SitesBLAST
Comparing Synpcc7942_2132 FitnessBrowser__SynE:Synpcc7942_2132 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)
42% identity, 94% coverage: 27:471/472 of query aligns to 4:444/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
42% identity, 94% coverage: 27:471/472 of query aligns to 4:444/445 of 7ojrA
P31120 Phosphoglucosamine mutase; EC 5.4.2.10 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 92% coverage: 27:459/472 of query aligns to 7:434/445 of P31120
- S100 (= S121) 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 (= S123) 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
37% identity, 94% coverage: 27:472/472 of query aligns to 3:441/441 of 3i3wA
- active site: R9 (= R33), S99 (= S123), H100 (= H124), K109 (= K133), D237 (= D262), D239 (= D264), D241 (= D266), R242 (= R267), H324 (= H351)
- binding zinc ion: S99 (= S123), D237 (= D262), D239 (= D264), D241 (= D266)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
32% identity, 94% coverage: 26:471/472 of query aligns to 4:454/455 of 1wqaA
- active site: R11 (= R33), S101 (= S123), H102 (= H124), K111 (= K133), D243 (= D262), D245 (= D264), D247 (= D266), R248 (= R267), G330 (≠ H351), R340 (≠ G361)
- binding magnesium ion: S101 (= S123), D243 (= D262), D245 (= D264), D247 (= D266)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
31% identity, 90% coverage: 24:449/472 of query aligns to 3:427/448 of 6nqhA
- active site: R12 (= R33), S97 (= S123), H98 (= H124), K107 (= K133), D237 (= D262), D239 (= D264), D241 (= D266), R242 (= R267), H324 (= H351)
- binding magnesium ion: D237 (= D262), D239 (= D264), D241 (= D266)
- binding 1-O-phosphono-alpha-D-xylopyranose: R12 (= R33), S97 (= S123), H98 (= H124), K107 (= K133), D239 (= D264), R242 (= R267), R280 (≠ M307), S301 (≠ V328), G302 (= G329), E320 (= E347), S322 (= S349), H324 (= H351), R414 (= R436), S416 (= S438), N417 (≠ G439), T418 (= T440), R423 (= R445)
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
31% identity, 90% coverage: 24:449/472 of query aligns to 3:427/448 of 6np8A
- active site: R12 (= R33), S97 (= S123), H98 (= H124), K107 (= K133), D237 (= D262), D239 (= D264), D241 (= D266), R242 (= R267), H324 (= H351)
- binding calcium ion: S97 (= S123), D237 (= D262), D239 (= D264), D241 (= D266)
- binding 6-O-phosphono-alpha-D-mannopyranose: Y9 (≠ D30), R280 (≠ M307), G302 (= G329), H303 (≠ D330), E320 (= E347), S322 (= S349), H324 (= H351), R414 (= R436), S416 (= S438), N417 (≠ G439), T418 (= T440), R423 (= R445)
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
31% identity, 90% coverage: 24:449/472 of query aligns to 3:427/448 of 6nolA
- active site: R12 (= R33), S97 (= S123), H98 (= H124), K107 (= K133), D237 (= D262), D239 (= D264), D241 (= D266), R242 (= R267), H324 (= H351)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G329), E320 (= E347), S322 (= S349), H324 (= H351), R414 (= R436), S416 (= S438), N417 (≠ G439), T418 (= T440), R423 (= R445)
- binding magnesium ion: S97 (= S123), D237 (= D262), D239 (= D264), D241 (= D266)
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
31% identity, 90% coverage: 24:449/472 of query aligns to 3:427/448 of 6nnpA
- active site: R12 (= R33), S97 (= S123), H98 (= H124), K107 (= K133), D237 (= D262), D239 (= D264), D241 (= D266), R242 (= R267), H324 (= H351)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ M307), G302 (= G329), H303 (≠ D330), E320 (= E347), H324 (= H351), R414 (= R436), S416 (= S438), N417 (≠ G439), T418 (= T440), R423 (= R445)
- binding magnesium ion: S97 (= S123), D237 (= D262), D239 (= D264), D241 (= D266)
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
31% identity, 90% coverage: 24:449/472 of query aligns to 3:427/448 of 6nn2A
- active site: R12 (= R33), S97 (= S123), H98 (= H124), K107 (= K133), D237 (= D262), D239 (= D264), D241 (= D266), R242 (= R267), H324 (= H351)
