SitesBLAST
Comparing Ga0059261_1954 FitnessBrowser__Korea:Ga0059261_1954 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)
P31120 Phosphoglucosamine mutase; EC 5.4.2.10 from Escherichia coli (strain K12) (see 3 papers)
54% identity, 96% coverage: 18:458/461 of query aligns to 4:444/445 of P31120
- S100 (= S115) 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 (= S117) 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)
48% identity, 95% coverage: 19:458/461 of query aligns to 2:442/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
48% identity, 95% coverage: 19:458/461 of query aligns to 2:442/445 of 7ojrA
3i3wA Structure of a phosphoglucosamine mutase from francisella tularensis
41% identity, 94% coverage: 19:452/461 of query aligns to 1:436/441 of 3i3wA
- active site: R9 (= R27), S99 (= S117), H100 (= H118), K109 (= K127), D237 (= D256), D239 (= D258), D241 (= D260), R242 (= R261), H324 (= H345)
- binding zinc ion: S99 (= S117), D237 (= D256), D239 (= D258), D241 (= D260)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
35% identity, 94% coverage: 19:450/461 of query aligns to 3:444/455 of 1wqaA
- active site: R11 (= R27), S101 (= S117), H102 (= H118), K111 (= K127), D243 (= D256), D245 (= D258), D247 (= D260), R248 (= R261), G330 (≠ H345), R340 (≠ G355)
- binding magnesium ion: S101 (= S117), D243 (= D256), D245 (= D258), D247 (= D260)
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)
28% identity, 98% coverage: 9:459/461 of query aligns to 2:458/463 of P26276
- R15 (≠ G22) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (≠ D24) binding ; binding
- R20 (= R27) mutation to A: No phosphoglucomutase activity.
- S108 (= S117) 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 (= N119) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D256) binding
- D244 (= D258) binding
- D246 (= D260) binding
- R247 (= R261) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Q276) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ M301) binding
- H308 (≠ D324) binding ; binding
- E325 (= E341) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ EQSGH 341:345) binding ; binding
- H329 (= H345) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P386) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R425) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RASGT 425:429) 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)
28% identity, 98% coverage: 9:459/461 of query aligns to 2:458/463 of Q02E40
- S108 (= S117) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
28% identity, 94% coverage: 26:459/461 of query aligns to 14:453/458 of 1pcjX
- active site: R15 (= R27), S103 (= S117), H104 (= H118), K113 (= K127), D237 (= D256), D239 (= D258), D241 (= D260), R242 (= R261), H324 (= H345), D335 (≠ G355)
- binding 1-O-phosphono-alpha-D-mannopyranose: S103 (= S117), T301 (≠ V322), G302 (= G323), E320 (= E341), S322 (= S343), H324 (= H345), R416 (= R425), S418 (= S427), N419 (≠ G428), T420 (= T429)
- binding zinc ion: S103 (= S117), D237 (= D256), D239 (= D258), D241 (= D260)
Sites not aligning to the query:
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
28% identity, 94% coverage: 26:459/461 of query aligns to 11:450/455 of 2h5aX
- active site: H101 (= H118), D234 (= D256), D236 (= D258), D238 (= D260), R239 (= R261), D332 (≠ G355)
