SitesBLAST
Comparing 206723 MicrobesOnline__882:206723 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)
44% identity, 99% coverage: 4:449/450 of query aligns to 2:444/445 of 7omlA
7ojrA Bacillus subtilis phosphoglucomutase glmm (phosphate bound) (see paper)
44% identity, 99% coverage: 4:449/450 of query aligns to 2:444/445 of 7ojrA
P31120 Phosphoglucosamine mutase; EC 5.4.2.10 from Escherichia coli (strain K12) (see 3 papers)
49% identity, 99% coverage: 3:446/450 of query aligns to 4:443/445 of P31120
- S100 (= S100) 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 (= S102) 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, 99% coverage: 4:449/450 of query aligns to 1:440/441 of 3i3wA
- active site: R9 (= R12), S99 (= S102), H100 (= H103), K109 (= K112), D237 (= D244), D239 (= D246), D241 (= D248), R242 (= R249), H324 (= H333)
- binding zinc ion: S99 (= S102), D237 (= D244), D239 (= D246), D241 (= D248)
1wqaA Crystal structure of pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with mg2+
34% identity, 99% coverage: 4:449/450 of query aligns to 3:454/455 of 1wqaA
- active site: R11 (= R12), S101 (= S102), H102 (= H103), K111 (= K112), D243 (= D244), D245 (= D246), D247 (= D248), R248 (= R249), G330 (≠ H333), R340 (≠ G343)
- binding magnesium ion: S101 (= S102), D243 (= D244), D245 (= D246), D247 (= D248)
6nqhA Xanthomonas citri dephospho-pgm in complex with xylose-1-phosphate
30% identity, 91% coverage: 20:427/450 of query aligns to 19:427/448 of 6nqhA
- active site: S97 (= S102), H98 (= H103), K107 (= K112), D237 (= D244), D239 (= D246), D241 (= D248), R242 (= R249), H324 (= H333)
- binding magnesium ion: D237 (= D244), D239 (= D246), D241 (= D248)
- binding 1-O-phosphono-alpha-D-xylopyranose: S97 (= S102), H98 (= H103), K107 (= K112), D239 (= D246), R242 (= R249), R280 (≠ M289), S301 (≠ V310), G302 (= G311), E320 (= E329), S322 (= S331), H324 (= H333), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
Sites not aligning to the query:
6np8A Xanthomonas citri phospho-pgm in complex with mannose-6-phosphate (see paper)
30% identity, 91% coverage: 20:427/450 of query aligns to 19:427/448 of 6np8A
- active site: S97 (= S102), H98 (= H103), K107 (= K112), D237 (= D244), D239 (= D246), D241 (= D248), R242 (= R249), H324 (= H333)
- binding calcium ion: S97 (= S102), D237 (= D244), D239 (= D246), D241 (= D248)
- binding 6-O-phosphono-alpha-D-mannopyranose: R280 (≠ M289), G302 (= G311), H303 (≠ D312), E320 (= E329), S322 (= S331), H324 (= H333), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
Sites not aligning to the query:
6nolA Xanthomonas citri dephospho-pgm in complex with mannose-1-phosphate (see paper)
30% identity, 91% coverage: 20:427/450 of query aligns to 19:427/448 of 6nolA
- active site: S97 (= S102), H98 (= H103), K107 (= K112), D237 (= D244), D239 (= D246), D241 (= D248), R242 (= R249), H324 (= H333)
- binding 1-O-phosphono-alpha-D-mannopyranose: G302 (= G311), E320 (= E329), S322 (= S331), H324 (= H333), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S102), D237 (= D244), D239 (= D246), D241 (= D248)
Sites not aligning to the query:
6nnpA Xanthomonas citri dephospho-pgm in complex with glucose-6-phosphate (see paper)
30% identity, 91% coverage: 20:427/450 of query aligns to 19:427/448 of 6nnpA