- binding calcium ion: S97 (= S123), D237 (= D262), D239 (= D264), D241 (= D266)
6n1eA Crystal structure of x. Citri phosphoglucomutase in complex with 1- methyl-glucose 6-phosphate (see paper)
31% identity, 90% coverage: 24:449/472 of query aligns to 3:427/448 of 6n1eA
6mnvA Crystal structure of x. Citri phosphoglucomutase in complex with ch2fg1p (see paper)
31% identity, 90% coverage: 24:449/472 of query aligns to 3:427/448 of 6mnvA
- binding 1-deoxy-1-fluoro-2-O-phosphono-alpha-D-gluco-hept-2-ulopyranose: R280 (≠ M307), G302 (= G329), E320 (= E347), S322 (= S349), H324 (= H351), R414 (= R436), S416 (= S438), N417 (≠ G439), T418 (= T440), R423 (= R445)
- binding magnesium ion: S97 (= S123), D237 (= D262), D239 (= D264), D241 (= D266)
6mlhA Crystal structure of x. Citri phosphoglucomutase in complex with glucopyranosyl-1-methyl-phosphonic acid (see paper)
31% identity, 90% coverage: 24:449/472 of query aligns to 3:427/448 of 6mlhA
- active site: R12 (= R33), S97 (= S123), H98 (= H124), K107 (= K133), D237 (= D262), D239 (= D264), D241 (= D266), R242 (= R267), H324 (= H351)
- binding (1S)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: R280 (≠ M307), G302 (= G329), E320 (= E347), H324 (= H351), R414 (= R436), S416 (= S438), N417 (≠ G439), T418 (= T440), R423 (= R445)
- binding magnesium ion: S97 (= S123), D237 (= D262), D239 (= D264), D241 (= D266)
6mlfA Crystal structure of x. Citri phosphoglucomutase in complex with 6- fluoro glucose 1-phosphate (see paper)
31% identity, 90% coverage: 24:449/472 of query aligns to 3:427/448 of 6mlfA
- active site: R12 (= R33), S97 (= S123), H98 (= H124), K107 (= K133), D237 (= D262), D239 (= D264), D241 (= D266), R242 (= R267), H324 (= H351)
- binding 6-deoxy-6-fluoro-1-O-phosphono-alpha-D-glucopyranose: R280 (≠ M307), G302 (= G329), E320 (= E347), H324 (= H351), R414 (= R436), S416 (= S438), T418 (= T440), R423 (= R445)
- binding magnesium ion: S97 (= S123), D237 (= D262), D239 (= D264), D241 (= D266)
5kl0A Crystal structure of phosphoglucomutase from xanthomonas citri citri complexed with glucose-1,6-biphosphate (see paper)
31% identity, 90% coverage: 24:449/472 of query aligns to 3:427/448 of 5kl0A
- active site: R12 (= R33), S97 (= S123), H98 (= H124), K107 (= K133), D237 (= D262), D239 (= D264), D241 (= D266), R242 (= R267), H324 (= H351)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: S97 (= S123), G302 (= G329), H303 (≠ D330), E320 (= E347), H324 (= H351), R414 (= R436), S416 (= S438), N417 (≠ G439), R423 (= R445)
- binding magnesium ion: S97 (= S123), D237 (= D262), D239 (= D264), D241 (= D266)
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
31% identity, 90% coverage: 24:449/472 of query aligns to 4:428/449 of 6mlwA
- active site: R13 (= R33), S98 (= S123), H99 (= H124), K108 (= K133), D238 (= D262), D240 (= D264), D242 (= D266), R243 (= R267), H325 (= H351)
- binding 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol: G303 (= G329), H304 (≠ D330), E321 (= E347), S323 (= S349), H325 (= H351), R415 (= R436), S417 (= S438), N418 (≠ G439), T419 (= T440), R424 (= R445)
- binding magnesium ion: S98 (= S123), D238 (= D262), D240 (= D264), D242 (= D266)
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
31% identity, 90% coverage: 24:449/472 of query aligns to 4:428/449 of 5bmpA
- active site: R13 (= R33), S98 (= S123), H99 (= H124), K108 (= K133), D238 (= D262), D240 (= D264), D242 (= D266), R243 (= R267), H325 (= H351)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ M307), G303 (= G329), E321 (= E347), S323 (= S349), H325 (= H351), R415 (= R436), S417 (= S438), N418 (≠ G439), T419 (= T440), R424 (= R445)
- binding magnesium ion: S98 (= S123), D238 (= D262), D240 (= D264), D242 (= D266)
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, 92% coverage: 26:461/472 of query aligns to 13:446/463 of P26276
- R15 (≠ G28) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold.
