SitesBLAST
Comparing PP_2052 FitnessBrowser__Putida:PP_2052 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)
7ocqA Nadh bound to the dehydrogenase domain of the bifunctional mannitol-1- phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
53% identity, 90% coverage: 1:637/707 of query aligns to 1:642/686 of 7ocqA
- binding magnesium ion: D15 (= D15), D17 (= D17), D175 (= D175)
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(3-aminocarbonyl-4~{H}-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{S},4~{R},5~{R})-3,4,5-tris(oxidanyl)oxolan-2-yl]methyl hydrogen phosphate: G252 (= G252), A253 (= A253), I254 (= I254), T279 (= T279), R280 (= R280), L335 (= L335), L369 (= L368), N370 (= N369)
7ocnA Crystal structure of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
52% identity, 90% coverage: 1:637/707 of query aligns to 1:646/690 of 7ocnA
7ocpA NADPH bound to the dehydrogenase domain of the bifunctional mannitol- 1-phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
52% identity, 90% coverage: 1:637/707 of query aligns to 1:646/688 of 7ocpA
- binding magnesium ion: D15 (= D15), D17 (= D17), D175 (= D175)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G250 (= G250), F251 (= F251), A253 (= A253), I254 (= I254), T279 (= T279), R280 (= R280), C334 (≠ S334), L335 (= L335), P336 (= P336), A339 (= A339), L369 (= L368), N370 (= N369)
7ocsA Mannitol-1-phosphate bound to the phosphatase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase mtld-d16a from acinetobacter baumannii (see paper)
52% identity, 90% coverage: 1:637/707 of query aligns to 1:638/682 of 7ocsA
- binding D-Mannitol-1-phosphate: M16 (= M16), D17 (= D17), E24 (= E24), R27 (= R27), L31 (= L31), C51 (≠ S51), L52 (= L52), L54 (= L54), T117 (= T117), S118 (= S118), K150 (= K150)
- binding magnesium ion: L372 (= L368), T411 (= T406)
7ocrB NADPH and fructose-6-phosphate bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
52% identity, 90% coverage: 1:637/707 of query aligns to 1:631/675 of 7ocrB
- binding fructose -6-phosphate: N362 (= N369), N403 (≠ S409), K508 (= K513), N513 (= N518), H516 (= H521), R587 (= R593), R590 (= R596), R594 (= R600), K595 (= K601), R601 (= R607)
- binding magnesium ion: D15 (= D15), D17 (= D17), D169 (= D175)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G244 (= G250), G246 (= G252), A247 (= A253), I248 (= I254), T273 (= T279), R274 (= R280), L329 (= L335), P330 (= P336), A333 (= A339), L361 (= L368), N362 (= N369), V406 (= V412), R587 (= R593), R590 (= R596)
7ocqB Nadh bound to the dehydrogenase domain of the bifunctional mannitol-1- phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
52% identity, 90% coverage: 1:637/707 of query aligns to 1:635/679 of 7ocqB
- binding magnesium ion: D15 (= D15), D17 (= D17), D170 (= D175)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G245 (= G250), F246 (= F251), G247 (= G252), A248 (= A253), I249 (= I254), T274 (= T279), R275 (= R280), C329 (≠ S334), L330 (= L335), A334 (= A339), N363 (= N369), V403 (= V408), R405 (= R410), V407 (= V412), R591 (= R593), R594 (= R596)
7ocsC Mannitol-1-phosphate bound to the phosphatase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase mtld-d16a from acinetobacter baumannii (see paper)
50% identity, 83% coverage: 1:584/707 of query aligns to 1:564/572 of 7ocsC
- binding D-Mannitol-1-phosphate: M16 (= M16), D17 (= D17), E24 (= E24), R27 (= R27), L31 (= L31), C51 (≠ S51), L52 (= L52), G53 (= G53), L54 (= L54), R77 (= R77), T117 (= T117), S118 (= S118), K150 (= K150)
P77247 Hexitol phosphatase B; 2-deoxyglucose-6-phosphate phosphatase; Mannitol-1-phosphatase; Sorbitol-6-phosphatase; Sugar-phosphatase; EC 3.1.3.68; EC 3.1.3.22; EC 3.1.3.50; EC 3.1.3.23 from Escherichia coli (strain K12) (see paper)
30% identity, 28% coverage: 7:202/707 of query aligns to 5:195/222 of P77247
- D13 (= D15) binding ; mutation to A: Loss of phosphatase activity.
