SitesBLAST
Comparing WP_005808422.1 NCBI__GCF_000021925.1:WP_005808422.1 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)
54% identity, 98% coverage: 8:449/451 of query aligns to 1:443/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
54% identity, 98% coverage: 8:449/451 of query aligns to 1:443/445 of 7ojrA
P31120 Phosphoglucosamine mutase; EC 5.4.2.10 from Escherichia coli (strain K12) (see 3 papers)
49% identity, 97% coverage: 9:447/451 of query aligns to 5:443/445 of P31120
- S100 (= S104) 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 (= S106) 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
42% identity, 98% coverage: 9:449/451 of query aligns to 1:439/441 of 3i3wA
- active site: R9 (= R17), S99 (= S106), H100 (= H107), K109 (= K116), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H334)
- binding zinc ion: S99 (= S106), D237 (= D245), D239 (= D247), D241 (= D249)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
37% identity, 95% coverage: 7:434/451 of query aligns to 1:438/455 of 1wqaA
- active site: R11 (= R17), S101 (= S106), H102 (= H107), K111 (= K116), D243 (= D245), D245 (= D247), D247 (= D249), R248 (= R250), G330 (≠ H334), R340 (≠ G344)
- binding magnesium ion: S101 (= S106), D243 (= D245), D245 (= D247), D247 (= D249)
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
29% identity, 94% coverage: 10:435/451 of query aligns to 8:436/458 of 1pcjX
- active site: R15 (= R17), S103 (= S106), H104 (= H107), K113 (= K116), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H334), D335 (≠ G344)
- binding 1-O-phosphono-alpha-D-mannopyranose: Y12 (≠ D14), S103 (= S106), T301 (≠ V311), G302 (= G312), E320 (= E330), S322 (= S332), H324 (= H334), R416 (= R415), S418 (= S417), N419 (≠ G418), T420 (= T419)
- binding zinc ion: S103 (= S106), D237 (= D245), D239 (= D247), D241 (= D249)
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
29% identity, 94% coverage: 10:435/451 of query aligns to 5:433/455 of 2h5aX
- active site: H101 (= H107), D234 (= D245), D236 (= D247), D238 (= D249), R239 (= R250), D332 (≠ G344)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (≠ D14), T298 (≠ V311), G299 (= G312), H300 (≠ D313), E317 (= E330), S319 (= S332), H321 (= H334), R413 (= R415), S415 (= S417), N416 (≠ G418), T417 (= T419)
- binding zinc ion: S100 (= S106), D234 (= D245), D236 (= D247), D238 (= D249)
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
29% identity, 94% coverage: 10:435/451 of query aligns to 5:433/455 of 2h4lX
- active site: H101 (= H107), D234 (= D245), D236 (= D247), D238 (= D249), R239 (= R250), D332 (≠ G344)
- binding 1-O-phosphono-alpha-D-ribofuranose: Y9 (≠ D14), R12 (= R17), S100 (= S106), T298 (≠ V311), E317 (= E330), R413 (= R415), S415 (= S417), N416 (≠ G418), T417 (= T419)
- binding zinc ion: S100 (= S106), D234 (= D245), D236 (= D247), D238 (= D249)
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
29% identity, 94% coverage: 10:435/451 of query aligns to 5:433/455 of 2fkfA
- active site: R12 (= R17), S100 (= S106), H101 (= H107), K110 (= K116), D234 (= D245), D236 (= D247), D238 (= D249), R239 (= R250), H321 (= H334), D332 (≠ G344)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: R7 (≠ G12), H101 (= H107), S319 (= S332), R413 (= R415), S415 (= S417), N416 (≠ G418), T417 (= T419)
- binding zinc ion: S100 (= S106), D234 (= D245), D236 (= D247), D238 (= D249)
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
29% identity, 94% coverage: 10:435/451 of query aligns to 5:433/455 of 1pcmX
- active site: R12 (= R17), S100 (= S106), H101 (= H107), K110 (= K116), D234 (= D245), D236 (= D247), D238 (= D249), R239 (= R250), H321 (= H334), D332 (≠ G344)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (≠ D14), S100 (= S106), T298 (≠ V311), G299 (= G312), H300 (≠ D313), E317 (= E330), S319 (= S332), H321 (= H334), R413 (= R415), S415 (= S417)
- binding zinc ion: S100 (= S106), D234 (= D245), D236 (= D247), D238 (= D249)
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
29% identity, 94% coverage: 10:435/451 of query aligns to 5:433/455 of 1p5gX
- active site: R12 (= R17), S100 (= S106), H101 (= H107), K110 (= K116), D234 (= D245), D236 (= D247), D238 (= D249), R239 (= R250), H321 (= H334), D332 (≠ G344)
- binding 6-O-phosphono-alpha-D-glucopyranose: Y9 (≠ D14), S100 (= S106), K277 (≠ M290), G299 (= G312), H300 (≠ D313), E317 (= E330), S319 (= S332), H321 (= H334), R413 (= R415), S415 (= S417), N416 (≠ G418), T417 (= T419)
- binding zinc ion: S100 (= S106), D234 (= D245), D236 (= D247), D238 (= D249)
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
29% identity, 94% coverage: 10:435/451 of query aligns to 5:433/455 of 1p5dX
- active site: R12 (= R17), S100 (= S106), H101 (= H107), K110 (= K116), D234 (= D245), D236 (= D247), D238 (= D249), R239 (= R250), H321 (= H334), D332 (≠ G344)
- binding 1-O-phosphono-alpha-D-glucopyranose: Y9 (≠ D14), S100 (= S106), R239 (= R250), T298 (≠ V311), G299 (= G312), H300 (≠ D313), E317 (= E330), S319 (= S332), H321 (= H334), R413 (= R415), S415 (= S417), T417 (= T419)
- binding zinc ion: S100 (= S106), D234 (= D245), D236 (= D247), D238 (= D249)
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: 10:435/451 of query aligns to 13:441/463 of P26276
- R15 (≠ G12) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (≠ D14) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- R20 (= R17) mutation to A: No phosphoglucomutase activity.
