SitesBLAST
Comparing 6938122 FitnessBrowser__SB2B:6938122 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)
61% identity, 99% coverage: 2:449/452 of query aligns to 3:445/445 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
7omlA Bacillus subtilis phosphoglucomutase glmm (metal bound) (see paper)
43% identity, 98% coverage: 4:448/452 of query aligns to 2:442/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
43% identity, 98% coverage: 4:448/452 of query aligns to 2:442/445 of 7ojrA
3i3wA Structure of a phosphoglucosamine mutase from francisella tularensis
43% identity, 98% coverage: 4:447/452 of query aligns to 1:437/441 of 3i3wA
- active site: R9 (= R12), S99 (= S101), H100 (= H102), K109 (= K111), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H333)
- binding zinc ion: S99 (= S101), D237 (= D245), D239 (= D247), D241 (= D249)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
34% identity, 97% coverage: 4:441/452 of query aligns to 3:445/455 of 1wqaA
- active site: R11 (= R12), S101 (= S101), H102 (= H102), K111 (= K111), D243 (= D245), D245 (= D247), D247 (= D249), R248 (= R250), G330 (≠ H333), R340 (≠ G343)
- binding magnesium ion: S101 (= S101), D243 (= D245), D245 (= D247), D247 (= D249)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
28% identity, 99% coverage: 1:447/452 of query aligns to 1:447/448 of 6nqhA
- active site: R12 (= R12), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H333)
- binding magnesium ion: D237 (= D245), D239 (= D247), D241 (= D249)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R12), S97 (= S101), H98 (= H102), K107 (= K111), D239 (= D247), R242 (= R250), R280 (≠ L288), S301 (≠ V310), G302 (= G311), E320 (= E329), S322 (= S331), H324 (= H333), 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, 99% coverage: 1:447/452 of query aligns to 1:447/448 of 6np8A
- active site: R12 (= R12), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H333)
- binding calcium ion: S97 (= S101), D237 (= D245), D239 (= D247), D241 (= D249)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (≠ D9), R280 (≠ L288), G302 (= G311), H303 (≠ D312), E320 (= E329), S322 (= S331), H324 (= H333), R414 (= R415), S416 (= S417), N417 (≠ G418), T418 (= T419), R423 (= R424)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
28% identity, 99% coverage: 1:447/452 of query aligns to 1:447/448 of 6nolA
- active site: R12 (= R12), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H333)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G311), E320 (= E329), S322 (= S331), H324 (= H333), R414 (= R415), S416 (= S417), N417 (≠ G418), T418 (= T419), R423 (= R424)
- binding magnesium ion: S97 (= S101), D237 (= D245), D239 (= D247), D241 (= D249)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
28% identity, 99% coverage: 1:447/452 of query aligns to 1:447/448 of 6nnpA
- active site: R12 (= R12), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H333)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ L288), G302 (= G311), H303 (≠ D312), E320 (= E329), H324 (= H333), R414 (= R415), S416 (= S417), N417 (≠ G418), T418 (= T419), R423 (= R424)
- binding magnesium ion: S97 (= S101), D237 (= D245), D239 (= D247), D241 (= D249)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
28% identity, 99% coverage: 1:447/452 of query aligns to 1:447/448 of 6nn2A
- active site: R12 (= R12), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H333)
- binding calcium ion: S97 (= S101), D237 (= D245), D239 (= D247), D241 (= D249)
6n1eA Crystal structure of x. Citri phosphoglucomutase in complex with 1- methyl-glucose 6-phosphate (see paper)
28% identity, 99% coverage: 1:447/452 of query aligns to 1:447/448 of 6n1eA
6mnvA Crystal structure of x. Citri phosphoglucomutase in complex with ch2fg1p (see paper)
28% identity, 99% coverage: 1:447/452 of query aligns to 1:447/448 of 6mnvA
- binding 1-deoxy-1-fluoro-2-O-phosphono-alpha-D-gluco-hept-2-ulopyranose: R280 (≠ L288), G302 (= G311), E320 (= E329), S322 (= S331), H324 (= H333), R414 (= R415), S416 (= S417), N417 (≠ G418), T418 (= T419), R423 (= R424)
- binding magnesium ion: S97 (= S101), D237 (= D245), D239 (= D247), D241 (= D249)
6mlhA Crystal structure of x. Citri phosphoglucomutase in complex with glucopyranosyl-1-methyl-phosphonic acid (see paper)
28% identity, 99% coverage: 1:447/452 of query aligns to 1:447/448 of 6mlhA
- active site: R12 (= R12), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H333)