- D15 (= D17) binding
- D173 (= D175) binding
1te2A Putative phosphatase ynic from escherichia coli k12
30% identity, 28% coverage: 7:202/707 of query aligns to 1:191/218 of 1te2A
- active site: D9 (= D15), D11 (= D17), S17 (≠ T23), D44 (≠ G50), S111 (≠ T117), A112 (≠ S118), K144 (= K150), E168 (= E174), D169 (= D175)
- binding calcium ion: D9 (= D15), D11 (= D17), D169 (= D175)
- binding 2-phosphoglycolic acid: D9 (= D15), M10 (= M16), D11 (= D17), G47 (= G53), S111 (≠ T117), A112 (≠ S118), K144 (= K150)
5olwA 5-fluorotryptophan labeled beta-phosphoglucomutase in an open conformation (see paper)
28% identity, 24% coverage: 9:180/707 of query aligns to 1:175/224 of 5olwA
- active site: D8 (= D15), L9 (≠ M16), D10 (= D17), T16 (= T23), K45 (≠ S44), S114 (≠ T117), A115 (≠ S118), K145 (= K150), E169 (= E174), D170 (= D175)
- binding calcium ion: D8 (= D15), D10 (= D17), P89 (vs. gap), V92 (≠ I95), E124 (≠ N130), N127 (= N132), E169 (= E174), D170 (= D175), S171 (= S176)
4c4sA Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
30% identity, 24% coverage: 9:180/707 of query aligns to 1:172/215 of 4c4sA
- active site: D8 (= D15), L9 (≠ M16), D10 (= D17), T16 (= T23), K45 (≠ S44), S111 (≠ T117), A112 (≠ S118), K142 (= K150), E166 (= E174), D167 (= D175)
- binding (1R)-1,5-anhydro-1-[(S)-fluoro(phosphono)methyl]-D-glucitol: D10 (= D17), H20 (≠ R27), W24 (≠ L31), L44 (= L43), G46 (vs. gap), V47 (vs. gap), R49 (vs. gap), S113 (= S119)
- binding magnesium ion: D8 (= D15), D10 (= D17), D167 (= D175)
- binding trifluoromagnesate: D8 (= D15), L9 (≠ M16), D10 (= D17), S111 (≠ T117), A112 (≠ S118), K142 (= K150)
Q8VZ10 Protein SUPPRESSOR OF QUENCHING 1, chloroplastic; EC 3.1.3.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
28% identity, 26% coverage: 8:194/707 of query aligns to 73:261/1055 of Q8VZ10
- D80 (= D15) mutation to N: Complete rescue in complementation test of the nonphotochemical quenching (NPQ) phenotype observed in disrupted plants.
Sites not aligning to the query:
- 431:434 CINC→SINS: No rescue in complementation test of the nonphotochemical quenching (NPQ) phenotype observed in disrupted plants.
- 859 E→K: In soq1-2; high light intensity-dependent and irreversible nonphotochemical quenching (NPQ) due to a decrease in chlorophyll excited-state lifetime.
P71447 Beta-phosphoglucomutase; Beta-PGM; EC 5.4.2.6 from Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) (see 3 papers)
28% identity, 24% coverage: 9:180/707 of query aligns to 1:175/221 of P71447
- D8 (= D15) modified: 4-aspartylphosphate; mutation to A: Inactive.; mutation to E: Inactive.
- D10 (= D17) mutation to A: Inactive.; mutation to E: Inactive.; mutation to N: Inactive.; mutation to S: Inactive.
- T16 (= T23) mutation to P: 500-fold reduction in the rate constant for Asp-8 phosphorylation by beta-G1,6bisP. 6,700-fold reduction in the apparent rate constant for cycling of the phosphorylated enzyme to convert beta-G1P to G6P. 13-fold increase in the estimated rate constant for phosphoryl transfer from the phospho-Asp8 to water.