- Y17 (≠ D30) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- R20 (= R33) mutation to A: No phosphoglucomutase activity.
- S108 (= S123) 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 (= N125) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D262) binding Mg(2+)
- D244 (= D264) binding Mg(2+)
- D246 (= D266) binding Mg(2+)
- R247 (= R267) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ H282) mutation to A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region.
- K285 (≠ M307) binding alpha-D-glucose 1-phosphate
- H308 (≠ D330) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- E325 (= E347) mutation to A: Reduces KM and Vmax approximately 2-fold.
- EMSGH 325:329 (≠ EQSGH 347:351) binding alpha-D-glucose 1-phosphate; binding alpha-D-mannose 1-phosphate
- H329 (= H351) mutation to A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure.
- P368 (= P393) mutation to G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact.
- R421 (= R436) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RASGT 436:440) 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, 92% coverage: 26:461/472 of query aligns to 13:446/463 of Q02E40
- S108 (= S123) active site, Non-phosphorylated intermediate; modified: Phosphoserine
2h5aX Complex of the enzyme pmm/pgm with xylose 1-phosphate (see paper)
29% identity, 92% coverage: 26:461/472 of query aligns to 5:438/455 of 2h5aX
- active site: H101 (= H124), D234 (= D262), D236 (= D264), D238 (= D266), R239 (= R267), D332 (≠ G361)
- binding 1-O-phosphono-alpha-D-xylopyranose: Y9 (≠ D30), T298 (≠ V328), G299 (= G329), H300 (≠ D330), E317 (= E347), S319 (= S349), H321 (= H351), R413 (= R436), S415 (= S438), N416 (≠ G439), T417 (= T440)
- binding zinc ion: S100 (= S123), D234 (= D262), D236 (= D264), D238 (= D266)
Query Sequence
>Synpcc7942_2132 FitnessBrowser__SynE:Synpcc7942_2132
MVSATRWETAIEVTPWIAAIAEQVPLFGTDGIRGRVGEHLTAPLAQQVGFWTGQVLRQAG
GDRGPVVVGQDSRNSSNMLAMALSSGLAAAGVEVLHLGLCPTPGVAYLTHHSEAIGGVMI
SASHNPPGDNGIKVFGADGSKLDRQLQAAIEAGLRGQQTSLPATTWGQHYYQPQLADHYQ
AAIAQSLGQRANLQGLKIVLDLAWGAAALLAPRLFRELGAEVIALHDLPDGNQINVNCGS
THLARLQAAVLEQGADMGFAFDGDADRVLAVDGRGRSVDGDHILFLWGRELEQQQQLPGQ
AIVTTVMANLGFERAWQAVGGEFVRTAVGDQYVQAEMQARGAMLGGEQSGHILCRHYALT
GDGTLTAAHVAALVQASGVSLADLVDQSFRPYPQLLRNVRVEDRDRRCNWQNCAALTQAI
AAAETDMGDRGRVLVRASGTEPLLRIMVEAEEAQQVEHWTTHLVQVAESHLL
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