SitesBLAST
Comparing WP_089300103.1 NCBI__GCF_900188115.1:WP_089300103.1 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)
4ygrA Crystal structure of had phosphatase from thermococcus onnurineus (see paper)
45% identity, 44% coverage: 95:198/234 of query aligns to 87:189/215 of 4ygrA
Sites not aligning to the query:
4knvA The crystal structure of apo human hdhd4 from se-mad (see paper)
27% identity, 94% coverage: 1:221/234 of query aligns to 1:232/241 of 4knvA
3vayA Crystal structure of 2-haloacid dehalogenase from pseudomonas syringae pv. Tomato dc3000 (see paper)
32% identity, 94% coverage: 1:221/234 of query aligns to 2:226/230 of 3vayA
3qnmA Haloalkane dehalogenase family member from bacteroides thetaiotaomicron of unknown function
26% identity, 83% coverage: 2:195/234 of query aligns to 4:205/231 of 3qnmA
8bp1A Crystal structure of bhmehis1.0, an engineered enzyme for the morita- baylis-hillman reaction (see paper)
29% identity, 57% coverage: 88:221/234 of query aligns to 94:226/231 of 8bp1A
Sites not aligning to the query:
6q7oA Crystal structure of oe1 (see paper)
28% identity, 57% coverage: 88:221/234 of query aligns to 94:226/230 of 6q7oA
Sites not aligning to the query:
6q7nA Crystal structure of bh32 alkylated with the mechanistic inhibitor 2- bromoacetophenone (see paper)
28% identity, 57% coverage: 88:221/234 of query aligns to 94:226/230 of 6q7nA
Sites not aligning to the query:
Q51645 (S)-2-haloacid dehalogenase 4A; 2-haloalkanoic acid dehalogenase IVA; Halocarboxylic acid halidohydrolase IVA; L-2-haloacid dehalogenase IVA; EC 3.8.1.2 from Burkholderia cepacia (Pseudomonas cepacia) (see 2 papers)
28% identity, 57% coverage: 96:229/234 of query aligns to 98:231/231 of Q51645
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 11 active site, Nucleophile
- 12:13 binding
- 42 binding
2no5B Crystal structure analysis of a dehalogenase with intermediate complex (see paper)
31% identity, 44% coverage: 96:199/234 of query aligns to 98:200/226 of 2no5B
Sites not aligning to the query:
4c4sA Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
27% identity, 75% coverage: 1:175/234 of query aligns to 2:167/215 of 4c4sA
- active site: D8 (= D7), L9 (≠ I8), D10 (= D9), T16 (≠ F15), K45 (≠ M57), S111 (≠ V116), A112 (≠ T117), K142 (= K150), E166 (≠ G174), D167 (= D175)
- binding (1R)-1,5-anhydro-1-[(S)-fluoro(phosphono)methyl]-D-glucitol: D10 (= D9), H20 (≠ G19), W24 (= W36), L44 (≠ S56), G46 (≠ H58), V47 (≠ R59), R49 (= R61), S113 (≠ N118)
- binding magnesium ion: D8 (= D7), D10 (= D9), D167 (= D175)
- binding trifluoromagnesate: D8 (= D7), L9 (≠ I8), D10 (= D9), S111 (≠ V116), A112 (≠ T117), K142 (= K150)
P71447 Beta-phosphoglucomutase; Beta-PGM; EC 5.4.2.6 from Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) (see 3 papers)
28% identity, 75% coverage: 1:175/234 of query aligns to 2:170/221 of P71447
- D8 (= D7) modified: 4-aspartylphosphate; mutation to A: Inactive.; mutation to E: Inactive.
- D10 (= D9) mutation to A: Inactive.; mutation to E: Inactive.; mutation to N: Inactive.; mutation to S: Inactive.
- T16 (≠ F15) 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 (≠ G19) 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 (≠ D53) mutation to A: 20'000-fold decrease in kcat/KM.
- G46 (≠ Y54) 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 (≠ M57) mutation to K: 1'000'000-fold decrease in kcat/KM.
- S52 (≠ Q60) mutation to A: Wild-type activity.