- H20 (≠ R27) mutation to A: Impairs Asp-8 phosphorylation by beta-G1,6bisP and phosphoryl transfer from the phospho-Asp8 to the substrate beta-G1P.; mutation to N: 300-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.; mutation to Q: 8-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.
- K45 (≠ S44) mutation to A: 20'000-fold decrease in kcat/KM.
- G46 (vs. gap) mutation to A: 1'000'000-fold decrease in kcat/KM.; mutation to P: 100'000-fold decrease in kcat/KM.; mutation to V: 10'000-fold decrease in kcat/KM.
- R49 (vs. gap) mutation to K: 1'000'000-fold decrease in kcat/KM.
- S52 (≠ T47) mutation to A: Wild-type activity.
- K76 (≠ A80) mutation to A: 100-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.
- D170 (= D175) mutation to A: Impaired, but active with an increase in the affinity for G1P.
6h91A Phosphorylated beta-phosphoglucomutase from lactococcus lactis in an open conformer to 2.4 a
28% identity, 24% coverage: 9:180/707 of query aligns to 1:175/218 of 6h91A
4c4rA Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
28% identity, 24% coverage: 9:180/707 of query aligns to 1:175/218 of 4c4rA
- active site: D8 (= D15), L9 (≠ M16), D10 (= D17), T16 (= T23), K45 (≠ S44), S114 (≠ T117), A115 (≠ S118), K145 (= K150), E169 (= E174), D170 (= D175)
- binding magnesium ion: D8 (= D15), D10 (= D17), D170 (= D175)
- binding trifluoromagnesate: D8 (= D15), L9 (≠ M16), D10 (= D17), S114 (≠ T117), A115 (≠ S118), K145 (= K150)
- binding (1R)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: D10 (= D17), H20 (≠ R27), W24 (≠ L31), L44 (= L43), G46 (vs. gap), V47 (vs. gap), R49 (vs. gap), S52 (≠ T47), S116 (= S119), K117 (≠ R120)
3zi4A The structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and scandium tetrafluoride
28% identity, 24% coverage: 9:180/707 of query aligns to 1:175/218 of 3zi4A
- active site: D8 (= D15), L9 (≠ M16), D10 (= D17), T16 (= T23), K45 (≠ S44), S114 (≠ T117), A115 (≠ S118), K145 (= K150), E169 (= E174), D170 (= D175)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D17), H20 (≠ R27), G46 (vs. gap), V47 (vs. gap), R49 (vs. gap), S116 (= S119), K117 (≠ R120)
- binding magnesium ion: D8 (= D15), D10 (= D17), D170 (= D175)
- binding Scandium Tetrafluoride: D8 (= D15), L9 (≠ M16), D10 (= D17), S114 (≠ T117), A115 (≠ S118), K145 (= K150)
2wf8A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, glucose-1-phosphate and beryllium trifluoride (see paper)
28% identity, 24% coverage: 9:180/707 of query aligns to 1:175/218 of 2wf8A
- active site: D8 (= D15), L9 (≠ M16), D10 (= D17), T16 (= T23), K45 (≠ S44), S114 (≠ T117), A115 (≠ S118), K145 (= K150), E169 (= E174), D170 (= D175)
- binding beryllium trifluoride ion: D8 (= D15), L9 (≠ M16), D10 (= D17), S114 (≠ T117), A115 (≠ S118), K145 (= K150)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D17), H20 (≠ R27), G46 (vs. gap), V47 (vs. gap), R49 (vs. gap), A115 (≠ S118), S116 (= S119), K117 (≠ R120)
