SitesBLAST
Comparing WP_052664356.1 NCBI__GCF_000969705.1:WP_052664356.1 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)
7omlA Bacillus subtilis phosphoglucomutase glmm (metal bound) (see paper)
49% identity, 99% coverage: 2:444/446 of query aligns to 1:444/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
49% identity, 99% coverage: 2:444/446 of query aligns to 1:444/445 of 7ojrA
P31120 Phosphoglucosamine mutase; EC 5.4.2.10 from Escherichia coli (strain K12) (see 3 papers)
46% identity, 98% coverage: 3:441/446 of query aligns to 5:443/445 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
3i3wA Structure of a phosphoglucosamine mutase from francisella tularensis
40% identity, 99% coverage: 3:444/446 of query aligns to 1:440/441 of 3i3wA
- active site: R9 (= R11), S99 (= S101), H100 (= H102), K109 (= K111), D237 (= D239), D239 (= D241), D241 (= D243), R242 (= R244), H324 (= H328)
- binding zinc ion: S99 (= S101), D237 (= D239), D239 (= D241), D241 (= D243)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
35% identity, 98% coverage: 1:435/446 of query aligns to 1:445/455 of 1wqaA
- active site: R11 (= R11), S101 (= S101), H102 (= H102), K111 (= K111), D243 (= D239), D245 (= D241), D247 (= D243), R248 (= R244), G330 (≠ H328), R340 (≠ G338)
- binding magnesium ion: S101 (= S101), D243 (= D239), D245 (= D241), D247 (= D243)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
30% identity, 98% coverage: 4:441/446 of query aligns to 5:445/455 of 2h5aX
- active site: H101 (= H102), D234 (= D239), D236 (= D241), D238 (= D243), R239 (= R244), D332 (≠ G338)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (≠ D8), T298 (≠ V305), G299 (= G306), H300 (≠ D307), E317 (= E324), S319 (= S326), H321 (= H328), R413 (= R409), S415 (= S411), N416 (≠ G412), T417 (= T413)
- binding zinc ion: S100 (= S101), D234 (= D239), D236 (= D241), D238 (= D243)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
30% identity, 98% coverage: 4:441/446 of query aligns to 5:445/455 of 2h4lX
- active site: H101 (= H102), D234 (= D239), D236 (= D241), D238 (= D243), R239 (= R244), D332 (≠ G338)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (≠ D8), R12 (= R11), S100 (= S101), T298 (≠ V305), E317 (= E324), R413 (= R409), S415 (= S411), N416 (≠ G412), T417 (= T413)
- binding zinc ion: S100 (= S101), D234 (= D239), D236 (= D241), D238 (= D243)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
30% identity, 98% coverage: 4:441/446 of query aligns to 5:445/455 of 2fkfA
- active site: R12 (= R11), S100 (= S101), H101 (= H102), K110 (= K111), D234 (= D239), D236 (= D241), D238 (= D243), R239 (= R244), H321 (= H328), D332 (≠ G338)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (≠ G6), H101 (= H102), S319 (= S326), R413 (= R409), S415 (= S411), N416 (≠ G412), T417 (= T413)
- binding zinc ion: S100 (= S101), D234 (= D239), D236 (= D241), D238 (= D243)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
30% identity, 98% coverage: 4:441/446 of query aligns to 5:445/455 of 1pcmX
- active site: R12 (= R11), S100 (= S101), H101 (= H102), K110 (= K111), D234 (= D239), D236 (= D241), D238 (= D243), R239 (= R244), H321 (= H328), D332 (≠ G338)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (≠ D8), S100 (= S101), T298 (≠ V305), G299 (= G306), H300 (≠ D307), E317 (= E324), S319 (= S326), H321 (= H328), R413 (= R409), S415 (= S411)
- binding zinc ion: S100 (= S101), D234 (= D239), D236 (= D241), D238 (= D243)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
30% identity, 98% coverage: 4:441/446 of query aligns to 5:445/455 of 1p5gX
- active site: R12 (= R11), S100 (= S101), H101 (= H102), K110 (= K111), D234 (= D239), D236 (= D241), D238 (= D243), R239 (= R244), H321 (= H328), D332 (≠ G338)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (≠ D8), S100 (= S101), K277 (≠ L287), G299 (= G306), H300 (≠ D307), E317 (= E324), S319 (= S326), H321 (= H328), R413 (= R409), S415 (= S411), N416 (≠ G412), T417 (= T413)
- binding zinc ion: S100 (= S101), D234 (= D239), D236 (= D241), D238 (= D243)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
30% identity, 98% coverage: 4:441/446 of query aligns to 5:445/455 of 1p5dX
- active site: R12 (= R11), S100 (= S101), H101 (= H102), K110 (= K111), D234 (= D239), D236 (= D241), D238 (= D243), R239 (= R244), H321 (= H328), D332 (≠ G338)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (≠ D8), S100 (= S101), R239 (= R244), T298 (≠ V305), G299 (= G306), H300 (≠ D307), E317 (= E324), S319 (= S326), H321 (= H328), R413 (= R409), S415 (= S411), T417 (= T413)
- binding zinc ion: S100 (= S101), D234 (= D239), D236 (= D241), D238 (= D243)
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
30% identity, 98% coverage: 4:441/446 of query aligns to 8:448/458 of 1pcjX