- K76 (≠ R85) 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.
2wf9A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, and beryllium trifluoride, crystal form 2 (see paper)
28% identity, 75% coverage: 1:175/234 of query aligns to 2:170/221 of 2wf9A
- active site: D8 (= D7), L9 (≠ I8), D10 (= D9), T16 (≠ F15), K45 (≠ D53), S114 (≠ V116), A115 (≠ T117), K145 (= K150), E169 (≠ G174), D170 (= D175)
- binding beryllium trifluoride ion: D8 (= D7), L9 (≠ I8), D10 (= D9), S114 (≠ V116), A115 (≠ T117), K145 (= K150)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D9), H20 (≠ G19), G46 (≠ Y54), V47 (≠ A55), R49 (≠ M57), S116 (≠ N118), K117 (≠ A119), N118 (≠ S120)
- binding 6-O-phosphono-alpha-D-glucopyranose: D10 (= D9), H20 (≠ G19), G46 (≠ Y54), V47 (≠ A55), R49 (≠ M57), A115 (≠ T117), S116 (≠ N118), K117 (≠ A119), N118 (≠ S120)
- binding magnesium ion: D8 (= D7), D10 (= D9), D170 (= D175)
1o03A Structure of pentavalent phosphorous intermediate of an enzyme catalyzed phosphoryl transfer reaction observed on cocrystallization with glucose 6-phosphate (see paper)
28% identity, 75% coverage: 1:175/234 of query aligns to 2:170/221 of 1o03A
- active site: D8 (= D7), L9 (≠ I8), D10 (= D9), T16 (≠ F15), K45 (≠ D53), S114 (≠ V116), A115 (≠ T117), K145 (= K150), E169 (≠ G174), D170 (= D175)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: D8 (= D7), L9 (≠ I8), D10 (= D9), H20 (≠ G19), G46 (≠ Y54), V47 (≠ A55), R49 (≠ M57), S114 (≠ V116), A115 (≠ T117), S116 (≠ N118), K117 (≠ A119), K145 (= K150)
- binding magnesium ion: D8 (= D7), D10 (= D9), D170 (= D175)
1lvhA The structure of phosphorylated beta-phosphoglucomutase from lactoccocus lactis to 2.3 angstrom resolution (see paper)
28% identity, 75% coverage: 1:175/234 of query aligns to 2:170/221 of 1lvhA
- active site: D8 (= D7), L9 (≠ I8), D10 (= D9), T16 (≠ F15), K45 (≠ D53), S114 (≠ V116), A115 (≠ T117), K145 (= K150), E169 (≠ G174), D170 (= D175)
- binding magnesium ion: D8 (= D7), D10 (= D9), D170 (= D175)
6h91A Phosphorylated beta-phosphoglucomutase from lactococcus lactis in an open conformer to 2.4 a
28% identity, 75% coverage: 1:175/234 of query aligns to 2:170/218 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, 75% coverage: 1:175/234 of query aligns to 2:170/218 of 4c4rA
- active site: D8 (= D7), L9 (≠ I8), D10 (= D9), T16 (≠ F15), K45 (≠ D53), S114 (≠ V116), A115 (≠ T117), K145 (= K150), E169 (≠ G174), D170 (= D175)
- binding magnesium ion: D8 (= D7), D10 (= D9), D170 (= D175)
- binding trifluoromagnesate: D8 (= D7), L9 (≠ I8), D10 (= D9), S114 (≠ V116), A115 (≠ T117), K145 (= K150)
- binding (1R)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: D10 (= D9), H20 (≠ G19), W24 (≠ L23), L44 (= L52), G46 (≠ Y54), V47 (≠ A55), R49 (≠ M57), S52 (≠ Q60), S116 (≠ N118), K117 (≠ A119)
3zi4A The structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and scandium tetrafluoride
28% identity, 75% coverage: 1:175/234 of query aligns to 2:170/218 of 3zi4A