- binding 1-O-phosphono-alpha-D-glucopyranose: D10 (= D17), H20 (≠ R27), W24 (≠ L31), L44 (= L43), G46 (vs. gap), V47 (vs. gap), R49 (vs. gap), S52 (≠ T47), A115 (≠ S118), S116 (= S119), K117 (≠ R120)
- binding magnesium ion: D8 (= D15), D10 (= D17), D170 (= D175)
2wf7A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphonate and aluminium tetrafluoride (see paper)
28% identity, 24% coverage: 9:180/707 of query aligns to 1:175/218 of 2wf7A
- active site: D8 (= D15), L9 (≠ M16), D10 (= D17), T16 (= T23), K45 (≠ S44), S114 (≠ T117), A115 (≠ S118), K145 (= K150), E169 (= E174), D170 (= D175)
- binding tetrafluoroaluminate ion: D8 (= D15), L9 (≠ M16), D10 (= D17), S114 (≠ T117), K145 (= K150)
- binding 6,7-dideoxy-7-phosphono-beta-D-gluco-heptopyranose: D10 (= D17), G46 (vs. gap), V47 (vs. gap), R49 (vs. gap), S116 (= S119), K117 (≠ R120), N118 (≠ R121)
- binding magnesium ion: D8 (= D15), D10 (= D17), D170 (= D175)
2wf6A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and aluminium tetrafluoride (see paper)
28% identity, 24% coverage: 9:180/707 of query aligns to 1:175/218 of 2wf6A
- active site: D8 (= D15), L9 (≠ M16), D10 (= D17), T16 (= T23), K45 (≠ S44), S114 (≠ T117), A115 (≠ S118), K145 (= K150), E169 (= E174), D170 (= D175)
- binding tetrafluoroaluminate ion: D8 (= D15), L9 (≠ M16), D10 (= D17), S114 (≠ T117), K145 (= K150)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D17), G46 (vs. gap), V47 (vs. gap), R49 (vs. gap), S116 (= S119), K117 (≠ R120)
- binding magnesium ion: D8 (= D15), D10 (= D17), D170 (= D175)
2wf5A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and trifluoromagnesate (see paper)
28% identity, 24% coverage: 9:180/707 of query aligns to 1:175/218 of 2wf5A
- active site: D8 (= D15), L9 (≠ M16), D10 (= D17), T16 (= T23), K45 (≠ S44), S114 (≠ T117), A115 (≠ S118), K145 (= K150), E169 (= E174), D170 (= D175)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D17), H20 (≠ R27), G46 (vs. gap), V47 (vs. gap), R49 (vs. gap), A115 (≠ S118), S116 (= S119)
- binding magnesium ion: D8 (= D15), D10 (= D17), D170 (= D175)
- binding trifluoromagnesate: D8 (= D15), L9 (≠ M16), D10 (= D17), S114 (≠ T117), A115 (≠ S118), K145 (= K150)
Query Sequence
>PP_2052 FitnessBrowser__Putida:PP_2052
MLFFHGKQIFSAIFDMDGTLFDTERLRFRTLKQASLEIFGKALSEQTLIGSLGLSAKKAE
ALAKAHNGEDFPYAQIRQRADELELEYVRNHGVPIKAGLLEVLERLRKSGLTMAVATSSR
RAIAEEYLINANVLKYFDITVCGDEVGQGKPHPEIFLKAARALNCEPGQCFMVEDSENGM
LSAMRAEGQAILIEDIKPPAPEIKAGALKAYRSMHEFLADLSECVPDLGMPALSEPFPAS
MNQFSVGIHGFGAIGGGYLTQVFSHWDGYTRPREIIAATRSRMLRESVSAFGRYSVRYGA
TSFDQTIDNVRMIDMDDDDAVISMYTTAEIIGLSLPEQAIRSQARVIAQGLLQRFERRGR
ELTLLIVLNKVGGAAFVRRHVQAELSLLCPPAISEQVLQKTHFAETVVSRIVSKLGNDAL
VRQLRIKSQMFQNSLEDEPASTRKSSTPLPEYERLIGHFRPFAQPSSAMSQLHLVLFNSE
ADMPLYAERGSDLLERLRQVKTVPDIAQIQIIKNRLWNGPHAIVAWYASLLGHAWVGQGM
GDARVSELAERLIRQEVAPALVAEYPQMAEVVSRFAEAFLERCKTSFKDPCARVGRDPLR
KLQRNERILSSIDLARKHGIATPALAFGAGLAIHHALNCSNSKDLESQAIRQVYLDNQES
VEAVLTHANKPFPGLCPVKDAELIAAIREGFRQLPQPAPRHAVAVGS
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