- S108 (= S106) 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 (= N108) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D245) binding Mg(2+)
- D244 (= D247) binding Mg(2+)
- D246 (= D249) binding Mg(2+)
- R247 (= R250) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ F265) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ M290) binding alpha-D-glucose 1-phosphate
- H308 (≠ D313) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- E325 (= E330) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ EQSGH 330:334) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- H329 (= H334) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (≠ M371) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R415) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RSSGT 415:419) 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)
29% identity, 94% coverage: 10:435/451 of query aligns to 13:441/463 of Q02E40
- S108 (= S106) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
29% identity, 94% coverage: 10:435/451 of query aligns to 9:437/459 of 1k2yX
4il8A Crystal structure of an h329a mutant of p. Aeruginosa pmm/pgm (see paper)
29% identity, 94% coverage: 10:435/451 of query aligns to 9:437/459 of 4il8A
- active site: R16 (= R17), S104 (= S106), H105 (= H107), K114 (= K116), D238 (= D245), D240 (= D247), D242 (= D249), R243 (= R250), A325 (≠ H334), D336 (≠ G344)
- binding magnesium ion: S104 (= S106), D238 (= D245), D240 (= D247), D242 (= D249)
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
28% identity, 94% coverage: 11:436/451 of query aligns to 7:436/449 of 6mlwA
- active site: R13 (= R17), S98 (= S106), H99 (= H107), K108 (= K116), 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 (= R415), S417 (= S417), N418 (≠ G418), T419 (= T419), R424 (= R424)
- binding magnesium ion: S98 (= S106), D238 (= D245), D240 (= D247), D242 (= D249)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
28% identity, 94% coverage: 11:436/451 of query aligns to 7:436/449 of 5bmpA
- active site: R13 (= R17), S98 (= S106), H99 (= H107), K108 (= K116), D238 (= D245), D240 (= D247), D242 (= D249), R243 (= R250), H325 (= H334)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ V285), G303 (= G312), E321 (= E330), S323 (= S332), H325 (= H334), R415 (= R415), S417 (= S417), N418 (≠ G418), T419 (= T419), R424 (= R424)
- binding magnesium ion: S98 (= S106), D238 (= D245), D240 (= D247), D242 (= D249)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
28% identity, 94% coverage: 11:436/451 of query aligns to 6:435/448 of 6nqhA
- active site: R12 (= R17), S97 (= S106), H98 (= H107), K107 (= K116), 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 (= R17), S97 (= S106), H98 (= H107), K107 (= K116), D239 (= D247), R242 (= R250), R280 (≠ V285), S301 (≠ V311), G302 (= G312), E320 (= E330), S322 (= S332), H324 (= H334), R414 (= R415), S416 (= S417), N417 (≠ G418), T418 (= T419), R423 (= R424)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
28% identity, 94% coverage: 11:436/451 of query aligns to 6:435/448 of 6np8A
- active site: R12 (= R17), S97 (= S106), H98 (= H107), K107 (= K116), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H334)
- binding calcium ion: S97 (= S106), D237 (= D245), D239 (= D247), D241 (= D249)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (≠ D14), R280 (≠ V285), G302 (= G312), H303 (≠ D313), E320 (= E330), S322 (= S332), H324 (= H334), R414 (= R415), S416 (= S417), N417 (≠ G418), T418 (= T419), R423 (= R424)
Query Sequence
>WP_005808422.1 NCBI__GCF_000021925.1:WP_005808422.1
MEGVVYLGKLFGTDGVRGVANKELTPDLAFRLGQAGAYVLSKEHPHPRIVIGKDTRISGD
MLEAALIAGICSVGADVLRVGVLPTPGIAYLTRTLKASAGVVISASHNPVQDNGIKFFSS
TGYKLPDAVEEEIEDLVHSHEKPWAIPVGSEIGRVIEIQDAQRRYMDFLKGTVGSLAGIK
VVYDGSNGAASHVGPQVLRELGVEVIPLSVTPDGININAGCGSTHPEVLQQAVIEHKADL
GLANDGDADRLIAVDENGEIVDGDFIMVICALALKAKGQLMEDSVVVTVMSNLGLHIALK
EAGIRVYETQVGDRYVMEELLKTGARLGGEQSGHIIFLDHNTTGDGLLTALQLLAVLKEQ
GKPISKLAAKMQRLPQVLINVRVKDKKKAMENPYVFQKVEEVKRFLGERGRVLVRSSGTE
SLVRVMVEGQDHEQLMGLAQSVVDIIKREEL
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