- active site: R15 (= R11), S103 (= S101), H104 (= H102), K113 (= K111), D237 (= D239), D239 (= D241), D241 (= D243), R242 (= R244), H324 (= H328), D335 (≠ G338)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (≠ D8), S103 (= S101), T301 (≠ V305), G302 (= G306), E320 (= E324), S322 (= S326), H324 (= H328), R416 (= R409), S418 (= S411), N419 (≠ G412), T420 (= T413)
- binding zinc ion: S103 (= S101), D237 (= D239), D239 (= D241), D241 (= D243)
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)
30% identity, 98% coverage: 4:441/446 of query aligns to 13:453/463 of P26276
- R15 (≠ G6) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (≠ D8) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- R20 (= R11) 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 (= D239) binding Mg(2+)
- D244 (= D241) binding Mg(2+)
- D246 (= D243) binding Mg(2+)
- R247 (= R244) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ V259) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ L287) 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 (≠ EQSGH 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 (vs. gap) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R409) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RPSGT 409:413) 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)
30% identity, 98% coverage: 4:441/446 of query aligns to 13:453/463 of Q02E40
- S108 (= S101) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
30% identity, 98% coverage: 4:441/446 of query aligns to 9:449/459 of 1k2yX
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
30% identity, 98% coverage: 4:441/446 of query aligns to 9:449/459 of 4il8A
- active site: R16 (= R11), S104 (= S101), H105 (= H102), K114 (= K111), D238 (= D239), D240 (= D241), D242 (= D243), R243 (= R244), A325 (≠ H328), D336 (≠ G338)
- binding magnesium ion: S104 (= S101), D238 (= D239), D240 (= D241), D242 (= D243)
3rsmA Crystal structure of s108c mutant of pmm/pgm (see paper)
29% identity, 95% coverage: 18:441/446 of query aligns to 6:426/436 of 3rsmA
- active site: C87 (≠ D107), K91 (= K111), D215 (= D239), D217 (= D241), D219 (= D243), R220 (= R244), H302 (= H328), D313 (≠ G338)
- binding phosphate ion: C87 (≠ D107), D215 (= D239), D217 (= D241), D219 (= D243), R220 (= R244)
- binding zinc ion: D215 (= D239), D217 (= D241), D219 (= D243)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
29% identity, 95% coverage: 5:429/446 of query aligns to 6:432/448 of 6nqhA
- active site: R12 (= R11), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D239), D239 (= D241), D241 (= D243), R242 (= R244), H324 (= H328)
- binding magnesium ion: D237 (= D239), D239 (= D241), D241 (= D243)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R11), S97 (= S101), H98 (= H102), K107 (= K111), D239 (= D241), R242 (= R244), R280 (vs. gap), S301 (≠ V305), G302 (= G306), E320 (= E324), S322 (= S326), H324 (= H328), R414 (= R409), S416 (= S411), N417 (≠ G412), T418 (= T413), R423 (= R418)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
29% identity, 95% coverage: 5:429/446 of query aligns to 6:432/448 of 6np8A
- active site: R12 (= R11), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D239), D239 (= D241), D241 (= D243), R242 (= R244), H324 (= H328)
- binding calcium ion: S97 (= S101), D237 (= D239), D239 (= D241), D241 (= D243)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (≠ D8), R280 (vs. gap), G302 (= G306), H303 (≠ D307), E320 (= E324), S322 (= S326), H324 (= H328), R414 (= R409), S416 (= S411), N417 (≠ G412), T418 (= T413), R423 (= R418)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
29% identity, 95% coverage: 5:429/446 of query aligns to 6:432/448 of 6nolA
- active site: R12 (= R11), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D239), D239 (= D241), D241 (= D243), R242 (= R244), H324 (= H328)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G306), E320 (= E324), S322 (= S326), H324 (= H328), R414 (= R409), S416 (= S411), N417 (≠ G412), T418 (= T413), R423 (= R418)
- binding magnesium ion: S97 (= S101), D237 (= D239), D239 (= D241), D241 (= D243)
Query Sequence
>WP_052664356.1 NCBI__GCF_000969705.1:WP_052664356.1
MGRIFGTDGIRGKANVDLTPELAISVGRALGTVLHEGGSKRPTVLIGRDPRWSGEMLDAA
LIAGLTSAGADAVSVSVVPTPAVAYLTKRSAAAAGVMISASHNPVGDNGIKIFGPDGYKL
SDEEEERLEELMDSDAARRPTGTGVGRRLRDPAAVSRYIEHIVGLAHVDLTGLRVVVDGA
NGAASSIAPQVYRQLGAEVITIHCTPDGENINAACGSTYPDVIAQAVLAHDADAGISHDG
DADRLIAATHEGAEIDGDVILAVLARQMHHQGTLAENAVATTVMTNLGFKRAMAGLGVEV
VETAVGDRYVLEAMRERGLNLGGEQSGHLIALDHATTGDGILSAVQLLSVVRSTGASLKE
LATVMTRLPQVLVNVRGVDRAGLPDADAIWEVVRSEEERLGDGGRVLLRPSGTEPIVRVM
AEAETEDDAQRAVDVIADAVRDHLTV
Or try a new SitesBLAST search
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