- active site: S97 (= S102), H98 (= H103), K107 (= K112), D237 (= D244), D239 (= D246), D241 (= D248), R242 (= R249), H324 (= H333)
- binding 6-O-phosphono-alpha-D-glucopyranose: R280 (≠ M289), G302 (= G311), H303 (≠ D312), E320 (= E329), H324 (= H333), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S102), D237 (= D244), D239 (= D246), D241 (= D248)
Sites not aligning to the query:
6nn2A Xanthomonas citri pgm apo-phospho (see paper)
30% identity, 91% coverage: 20:427/450 of query aligns to 19:427/448 of 6nn2A
- active site: S97 (= S102), H98 (= H103), K107 (= K112), D237 (= D244), D239 (= D246), D241 (= D248), R242 (= R249), H324 (= H333)
- binding calcium ion: S97 (= S102), D237 (= D244), D239 (= D246), D241 (= D248)
Sites not aligning to the query:
6n1eA Crystal structure of x. Citri phosphoglucomutase in complex with 1- methyl-glucose 6-phosphate (see paper)
30% identity, 91% coverage: 20:427/450 of query aligns to 19:427/448 of 6n1eA
6mnvA Crystal structure of x. Citri phosphoglucomutase in complex with ch2fg1p (see paper)
30% identity, 91% coverage: 20:427/450 of query aligns to 19:427/448 of 6mnvA
- binding 1-deoxy-1-fluoro-2-O-phosphono-alpha-D-gluco-hept-2-ulopyranose: R280 (≠ M289), G302 (= G311), E320 (= E329), S322 (= S331), H324 (= H333), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S102), D237 (= D244), D239 (= D246), D241 (= D248)
6mlhA Crystal structure of x. Citri phosphoglucomutase in complex with glucopyranosyl-1-methyl-phosphonic acid (see paper)
30% identity, 91% coverage: 20:427/450 of query aligns to 19:427/448 of 6mlhA
- active site: S97 (= S102), H98 (= H103), K107 (= K112), D237 (= D244), D239 (= D246), D241 (= D248), R242 (= R249), H324 (= H333)
- binding (1S)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: R280 (≠ M289), G302 (= G311), E320 (= E329), H324 (= H333), R414 (= R414), S416 (= S416), N417 (≠ G417), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S102), D237 (= D244), D239 (= D246), D241 (= D248)
Sites not aligning to the query:
6mlfA Crystal structure of x. Citri phosphoglucomutase in complex with 6- fluoro glucose 1-phosphate (see paper)
30% identity, 91% coverage: 20:427/450 of query aligns to 19:427/448 of 6mlfA
- active site: S97 (= S102), H98 (= H103), K107 (= K112), D237 (= D244), D239 (= D246), D241 (= D248), R242 (= R249), H324 (= H333)
- binding 6-deoxy-6-fluoro-1-O-phosphono-alpha-D-glucopyranose: R280 (≠ M289), G302 (= G311), E320 (= E329), H324 (= H333), R414 (= R414), S416 (= S416), T418 (= T418), R423 (= R423)
- binding magnesium ion: S97 (= S102), D237 (= D244), D239 (= D246), D241 (= D248)
Sites not aligning to the query:
5kl0A Crystal structure of phosphoglucomutase from xanthomonas citri citri complexed with glucose-1,6-biphosphate (see paper)
30% identity, 91% coverage: 20:427/450 of query aligns to 19:427/448 of 5kl0A
- active site: S97 (= S102), H98 (= H103), K107 (= K112), D237 (= D244), D239 (= D246), D241 (= D248), R242 (= R249), H324 (= H333)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: S97 (= S102), G302 (= G311), H303 (≠ D312), E320 (= E329), H324 (= H333), R414 (= R414), S416 (= S416), N417 (≠ G417), R423 (= R423)
- binding magnesium ion: S97 (= S102), D237 (= D244), D239 (= D246), D241 (= D248)
Sites not aligning to the query:
6mlwA Crystal structure of x. Citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid (see paper)
