 (≠ G342)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (≠ D9), S103 (= S102), T301 (≠ V309), G302 (= G310), E320 (= E328), S322 (= S330), H324 (= H332), R416 (= R414), S418 (= S416), N419 (≠ G417), T420 (= T418)
- binding zinc ion: S103 (= S102), D237 (= D243), D239 (= D245), D241 (= D247)
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
29% identity, 94% coverage: 5:431/455 of query aligns to 9:434/459 of 1k2yX
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
28% identity, 94% coverage: 1:427/455 of query aligns to 2:428/449 of 6mlwA
- active site: R13 (= R12), S98 (= S102), H99 (= H103), K108 (= K112), D238 (= D243), D240 (= D245), D242 (= D247), R243 (= R248), H325 (= H332)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G310), H304 (≠ D311), E321 (= E328), S323 (= S330), H325 (= H332), R415 (= R414), S417 (= S416), N418 (≠ G417), T419 (= T418), R424 (= R423)
- binding magnesium ion: S98 (= S102), D238 (= D243), D240 (= D245), D242 (= D247)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
28% identity, 94% coverage: 1:427/455 of query aligns to 2:428/449 of 5bmpA
- active site: R13 (= R12), S98 (= S102), H99 (= H103), K108 (= K112), D238 (= D243), D240 (= D245), D242 (= D247), R243 (= R248), H325 (= H332)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ M288), G303 (= G310), E321 (= E328), S323 (= S330), H325 (= H332), R415 (= R414), S417 (= S416), N418 (≠ G417), T419 (= T418), R424 (= R423)
- binding magnesium ion: S98 (= S102), D238 (= D243), D240 (= D245), D242 (= D247)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
28% identity, 94% coverage: 1:427/455 of query aligns to 1:427/448 of 6nqhA
- active site: R12 (= R12), S97 (= S102), H98 (= H103), K107 (= K112), D237 (= D243), D239 (= D245), D241 (= D247), R242 (= R248), H324 (= H332)
- binding magnesium ion: D237 (= D243), D239 (= D245), D241 (= D247)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R12), S97 (= S102), H98 (= H103), K107 (= K112), D239 (= D245), R242 (= R248), R280 (≠ M288), S301 (≠ V309), G302 (= G310), E320 (= E328), S322 (= S330), H324 (= H332), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
28% identity, 94% coverage: 1:427/455 of query aligns to 1:427/448 of 6np8A
- active site: R12 (= R12), S97 (= S102), H98 (= H103), K107 (= K112), D237 (= D243), D239 (= D245), D241 (= D247), R242 (= R248), H324 (= H332)
- binding calcium ion: S97 (= S102), D237 (= D243), D239 (= D245), D241 (= D247)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (≠ D9), R280 (≠ M288), G302 (= G310), H303 (≠ D311), E320 (= E328), S322 (= S330), H324 (= H332), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
28% identity, 94% coverage: 1:427/455 of query aligns to 1:427/448 of 6nolA
- active site: R12 (= R12), S97 (= S102), H98 (= H103), K107 (= K112), D237 (= D243), D239 (= D245), D241 (= D247), R242 (= R248), H324 (= H332)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G310), E320 (= E328), S322 (= S330), H324 (= H332), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S102), D237 (= D243), D239 (= D245), D241 (= D247)
Query Sequence
>AZOBR_RS07040 AZOBR_RS07040 phosphoglucosamine mutase
MTRHLFGTDGIRGTANIDPMTAETALRVAMASALQFRRGDHRHRVVIGKDTRLSGYLLEP
ALTAGFISMGMDVVLLGPLPTPAVAMLTRSLRADLGVMISASHNPYQDNGIKLFGPDGYK
LSDAVELAIETRMGQPFAPDLAGSADLGRASRLEDSTGRYIEYVKNTFPRGLRLDGLRIV
VDCANGAAYRVAPKVLYELGADVIPVGVNPDGLNINKDCGATATRTLQEQVVAHGAHLGI
ALDGDADRLIMVDEAGRVVDGDQVMALIASSWAQAQTLKGGGVVATVMSNLGMERHLQGL
GIALVRTPVGDRYVVEHMREHGYNVGGEQSGHVVLSDYSTTGDGLIAALQVLAVLIQSGG
RAASEVCQVFAPVPQKLTNVRFAAGSKPLEIASVQAAIRDGEARLNGSGRILIRKSGTEP
VIRVMAEGDDEGLVHAVVADIVGAITDAARLETAS
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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