- binding 1-O-phosphono-alpha-D-xylopyranose: T298 (≠ V322), G299 (= G323), H300 (≠ D324), E317 (= E341), S319 (= S343), H321 (= H345), R413 (= R425), S415 (= S427), N416 (≠ G428), T417 (= T429)
- binding zinc ion: S100 (= S117), D234 (= D256), D236 (= D258), D238 (= D260)
Sites not aligning to the query:
2h4lX Complex of pmm/pgm with ribose 1-phosphate (see paper)
28% identity, 94% coverage: 26:459/461 of query aligns to 11:450/455 of 2h4lX
- active site: H101 (= H118), D234 (= D256), D236 (= D258), D238 (= D260), R239 (= R261), D332 (≠ G355)
- binding 1-O-phosphono-alpha-D-ribofuranose: R12 (= R27), S100 (= S117), T298 (≠ V322), E317 (= E341), R413 (= R425), S415 (= S427), N416 (≠ G428), T417 (= T429)
- binding zinc ion: S100 (= S117), D234 (= D256), D236 (= D258), D238 (= D260)
Sites not aligning to the query:
2fkfA Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound (see paper)
28% identity, 94% coverage: 26:459/461 of query aligns to 11:450/455 of 2fkfA
- active site: R12 (= R27), S100 (= S117), H101 (= H118), K110 (= K127), D234 (= D256), D236 (= D258), D238 (= D260), R239 (= R261), H321 (= H345), D332 (≠ G355)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: H101 (= H118), S319 (= S343), R413 (= R425), S415 (= S427), N416 (≠ G428), T417 (= T429)
- binding zinc ion: S100 (= S117), D234 (= D256), D236 (= D258), D238 (= D260)
Sites not aligning to the query:
1pcmX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
28% identity, 94% coverage: 26:459/461 of query aligns to 11:450/455 of 1pcmX
- active site: R12 (= R27), S100 (= S117), H101 (= H118), K110 (= K127), D234 (= D256), D236 (= D258), D238 (= D260), R239 (= R261), H321 (= H345), D332 (≠ G355)
- binding 6-O-phosphono-alpha-D-mannopyranose: S100 (= S117), T298 (≠ V322), G299 (= G323), H300 (≠ D324), E317 (= E341), S319 (= S343), H321 (= H345), R413 (= R425), S415 (= S427)
- binding zinc ion: S100 (= S117), D234 (= D256), D236 (= D258), D238 (= D260)
Sites not aligning to the query:
1p5gX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
28% identity, 94% coverage: 26:459/461 of query aligns to 11:450/455 of 1p5gX
- active site: R12 (= R27), S100 (= S117), H101 (= H118), K110 (= K127), D234 (= D256), D236 (= D258), D238 (= D260), R239 (= R261), H321 (= H345), D332 (≠ G355)
- binding 6-O-phosphono-alpha-D-glucopyranose: S100 (= S117), K277 (≠ M301), G299 (= G323), H300 (≠ D324), E317 (= E341), S319 (= S343), H321 (= H345), R413 (= R425), S415 (= S427), N416 (≠ G428), T417 (= T429)
- binding zinc ion: S100 (= S117), D234 (= D256), D236 (= D258), D238 (= D260)
Sites not aligning to the query:
1p5dX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
28% identity, 94% coverage: 26:459/461 of query aligns to 11:450/455 of 1p5dX
- active site: R12 (= R27), S100 (= S117), H101 (= H118), K110 (= K127), D234 (= D256), D236 (= D258), D238 (= D260), R239 (= R261), H321 (= H345), D332 (≠ G355)
- binding 1-O-phosphono-alpha-D-glucopyranose: S100 (= S117), R239 (= R261), T298 (≠ V322), G299 (= G323), H300 (≠ D324), E317 (= E341), S319 (= S343), H321 (= H345), R413 (= R425), S415 (= S427), T417 (= T429)
- binding zinc ion: S100 (= S117), D234 (= D256), D236 (= D258), D238 (= D260)
Sites not aligning to the query:
1k2yX Crystal structure of phosphomannomutase/phosphoglucomutase s108a mutant from p. Aeruginosa (see paper)