- binding (1S)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: R280 (≠ L288), G302 (= G311), E320 (= E329), H324 (= H333), R414 (= R415), S416 (= S417), N417 (≠ G418), T418 (= T419), R423 (= R424)
- binding magnesium ion: S97 (= S101), D237 (= D245), D239 (= D247), D241 (= D249)
6mlfA Crystal structure of x. Citri phosphoglucomutase in complex with 6- fluoro glucose 1-phosphate (see paper)
28% identity, 99% coverage: 1:447/452 of query aligns to 1:447/448 of 6mlfA
- active site: R12 (= R12), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H333)
- binding 6-deoxy-6-fluoro-1-O-phosphono-alpha-D-glucopyranose: R280 (≠ L288), G302 (= G311), E320 (= E329), H324 (= H333), R414 (= R415), S416 (= S417), T418 (= T419), R423 (= R424)
- binding magnesium ion: S97 (= S101), D237 (= D245), D239 (= D247), D241 (= D249)
5kl0A Crystal structure of phosphoglucomutase from xanthomonas citri citri complexed with glucose-1,6-biphosphate (see paper)
28% identity, 99% coverage: 1:447/452 of query aligns to 1:447/448 of 5kl0A
- active site: R12 (= R12), S97 (= S101), H98 (= H102), K107 (= K111), D237 (= D245), D239 (= D247), D241 (= D249), R242 (= R250), H324 (= H333)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: S97 (= S101), G302 (= G311), H303 (≠ D312), E320 (= E329), H324 (= H333), R414 (= R415), S416 (= S417), N417 (≠ G418), R423 (= R424)
- binding magnesium ion: S97 (= S101), D237 (= D245), D239 (= D247), D241 (= D249)
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
28% identity, 99% coverage: 1:447/452 of query aligns to 2:448/449 of 6mlwA
- active site: R13 (= R12), S98 (= S101), H99 (= H102), K108 (= K111), D238 (= D245), D240 (= D247), D242 (= D249), R243 (= R250), H325 (= H333)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G311), H304 (≠ D312), E321 (= E329), S323 (= S331), H325 (= H333), R415 (= R415), S417 (= S417), N418 (≠ G418), T419 (= T419), R424 (= R424)
- binding magnesium ion: S98 (= S101), D238 (= D245), D240 (= D247), D242 (= D249)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
28% identity, 99% coverage: 1:447/452 of query aligns to 2:448/449 of 5bmpA
- active site: R13 (= R12), S98 (= S101), H99 (= H102), K108 (= K111), D238 (= D245), D240 (= D247), D242 (= D249), R243 (= R250), H325 (= H333)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ L288), G303 (= G311), E321 (= E329), S323 (= S331), H325 (= H333), R415 (= R415), S417 (= S417), N418 (≠ G418), T419 (= T419), R424 (= R424)
- binding magnesium ion: S98 (= S101), D238 (= D245), D240 (= D247), D242 (= D249)
3uw2A X-ray crystal structure of phosphoglucomutase/phosphomannomutase family protein (bth_i1489)from burkholderia thailandensis (see paper)
29% identity, 95% coverage: 1:429/452 of query aligns to 2:430/458 of 3uw2A
- active site: R13 (= R12), S109 (= S101), H110 (= H102), K119 (= K111), D243 (= D245), D245 (= D247), D247 (= D249), R248 (= R250), H330 (= H333)
- binding zinc ion: D243 (= D245), D245 (= D247), D247 (= 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)
27% identity, 97% coverage: 11:449/452 of query aligns to 19:455/463 of P26276
- R20 (= R12) 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 (= 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 (≠ A265) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ M289) binding
- H308 (≠ D312) binding ; binding
- E325 (= E329) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ ENSGH 329:333) binding ; binding
- H329 (= H333) 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 (= R415) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RKSGT 415:419) 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
Q02E40 Phosphomannomutase/phosphoglucomutase; PMM / PGM; EC 5.4.2.2; EC 5.4.2.8 from Pseudomonas aeruginosa (strain UCBPP-PA14) (see paper)
27% identity, 97% coverage: 11:449/452 of query aligns to 19:455/463 of Q02E40
- S108 (= S101) active site, Non-phosphorylated intermediate; modified: Phosphoserine
Query Sequence
>6938122 FitnessBrowser__SB2B:6938122
MSRKYFGTDGVRGKVGEFPITPDFAMKLGWAAGTVMAASGTKEVIIGKDTRLSGYMLESA
MEAGFCAAGVNVALTGPLPTPAIAYLTSTFRADAGVVISASHNPYYDNGIKFFSNTGTKL
TDEQELEIERLLVSAIEGGAMTCVASDKLGKVRRINDAAGRYIEFCKGTFPNSLSLTGLK
IVVDSAHGAAYHIAKNVYRELGAEVISINDKPDGININEHCGATHMDSLQTAVMIHEADL
GIALDGDADRLMMVDSKGQVIDGDALLYLLAKSAQQRGEQVSGVIGTLMSNLGFEQALAN
LGIPFKRAKVGDRYVVELLKETGWRLGGENSGHLLMLDFTTTGDAIVASLQVLRALLESG
AGLADAITELNMFPQVLINVRLNGNAAVGLSHPSVSDAVATAESALGNDGRVLLRKSGTE
PLIRVMVEAKDAVKANQYAELIADAVRAVFPA
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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