- active site: D8 (= D7), L9 (≠ I8), D10 (= D9), T16 (≠ F15), K45 (≠ D53), S114 (≠ V116), A115 (≠ T117), K145 (= K150), E169 (≠ G174), D170 (= D175)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D9), H20 (≠ G19), G46 (≠ Y54), V47 (≠ A55), R49 (≠ M57), S116 (≠ N118), K117 (≠ A119)
- binding magnesium ion: D8 (= D7), D10 (= D9), D170 (= D175)
- binding Scandium Tetrafluoride: D8 (= D7), L9 (≠ I8), D10 (= D9), S114 (≠ V116), A115 (≠ T117), K145 (= K150)
2wf8A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, glucose-1-phosphate and beryllium trifluoride (see paper)
28% identity, 75% coverage: 1:175/234 of query aligns to 2:170/218 of 2wf8A
- active site: D8 (= D7), L9 (≠ I8), D10 (= D9), T16 (≠ F15), K45 (≠ D53), S114 (≠ V116), A115 (≠ T117), K145 (= K150), E169 (≠ G174), D170 (= D175)
- binding beryllium trifluoride ion: D8 (= D7), L9 (≠ I8), D10 (= D9), S114 (≠ V116), A115 (≠ T117), K145 (= K150)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D9), H20 (≠ G19), G46 (≠ Y54), V47 (≠ A55), R49 (≠ M57), A115 (≠ T117), S116 (≠ N118), K117 (≠ A119)
- binding 1-O-phosphono-alpha-D-glucopyranose: D10 (= D9), H20 (≠ G19), W24 (≠ L23), L44 (= L52), G46 (≠ Y54), V47 (≠ A55), R49 (≠ M57), S52 (≠ Q60), A115 (≠ T117), S116 (≠ N118), K117 (≠ A119)
- binding magnesium ion: D8 (= D7), D10 (= D9), D170 (= D175)
2wf7A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphonate and aluminium tetrafluoride (see paper)
28% identity, 75% coverage: 1:175/234 of query aligns to 2:170/218 of 2wf7A
- active site: D8 (= D7), L9 (≠ I8), D10 (= D9), T16 (≠ F15), K45 (≠ D53), S114 (≠ V116), A115 (≠ T117), K145 (= K150), E169 (≠ G174), D170 (= D175)
- binding tetrafluoroaluminate ion: D8 (= D7), L9 (≠ I8), D10 (= D9), S114 (≠ V116), K145 (= K150)
- binding 6,7-dideoxy-7-phosphono-beta-D-gluco-heptopyranose: D10 (= D9), G46 (≠ Y54), V47 (≠ A55), R49 (≠ M57), S116 (≠ N118), K117 (≠ A119), N118 (≠ S120)
- binding magnesium ion: D8 (= D7), D10 (= D9), D170 (= D175)
2wf6A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and aluminium tetrafluoride (see paper)
28% identity, 75% coverage: 1:175/234 of query aligns to 2:170/218 of 2wf6A
- active site: D8 (= D7), L9 (≠ I8), D10 (= D9), T16 (≠ F15), K45 (≠ D53), S114 (≠ V116), A115 (≠ T117), K145 (= K150), E169 (≠ G174), D170 (= D175)
- binding tetrafluoroaluminate ion: D8 (= D7), L9 (≠ I8), D10 (= D9), S114 (≠ V116), K145 (= K150)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D9), G46 (≠ Y54), V47 (≠ A55), R49 (≠ M57), S116 (≠ N118), K117 (≠ A119)
- binding magnesium ion: D8 (= D7), D10 (= D9), D170 (= D175)
Query Sequence
>WP_089300103.1 NCBI__GCF_900188115.1:WP_089300103.1
MRAVCLDIDDTLVDFSAAGRRALAAMIGRDDMWPVWERLTELHVARVVADRLDYASMHRQ
RTKSFLDELGVAVSDEDAARFERRRAALVQCHWDVYGDVLPCLEWLRAAGIALAAVTNAS
GAHQRKKLDTLGLSRYFGHVAIAGEVGAAKPDPLIFHSACAALGCDPAEAVHVGDKLEAD
AAGAVRAGLGGVWLDRHGRCESDRDTDVQVISGLDELPSVLVADLGRAGVPVPR
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