SitesBLAST
Comparing WP_022528084.1 NCBI__GCF_000469325.1:WP_022528084.1 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)
Q8VZ10 Protein SUPPRESSOR OF QUENCHING 1, chloroplastic; EC 3.1.3.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
36% identity, 85% coverage: 2:185/216 of query aligns to 73:260/1055 of Q8VZ10
- D80 (= D9) 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.
7ocsC Mannitol-1-phosphate bound to the phosphatase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase mtld-d16a from acinetobacter baumannii (see paper)
28% identity, 86% coverage: 5:190/216 of query aligns to 11:198/572 of 7ocsC
- binding D-Mannitol-1-phosphate: M16 (= M10), D17 (= D11), E24 (= E18), R27 (≠ Y21), L31 (≠ N25), C51 (≠ L44), L52 (≠ A45), G53 (= G46), L54 (≠ A47), R77 (≠ Q66), T117 (≠ S109), S118 (= S110), K150 (= K142)
7ocqB Nadh bound to the dehydrogenase domain of the bifunctional mannitol-1- phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
29% identity, 88% coverage: 5:193/216 of query aligns to 11:196/679 of 7ocqB
Sites not aligning to the query:
- binding 1,4-dihydronicotinamide adenine dinucleotide: 245, 246, 247, 248, 249, 274, 275, 329, 330, 334, 363, 403, 405, 407, 591, 594
7ocnA Crystal structure of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
28% identity, 88% coverage: 5:193/216 of query aligns to 11:201/690 of 7ocnA
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)
28% identity, 88% coverage: 5:193/216 of query aligns to 11:195/675 of 7ocrB
Sites not aligning to the query:
- binding fructose -6-phosphate: 362, 403, 508, 513, 516, 587, 590, 594, 595, 601
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: 244, 246, 247, 248, 273, 274, 329, 330, 333, 361, 362, 406, 587, 590
7ocqA Nadh bound to the dehydrogenase domain of the bifunctional mannitol-1- phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
28% identity, 88% coverage: 5:193/216 of query aligns to 11:201/686 of 7ocqA
Sites not aligning to the query:
- 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: 252, 253, 254, 279, 280, 335, 369, 370
7ocpA NADPH bound to the dehydrogenase domain of the bifunctional mannitol- 1-phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
28% identity, 88% coverage: 5:193/216 of query aligns to 11:201/688 of 7ocpA
Sites not aligning to the query:
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: 250, 251, 253, 254, 279, 280, 334, 335, 336, 339, 369, 370
4c4sA Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
34% identity, 85% coverage: 3:185/216 of query aligns to 2:185/215 of 4c4sA
- active site: D8 (= D9), L9 (≠ M10), D10 (= D11), T16 (≠ S17), K45 (≠ A45), S111 (= S109), A112 (vs. gap), K142 (= K142), E166 (= E166), D167 (= D167)
- binding (1R)-1,5-anhydro-1-[(S)-fluoro(phosphono)methyl]-D-glucitol: D10 (= D11), H20 (≠ Y21), W24 (≠ N25), L44 (= L44), G46 (= G46), V47 (≠ A47), R49 (≠ N49), S113 (= S110)
- binding magnesium ion: D8 (= D9), D10 (= D11), D167 (= D167)
- binding trifluoromagnesate: D8 (= D9), L9 (≠ M10), D10 (= D11), S111 (= S109), A112 (vs. gap), K142 (= K142)
2wf9A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, and beryllium trifluoride, crystal form 2 (see paper)
34% identity, 85% coverage: 3:185/216 of query aligns to 2:188/221 of 2wf9A
- active site: D8 (= D9), L9 (≠ M10), D10 (= D11), T16 (≠ S17), K45 (≠ A45), S114 (= S109), A115 (vs. gap), K145 (= K142), E169 (= E166), D170 (= D167)
- binding beryllium trifluoride ion: D8 (= D9), L9 (≠ M10), D10 (= D11), S114 (= S109), A115 (vs. gap), K145 (= K142)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D11), H20 (≠ Y21), G46 (= G46), V47 (≠ A47), R49 (≠ N49), S116 (= S110), K117 (≠ N111), N118 (≠ Y112)