30% identity, 91% coverage: 20:427/450 of query aligns to 20:428/449 of 6mlwA
- active site: S98 (= S102), H99 (= H103), K108 (= K112), D238 (= D244), D240 (= D246), D242 (= D248), R243 (= R249), 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 (= R414), S417 (= S416), N418 (≠ G417), T419 (= T418), R424 (= R423)
- binding magnesium ion: S98 (= S102), D238 (= D244), D240 (= D246), D242 (= D248)
Sites not aligning to the query:
5bmpA Crystal structure of phosphoglucomutase from xanthomonas citri complexed with glucose-1-phosphate (see paper)
30% identity, 91% coverage: 20:427/450 of query aligns to 20:428/449 of 5bmpA
- active site: S98 (= S102), H99 (= H103), K108 (= K112), D238 (= D244), D240 (= D246), D242 (= D248), R243 (= R249), H325 (= H333)
- binding 1-O-phosphono-alpha-D-glucopyranose: R281 (≠ M289), G303 (= G311), E321 (= E329), S323 (= S331), H325 (= H333), R415 (= R414), S417 (= S416), N418 (≠ G417), T419 (= T418), R424 (= R423)
- binding magnesium ion: S98 (= S102), D238 (= D244), D240 (= D246), D242 (= D248)
Sites not aligning to the query:
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, 94% coverage: 20:441/450 of query aligns to 27:448/463 of P26276
- S108 (= S102) 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 (= N104) mutation to A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold.
- D242 (= D244) binding
- D244 (= D246) binding
- D246 (= D248) binding
- R247 (= R249) mutation to A: Small reduction in KM, small increase in dissociation of G1,6P intermediate.
- R262 (≠ Q264) 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 (≠ EQSGH 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 (= R414) mutation to C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity.
- RASNT 421:425 (≠ RYSGT 414:418) 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
- 20 R→A: No phosphoglucomutase activity.
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, 94% coverage: 20:441/450 of query aligns to 27:448/463 of Q02E40
- S108 (= S102) active site, Non-phosphorylated intermediate; modified: Phosphoserine
1pcjX Enzyme-ligand complex of p. Aeruginosa pmm/pgm (see paper)
28% identity, 94% coverage: 20:441/450 of query aligns to 22:443/458 of 1pcjX
- active site: S103 (= S102), H104 (= H103), K113 (= K112), D237 (= D244), D239 (= D246), D241 (= D248), R242 (= R249), H324 (= H333), D335 (≠ G343)
- binding 1-O-phosphono-alpha-D-mannopyranose: S103 (= S102), T301 (≠ V310), G302 (= G311), E320 (= E329), S322 (= S331), H324 (= H333), R416 (= R414), S418 (= S416), N419 (≠ G417), T420 (= T418)
- binding zinc ion: S103 (= S102), D237 (= D244), D239 (= D246), D241 (= D248)
Sites not aligning to the query:
Query Sequence
>206723 MicrobesOnline__882:206723
MGRRLFGTDGLRGQVNIYPMTADMALRLGLAAGTRFRNGNRRHRVVIGKDTRLSGYMFES
ALTAGLCAAGMDVFQVGPLPTPAISFLTRNMRADLGVVISASHNPFMDNGIKFFDRSGFK
LPDDVENQMTDMVLDPDWQWDYPASEKVGRAYKIADAPGRYIVYIKSSFPADLTLDGLRV
VIDCANGANYKVAPLALEELGAEVIKLGTEPNGLNINHQCGSLYPEVVAAKVRETRADIG
LALDGDADRLIVVDEKGTILDGDQIMALCAQDLMAKGKLPGNMLVATVMSNMALEVFMKE
HGGTLLRTAVGDRYVVEAMRQHGALLGGEQSGHLIFREYSTTGDGLLAALQILRIMRERG
KPLSELAGQLQLFPQQLINVHVERKIPFAECQPVADAVAAIETELGDRGRVLLRYSGTES
VCRVMVEGEHPEQVARLAEMLAETVQKHLR
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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