27% identity, 97% coverage: 12:459/461 of query aligns to 1:454/459 of 1k2yX
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
28% identity, 95% coverage: 21:457/461 of query aligns to 6:447/448 of 6nqhA
- active site: R12 (= R27), S97 (= S117), H98 (= H118), K107 (= K127), D237 (= D256), D239 (= D258), D241 (= D260), R242 (= R261), H324 (= H345)
- binding magnesium ion: D237 (= D256), D239 (= D258), D241 (= D260)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R27), S97 (= S117), H98 (= H118), K107 (= K127), D239 (= D258), R242 (= R261), R280 (≠ M301), S301 (≠ V322), G302 (= G323), E320 (= E341), S322 (= S343), H324 (= H345), R414 (= R425), S416 (= S427), N417 (≠ G428), T418 (= T429), R423 (= R434)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
28% identity, 95% coverage: 21:457/461 of query aligns to 6:447/448 of 6np8A
- active site: R12 (= R27), S97 (= S117), H98 (= H118), K107 (= K127), D237 (= D256), D239 (= D258), D241 (= D260), R242 (= R261), H324 (= H345)
- binding calcium ion: S97 (= S117), D237 (= D256), D239 (= D258), D241 (= D260)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (≠ D24), R280 (≠ M301), G302 (= G323), H303 (≠ D324), E320 (= E341), S322 (= S343), H324 (= H345), R414 (= R425), S416 (= S427), N417 (≠ G428), T418 (= T429), R423 (= R434)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
28% identity, 95% coverage: 21:457/461 of query aligns to 6:447/448 of 6nolA
- active site: R12 (= R27), S97 (= S117), H98 (= H118), K107 (= K127), D237 (= D256), D239 (= D258), D241 (= D260), R242 (= R261), H324 (= H345)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G323), E320 (= E341), S322 (= S343), H324 (= H345), R414 (= R425), S416 (= S427), N417 (≠ G428), T418 (= T429), R423 (= R434)
- binding magnesium ion: S97 (= S117), D237 (= D256), D239 (= D258), D241 (= D260)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
28% identity, 95% coverage: 21:457/461 of query aligns to 6:447/448 of 6nnpA
- active site: R12 (= R27), S97 (= S117), H98 (= H118), K107 (= K127), D237 (= D256), D239 (= D258), D241 (= D260), R242 (= R261), H324 (= H345)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ M301), G302 (= G323), H303 (≠ D324), E320 (= E341), H324 (= H345), R414 (= R425), S416 (= S427), N417 (≠ G428), T418 (= T429), R423 (= R434)
- binding magnesium ion: S97 (= S117), D237 (= D256), D239 (= D258), D241 (= D260)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
28% identity, 95% coverage: 21:457/461 of query aligns to 6:447/448 of 6nn2A
- active site: R12 (= R27), S97 (= S117), H98 (= H118), K107 (= K127), D237 (= D256), D239 (= D258), D241 (= D260), R242 (= R261), H324 (= H345)
- binding calcium ion: S97 (= S117), D237 (= D256), D239 (= D258), D241 (= D260)
Query Sequence
>Ga0059261_1954 FitnessBrowser__Korea:Ga0059261_1954
MTACQKGGNVAKQADMARKYFGTDGIRGKTNVTPMTAAMAMQVGMAAGAHFRRGDHKHRV
VIGKDTRLSGYMIENALVAGFTSVGMDVVLVGPMPTPAVAMLTHSMRADMGVMISASHNP
YADNGIKLFGPDGYKLSDADELAIEALIDGEIPLAPAADIGRAKRIEDAKGRYIHFAKST
FPEDLRLDGLKVVVDCANGAAYQVAPSALWELGAEVVAIGVTPDGKNINDQVGSTAPLTL
CETVVASGAHIGIALDGDADRLIVVDEQGEVVDGDQLMATIASGWARQGRLSGGGLVATV
MSNLGLERHLAAQGLGLVRTKVGDRYVLEKMRASGYNVGGEQSGHIILSDYATTGDGLVA
ALQVLAELVRAGAPASEVLHRFDPLPQLLKNVRFSGGKPLENETVKSVIAAAETELDGTG
RVLIRASGTEPVIRVMAEGEDLKQVEAVVDRICDAVRAAAA
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