- binding 6-O-phosphono-alpha-D-glucopyranose: D10 (= D11), H20 (≠ Y21), G46 (= G46), V47 (≠ A47), R49 (≠ N49), A115 (vs. gap), S116 (= S110), K117 (≠ N111), N118 (≠ Y112)
- binding magnesium ion: D8 (= D9), D10 (= D11), D170 (= D167)
1o03A Structure of pentavalent phosphorous intermediate of an enzyme catalyzed phosphoryl transfer reaction observed on cocrystallization with glucose 6-phosphate (see paper)
34% identity, 85% coverage: 3:185/216 of query aligns to 2:188/221 of 1o03A
- active site: D8 (= D9), L9 (≠ M10), D10 (= D11), T16 (≠ S17), K45 (≠ A45), S114 (= S109), A115 (vs. gap), K145 (= K142), E169 (= E166), D170 (= D167)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: D8 (= D9), L9 (≠ M10), D10 (= D11), H20 (≠ Y21), G46 (= G46), V47 (≠ A47), R49 (≠ N49), S114 (= S109), A115 (vs. gap), S116 (= S110), K117 (≠ N111), K145 (= K142)
- binding magnesium ion: D8 (= D9), D10 (= D11), D170 (= D167)
1lvhA The structure of phosphorylated beta-phosphoglucomutase from lactoccocus lactis to 2.3 angstrom resolution (see paper)
34% identity, 85% coverage: 3:185/216 of query aligns to 2:188/221 of 1lvhA
- active site: D8 (= D9), L9 (≠ M10), D10 (= D11), T16 (≠ S17), K45 (≠ A45), S114 (= S109), A115 (vs. gap), K145 (= K142), E169 (= E166), D170 (= D167)
- binding magnesium ion: D8 (= D9), D10 (= D11), D170 (= D167)
6h91A Phosphorylated beta-phosphoglucomutase from lactococcus lactis in an open conformer to 2.4 a
34% identity, 85% coverage: 3:185/216 of query aligns to 2:188/218 of 6h91A
4c4rA Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
34% identity, 85% coverage: 3:185/216 of query aligns to 2:188/218 of 4c4rA
- active site: D8 (= D9), L9 (≠ M10), D10 (= D11), T16 (≠ S17), K45 (≠ A45), S114 (= S109), A115 (vs. gap), K145 (= K142), E169 (= E166), D170 (= D167)
- binding magnesium ion: D8 (= D9), D10 (= D11), D170 (= D167)
- binding trifluoromagnesate: D8 (= D9), L9 (≠ M10), D10 (= D11), S114 (= S109), A115 (vs. gap), K145 (= K142)
- binding (1R)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: D10 (= D11), H20 (≠ Y21), W24 (≠ N25), L44 (= L44), G46 (= G46), V47 (≠ A47), R49 (≠ N49), S52 (≠ A52), S116 (= S110), K117 (≠ N111)
3zi4A The structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and scandium tetrafluoride (see paper)
34% identity, 85% coverage: 3:185/216 of query aligns to 2:188/218 of 3zi4A
- active site: D8 (= D9), L9 (≠ M10), D10 (= D11), T16 (≠ S17), K45 (≠ A45), S114 (= S109), A115 (vs. gap), K145 (= K142), E169 (= E166), D170 (= D167)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D11), H20 (≠ Y21), G46 (= G46), V47 (≠ A47), R49 (≠ N49), S116 (= S110), K117 (≠ N111)
- binding magnesium ion: D8 (= D9), D10 (= D11), D170 (= D167)
- binding Scandium Tetrafluoride: D8 (= D9), L9 (≠ M10), D10 (= D11), S114 (= S109), A115 (vs. gap), K145 (= K142)
2wf8A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, glucose-1-phosphate and beryllium trifluoride (see paper)
34% identity, 85% coverage: 3:185/216 of query aligns to 2:188/218 of 2wf8A
- active site: D8 (= D9), L9 (≠ M10), D10 (= D11), T16 (≠ S17), K45 (≠ A45), S114 (= S109), A115 (vs. gap), K145 (= K142), E169 (= E166), D170 (= D167)
- binding beryllium trifluoride ion: D8 (= D9), L9 (≠ M10), D10 (= D11), S114 (= S109), A115 (vs. gap), K145 (= K142)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D11), H20 (≠ Y21), G46 (= G46), V47 (≠ A47), R49 (≠ N49), A115 (vs. gap), S116 (= S110), K117 (≠ N111)
- binding 1-O-phosphono-alpha-D-glucopyranose: D10 (= D11), H20 (≠ Y21), W24 (≠ N25), L44 (= L44), G46 (= G46), V47 (≠ A47), R49 (≠ N49), S52 (≠ A52), A115 (vs. gap), S116 (= S110), K117 (≠ N111)
- binding magnesium ion: D8 (= D9), D10 (= D11), D170 (= D167)
2wf7A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphonate and aluminium tetrafluoride (see paper)
34% identity, 85% coverage: 3:185/216 of query aligns to 2:188/218 of 2wf7A
- active site: D8 (= D9), L9 (≠ M10), D10 (= D11), T16 (≠ S17), K45 (≠ A45), S114 (= S109), A115 (vs. gap), K145 (= K142), E169 (= E166), D170 (= D167)
- binding tetrafluoroaluminate ion: D8 (= D9), L9 (≠ M10), D10 (= D11), S114 (= S109), K145 (= K142)
- binding 6,7-dideoxy-7-phosphono-beta-D-gluco-heptopyranose: D10 (= D11), G46 (= G46), V47 (≠ A47), R49 (≠ N49), S116 (= S110), K117 (≠ N111), N118 (≠ Y112)
- binding magnesium ion: D8 (= D9), D10 (= D11), D170 (= D167)
2wf6A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and aluminium tetrafluoride (see paper)
34% identity, 85% coverage: 3:185/216 of query aligns to 2:188/218 of 2wf6A
- active site: D8 (= D9), L9 (≠ M10), D10 (= D11), T16 (≠ S17), K45 (≠ A45), S114 (= S109), A115 (vs. gap), K145 (= K142), E169 (= E166), D170 (= D167)
- binding tetrafluoroaluminate ion: D8 (= D9), L9 (≠ M10), D10 (= D11), S114 (= S109), K145 (= K142)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D11), G46 (= G46), V47 (≠ A47), R49 (≠ N49), S116 (= S110), K117 (≠ N111)
- binding magnesium ion: D8 (= D9), D10 (= D11), D170 (= D167)
2wf5A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and trifluoromagnesate (see paper)
34% identity, 85% coverage: 3:185/216 of query aligns to 2:188/218 of 2wf5A
- active site: D8 (= D9), L9 (≠ M10), D10 (= D11), T16 (≠ S17), K45 (≠ A45), S114 (= S109), A115 (vs. gap), K145 (= K142), E169 (= E166), D170 (= D167)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D11), H20 (≠ Y21), G46 (= G46), V47 (≠ A47), R49 (≠ N49), A115 (vs. gap), S116 (= S110)
- binding magnesium ion: D8 (= D9), D10 (= D11), D170 (= D167)
- binding trifluoromagnesate: D8 (= D9), L9 (≠ M10), D10 (= D11), S114 (= S109), A115 (vs. gap), K145 (= K142)
6qzgA Beta-glucose 1,6-bisphosphonate bound to wild type beta- phosphoglucomutse in an open conformation.
34% identity, 85% coverage: 3:185/216 of query aligns to 2:188/219 of 6qzgA
- binding 3,7-anhydro-1,2,8-trideoxy-1,8-diphosphono-D-glycero-D-gulo-octitol: D8 (= D9), L9 (≠ M10), D10 (= D11), H20 (≠ Y21), G46 (= G46), S114 (= S109), A115 (vs. gap), S116 (= S110), K117 (≠ N111), K145 (= K142)
- binding magnesium ion: D8 (= D9), D10 (= D11), D170 (= D167)
1z4nA Structure of beta-phosphoglucomutase with inhibitor bound alpha- galactose 1-phosphate cocrystallized with fluoride (see paper)
34% identity, 85% coverage: 3:185/216 of query aligns to 2:188/219 of 1z4nA
- active site: D8 (= D9), L9 (≠ M10), D10 (= D11), T16 (≠ S17), K45 (≠ A45), S114 (= S109), A115 (vs. gap), K145 (= K142), E169 (= E166), D170 (= D167)
- binding 1-O-phosphono-alpha-D-galactopyranose: H20 (≠ Y21), W24 (≠ N25), V47 (≠ A47), R49 (≠ N49), S116 (= S110), K117 (≠ N111), N118 (≠ Y112)
- binding magnesium ion: D8 (= D9), D10 (= D11), E169 (= E166), D170 (= D167)
Query Sequence
>WP_022528084.1 NCBI__GCF_000469325.1:WP_022528084.1
MKFDGVIFDMDGVLVDSERMYLRANLAAGQAQGLTLTAADYAPLAGAANADAKIFFQKYF
PGEKAQEFLDDTYALVDQYVAAGDLKIKPGVKTLLTTLHQKGIPLAVGSSNYGRTVNEFL
TAVGIKDAFDHIITSDDVAAGKPAPDIFLAAAHALHIAPARALVVEDSANGVQAALNARM
TPVLVPDLRSAEEILTPIPQPVLVAPRITHIAHLFD
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